ID 5HT1A_FUGRU STANDARD; PRT; 423 AA. AC O42385; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 07-MAR-2006, entry version 39. DE 5-hydroxytryptamine 1A-alpha receptor (5-HT-1A-alpha) (Serotonin DE receptor 1A-alpha) (5-HT1A-alpha) (F1A). OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4; RA Yamaguchi F., Brenner S.; RT "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes RT from the Japanese puffer fish, Fugu rubripes."; RL Gene 191:219-223(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X95936; CAA65175.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR Ensembl; SINFRUG00000145569; Fugu rubripes. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PANTHER; PTHR19266:SF103; 5HT1A_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 423 5-hydroxytryptamine 1A-alpha receptor. FT /FTId=PRO_0000068909. FT TOPO_DOM 1 45 Extracellular (Potential). FT TRANSMEM 46 71 1 (Potential). FT TOPO_DOM 72 82 Cytoplasmic (Potential). FT TRANSMEM 83 107 2 (Potential). FT TOPO_DOM 108 118 Extracellular (Potential). FT TRANSMEM 119 141 3 (Potential). FT TOPO_DOM 142 161 Cytoplasmic (Potential). FT TRANSMEM 162 186 4 (Potential). FT TOPO_DOM 187 200 Extracellular (Potential). FT TRANSMEM 201 226 5 (Potential). FT TOPO_DOM 227 346 Cytoplasmic (Potential). FT TRANSMEM 347 368 6 (Potential). FT TOPO_DOM 369 379 Extracellular (Potential). FT TRANSMEM 380 404 7 (Potential). FT TOPO_DOM 405 423 Cytoplasmic (Potential). FT CARBOHYD 9 9 N-linked (GlcNAc...) (Potential). FT CARBOHYD 12 12 N-linked (GlcNAc...) (Potential). FT CARBOHYD 30 30 N-linked (GlcNAc...) (Potential). FT DISULFID 118 196 By similarity. SQ SEQUENCE 423 AA; 47001 MW; 7B1308626B40190F CRC64; MDLRATSSND SNATSGYSDT AAVDWDEGEN ATGSGSLPDP ELSYQIITSL FLGALILCSI FGNSCVVAAI ALERSLQNVA NYLIGSLAVT DLMVSVLVLP MAALYQVLNK WTLGQDICDL FIALDVLCCT SSILHLCAIA LDRYWAITDP IDYVNKRTPR RAAVLISVTW LIGFSISIPP MLGWRSAEDR ANPDACIISQ DPGYTIYSTF GAFYIPLILM LVLYGRIFKA ARFRIRKTVK KTEKAKASDM CLTLSPAVFH KRANGDAVSA EWKRGYKFKP SSPCANGAVR HGEEMESLEI IEVNSNSKTH LPLPNTPQSS SHENINEKTT GTRRKIALAR ERKTVKTLGI IMGTFIFCWL PFFIVALVLP FCAENCYMPE WLGAVINWLG YSNSLLNPII YAYFNKDFQS AFKKILRCKF HRH // ID 5HT1A_CANFA STANDARD; PRT; 423 AA. AC Q6XXX9; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-MAY-2006, entry version 19. DE 5-hydroxytryptamine 1A receptor (5-HT-1A) (Serotonin receptor 1A) (5- DE HT1A). GN Name=HTR1A; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15220384; DOI=10.1093/jhered/esh033; RA Kukekova A.V., Trut L.N., Oskina I.N., Kharlamova A.V., RA Shikhevich S.G., Kirkness E.F., Aguirre G.D., Acland G.M.; RT "A marker set for construction of a genetic map of the silver fox RT (Vulpes vulpes)."; RL J. Hered. 95:185-194(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY204570; AAP12467.1; -; Genomic_DNA. DR UniGene; Cfa.23472; -. DR Ensembl; ENSCAFG00000007276; Canis familiaris. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PANTHER; PTHR19266:SF103; 5HT1A_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 423 5-hydroxytryptamine 1A receptor. FT /FTId=PRO_0000068901. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 62 1 (Potential). FT TOPO_DOM 63 73 Cytoplasmic (Potential). FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 178 4 (Potential). FT TOPO_DOM 179 191 Extracellular (Potential). FT TRANSMEM 192 217 5 (Potential). FT TOPO_DOM 218 345 Cytoplasmic (Potential). FT TRANSMEM 346 367 6 (Potential). FT TOPO_DOM 368 378 Extracellular (Potential). FT TRANSMEM 379 403 7 (Potential). FT TOPO_DOM 404 423 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. SQ SEQUENCE 423 AA; 46356 MW; 0E397FD4AE673269 CRC64; MEGLSPRQGN NTTSSEGPFG TLGNATGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKAERKGADA RSGVSPAPQP RKSVNGEPGG REWRQGPGSQ AGGPLCTNGA VRRGDDGAAL EVIEVHRVGS SKEHLPLPCE AGAIPCAPAS FEKKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIVRCKFC RRR // ID 5HT1D_FUGRU STANDARD; PRT; 379 AA. AC P79748; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 07-MAR-2006, entry version 37. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D) DE (5HT1D) (F1D). OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4; RA Yamaguchi F., Brenner S.; RT "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes RT from the Japanese puffer fish, Fugu rubripes."; RL Gene 191:219-223(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X83865; CAA58745.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR Ensembl; SINFRUG00000120815; Fugu rubripes. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PANTHER; PTHR19266:SF128; 5HT1D_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 379 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068932. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 60 1 (Potential). FT TOPO_DOM 61 73 Cytoplasmic (Potential). FT TRANSMEM 74 96 2 (Potential). FT TOPO_DOM 97 106 Extracellular (Potential). FT TRANSMEM 107 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 174 4 (Potential). FT TOPO_DOM 175 192 Extracellular (Potential). FT TRANSMEM 193 216 5 (Potential). FT TOPO_DOM 217 307 Cytoplasmic (Potential). FT TRANSMEM 308 331 6 (Potential). FT TOPO_DOM 332 339 Extracellular (Potential). FT TRANSMEM 340 364 7 (Potential). FT TOPO_DOM 365 379 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 109 186 By similarity. SQ SEQUENCE 379 AA; 42302 MW; 99B6E2C0379EBC78 CRC64; MELDNNSLDY FSSNFTDIPS NTTVAHWTEA TLLGLQISVS VVLAIVTLAT MLSNAFVIAT IFLTRKLHTP ANFLIGSLAV TDMLVSILVM PISIVYTVSK TWSLGQIVCD IWLSSDITFC TASILHLCVI ALDRYWAITD ALEYSKRRTM RRAAVMVAVV WVISISISMP PLFWRQAKAH EELKECMVNT DQISYTLYST FGAFYVPTVL LIILYGRIYV AARSRIFKTP SYSGKRFTTA QLIQTSAGSS LCSLNSASNQ EAHLHSGAGG EGGGSPLFVN SVKVKLADNV LERKRLCAAR ERKATKTLGI ILGAFIICWL PFFVVTLVWA ICKECSFDPL LFDVFTWLGY LNSLINPVIY TVFNDEFKQA FQKLIKFRR // ID 5HT1F_CAVPO STANDARD; PRT; 366 AA. AC O08890; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 07-MAR-2006, entry version 35. DE 5-hydroxytryptamine 1F receptor (5-HT-1F) (Serotonin receptor 1F) (5- DE HT1F). GN Name=HTR1F; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=97368668; PubMed=9225282; DOI=10.1016/S0028-3908(97)00020-8; RA Adham N., Bard J.A., Zgombick J.M., Durkin M.M., Kucharewicz S., RA Weinshank R.L., Branchek T.A.; RT "Cloning and characterization of the guinea pig 5-HT1F receptor RT subtype: a comparison of the pharmacological profile to the human RT species homolog."; RL Neuropharmacology 36:569-576(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U80852; AAB58496.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR000450; 5HT1F_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00515; 5HT1FRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 366 5-hydroxytryptamine 1F receptor. FT /FTId=PRO_0000068936. FT TOPO_DOM 1 23 Extracellular (Potential). FT TRANSMEM 24 48 1 (Potential). FT TOPO_DOM 49 60 Cytoplasmic (Potential). FT TRANSMEM 61 83 2 (Potential). FT TOPO_DOM 84 94 Extracellular (Potential). FT TRANSMEM 95 119 3 (Potential). FT TOPO_DOM 120 139 Cytoplasmic (Potential). FT TRANSMEM 140 161 4 (Potential). FT TOPO_DOM 162 178 Extracellular (Potential). FT TRANSMEM 179 202 5 (Potential). FT TOPO_DOM 203 291 Cytoplasmic (Potential). FT TRANSMEM 292 314 6 (Potential). FT TOPO_DOM 315 327 Extracellular (Potential). FT TRANSMEM 328 351 7 (Potential). FT TOPO_DOM 352 366 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT DISULFID 96 172 By similarity. SQ SEQUENCE 366 AA; 41839 MW; FE4200E2DA26C9C3 CRC64; MDFLNSSDQN LTSEELLHRM PSKILVSLTL SGLALMTTTI NSLVIAAIIV TRKLHHPANY LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQVLCDIWL SVDIICCTCS ILHLSAIALD RYRAITDAVE YARKRTPKQA GIMITIVWII SVFISMPPLF WRHQGTSRDD ECIIKHDHIV STIYSTFGAF YIPLVLILIL YYKIYKAAKT LYHKRQASRI AKEELNGQVL LESGEKSIKM VSTTYVPEKS LSDPSTDFDK IHNTVKSPRC KLRHEKSWRR QKISGTRERK AATTLGLILG AFVICWLPFF VKELVVNVCE KCKISEEMAN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK LVRCQY // ID 5HT2A_DROME STANDARD; PRT; 834 AA. AC P28285; Q5MTE9; Q5MTF1; Q5MTF2; Q5MTF3; Q5MTF8; Q5MTF9; Q5MTG0; AC Q5MTG1; Q5MTG2; Q5MTG3; Q5MTG4; Q5MTG6; Q5MTG9; Q5MTH1; Q5MTH2; AC Q5MTH5; Q5MTH6; Q5MTH7; Q5MTH9; Q5MTI0; Q5MTI1; Q5MTI4; Q5MTI6; AC Q5MTI7; Q5MTI8; Q5MTJ0; Q5MTJ4; Q5MTJ5; Q5MTJ6; Q5MTJ9; Q5MTK5; AC Q5MTL1; Q5MTL5; Q5MTL6; Q5MTM2; Q5MTM5; Q5MTM8; Q5MTN6; Q5MTQ1; AC Q5MTR1; Q5MTR3; Q5MTR6; Q5MTR8; Q5MTS1; Q5MTT8; Q5MTV6; Q5MTV7; AC Q5MTV9; Q5MTW8; Q5MTX2; Q5MTX7; Q5MTY3; Q5MTY7; Q5MTY8; Q5MTY9; AC Q5MTZ0; Q5MTZ6; Q5MUJ0; Q5MUK2; Q5MUK5; Q5MUK8; Q5MUL0; Q5MUL2; AC Q5MUL5; Q5MUM3; Q5MUM7; Q5MUM9; Q5MUN0; Q5MUN1; Q5MUN2; Q5MUP0; AC Q5MUP5; Q5MUP6; Q5MUP7; Q5MUP8; Q5MUQ1; Q5MUQ6; Q5MUQ7; Q5MUQ8; AC Q5MUQ9; Q5MUR1; Q5MUR2; Q5MUR3; Q5MUR4; Q5MUR5; Q5MUT3; Q5MUT4; AC Q5MUT7; Q5MUT9; Q5MUU2; Q5MUU5; Q5MUU6; Q5MUV4; Q5MUV5; Q5MUV8; AC Q5MUV9; Q5MUW3; Q5MUW4; Q5MUW7; Q5MUX4; Q5MUX6; Q5MUY1; Q5MUY3; AC Q5MV05; Q5MV06; Q5MV07; Q5MV08; Q5MV13; Q5MV14; Q5MV15; Q5MV26; AC Q5MV30; Q9V8Q9; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 04-APR-2006, entry version 46. DE 5-hydroxytryptamine receptor 2A (5-HT receptor) (Serotonin receptor DE 2A). GN Name=5-HT1A; Synonyms=5HT-R2A; ORFNames=CG16720; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Canton-S, and Oregon-R; TISSUE=Head; RX MEDLINE=92155185; PubMed=1310937; RA Saudou F., Boschert U., Amlaiky N., Plassat J.-L., Hen R.; RT "A family of Drosophila serotonin receptors with distinct RT intracellular signalling properties and expression patterns."; RL EMBO J. 11:7-17(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242, AND NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 511-834. RC STRAIN=CA-001, CA-002, CA-003, CA-008, CA-009, CA-010, CA-011, CA-012, RC CA-013, CA-015, CA-017, CA-018, CA-023, CA-026, CA-027, CA-030, RC CA-031, CA-033, CA-034, CA-035, CA-037, CA-040, CA-041, CA-043, RC CA-044, CA-045, CA-046, CA-047, CA-048, CA-052, CA-055, CA-056, RC CA-057, CA-058, CA-060, CA-061, CA-062, CA-063, CA-064, CA-065, RC CA-066, CA-068, CA-069, CA-070, CA-072, CA-073, CA-075, CA-081, RC CA-083, CA-086, CA-087, CA-088, CA-089, CA-090, CA-091, CA-093, RC CA-095, CA-096, CA-100, CA-105, CA-113, CA-114, CA-115, CA-118, RC CA-120, CA-123, CA-126, CA-127, CA-128, CA-129, CA-130, CA-132, RC CA-133, CA-136, CA-137, CA-140, CA-142, CA-144, CA-145, CA-147, RC CA-148, NC-001, NC-002, NC-003, NC-004, NC-005, NC-006, NC-008, RC NC-010, NC-011, NC-012, NC-013, NC-014, NC-015, NC-017, NC-021, RC NC-022, NC-023, NC-024, NC-025, NC-026, NC-027, NC-028, NC-029, RC NC-030, NC-032, NC-033, NC-034, NC-036, NC-037, NC-038, NC-039, RC NC-040, NC-041, NC-042, NC-043, NC-044, NC-046, NC-047, NC-048, RC NC-049, NC-050, NC-051, NC-052, NC-053, NC-054, NC-057, NC-058, RC NC-059, NC-060, NC-061, NC-064, NC-066, NC-067, NC-068, NC-069, RC NC-070, NC-071, NC-072, NC-073, NC-074, NC-075, NC-077, NC-079, RC NC-080, NC-081, NC-084, NC-086, NC-087, NC-088, NC-089, NC-091, RC NC-092, NC-094, NC-095, NC-096, NC-097, NC-098, NC-100, NC-101, RC NC-103, NC-104, NC-105, NC-107, NC-108, NC-109, NC-110, NC-111, RC NC-112, NC-113, NC-114, NC-115, NC-116, NC-118, NC-119, NC-121, RC NC-123, NC-124, NC-125, NC-126, NC-127, NC-128, NC-129, NC-131, RC NC-133, NC-134, NC-135, NC-136, NC-137, NC-138, NC-139, NC-141, RC NC-142, NC-144, NC-146, NC-147, NC-148, NC-149, and NC-150; RX PubMed=15611167; DOI=10.1534/genetics.104.028712; RA Nikoh N., Duty A., Gibson G.; RT "Effects of population structure and sex on association between RT serotonin receptors and Drosophila heart rate."; RL Genetics 168:1963-1974(2004). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins which inhibit adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11489; CAA77570.1; -; mRNA. DR EMBL; AE003797; AAM68432.1; -; Genomic_DNA. DR EMBL; AY564785; AAS73796.1; -; Genomic_DNA. DR EMBL; AY564786; AAS73797.1; -; Genomic_DNA. DR EMBL; AY564787; AAS73798.1; -; Genomic_DNA. DR EMBL; AY564788; AAS73799.1; -; Genomic_DNA. DR EMBL; AY564789; AAS73800.1; -; Genomic_DNA. DR EMBL; AY564790; AAS73801.1; -; Genomic_DNA. DR EMBL; AY564791; AAS73802.1; -; Genomic_DNA. DR EMBL; AY564792; AAS73803.1; -; Genomic_DNA. DR EMBL; AY564793; AAS73804.1; -; Genomic_DNA. DR EMBL; AY564794; AAS73805.1; -; Genomic_DNA. DR EMBL; AY564795; AAS73806.1; -; Genomic_DNA. DR EMBL; AY564796; AAS73807.1; -; Genomic_DNA. DR EMBL; AY564797; AAS73808.1; -; Genomic_DNA. DR EMBL; AY564798; AAS73809.1; -; Genomic_DNA. DR EMBL; AY564799; AAS73810.1; -; Genomic_DNA. DR EMBL; AY564800; AAS73811.1; -; Genomic_DNA. DR EMBL; AY564801; AAS73812.1; -; Genomic_DNA. DR EMBL; AY564802; AAS73813.1; -; Genomic_DNA. DR EMBL; AY564803; AAS73814.1; -; Genomic_DNA. DR EMBL; AY564804; AAS73815.1; -; Genomic_DNA. DR EMBL; AY564805; AAS73816.1; -; Genomic_DNA. DR EMBL; AY564806; AAS73817.1; -; Genomic_DNA. DR EMBL; AY564807; AAS73818.1; -; Genomic_DNA. DR EMBL; AY564808; AAS73819.1; -; Genomic_DNA. DR EMBL; AY564809; AAS73820.1; -; Genomic_DNA. DR EMBL; AY564810; AAS73821.1; -; Genomic_DNA. DR EMBL; AY564811; AAS73822.1; -; Genomic_DNA. DR EMBL; AY564812; AAS73823.1; -; Genomic_DNA. DR EMBL; AY564813; AAS73824.1; -; Genomic_DNA. DR EMBL; AY564814; AAS73825.1; -; Genomic_DNA. DR EMBL; AY564815; AAS73826.1; -; Genomic_DNA. DR EMBL; AY564816; AAS73827.1; -; Genomic_DNA. DR EMBL; AY564817; AAS73828.1; -; Genomic_DNA. DR EMBL; AY564818; AAS73829.1; -; Genomic_DNA. DR EMBL; AY564819; AAS73830.1; -; Genomic_DNA. DR EMBL; AY564820; AAS73831.1; -; Genomic_DNA. DR EMBL; AY564821; AAS73832.1; -; Genomic_DNA. DR EMBL; AY564822; AAS73833.1; -; Genomic_DNA. DR EMBL; AY564823; AAS73834.1; -; Genomic_DNA. DR EMBL; AY564824; AAS73835.1; -; Genomic_DNA. DR EMBL; AY564825; AAS73836.1; -; Genomic_DNA. DR EMBL; AY564826; AAS73837.1; -; Genomic_DNA. DR EMBL; AY564827; AAS73838.1; -; Genomic_DNA. DR EMBL; AY564828; AAS73839.1; -; Genomic_DNA. DR EMBL; AY564829; AAS73840.1; -; Genomic_DNA. DR EMBL; AY564830; AAS73841.1; -; Genomic_DNA. DR EMBL; AY564831; AAS73842.1; -; Genomic_DNA. DR EMBL; AY564832; AAS73843.1; -; Genomic_DNA. DR EMBL; AY564833; AAS73844.1; -; Genomic_DNA. DR EMBL; AY564834; AAS73845.1; -; Genomic_DNA. DR EMBL; AY564835; AAS73846.1; -; Genomic_DNA. DR EMBL; AY564836; AAS73847.1; -; Genomic_DNA. DR EMBL; AY564837; AAS73848.1; -; Genomic_DNA. DR EMBL; AY564838; AAS73849.1; -; Genomic_DNA. DR EMBL; AY564839; AAS73850.1; -; Genomic_DNA. DR EMBL; AY564840; AAS73851.1; -; Genomic_DNA. DR EMBL; AY564841; AAS73852.1; -; Genomic_DNA. DR EMBL; AY564842; AAS73853.1; -; Genomic_DNA. DR EMBL; AY564843; AAS73854.1; -; Genomic_DNA. DR EMBL; AY564844; AAS73855.1; -; Genomic_DNA. DR EMBL; AY564845; AAS73856.1; -; Genomic_DNA. DR EMBL; AY564846; AAS73857.1; -; Genomic_DNA. DR EMBL; AY564847; AAS73858.1; -; Genomic_DNA. DR EMBL; AY564848; AAS73859.1; -; Genomic_DNA. DR EMBL; AY564849; AAS73860.1; -; Genomic_DNA. DR EMBL; AY564850; AAS73861.1; -; Genomic_DNA. DR EMBL; AY564851; AAS73862.1; -; Genomic_DNA. DR EMBL; AY564852; AAS73863.1; -; Genomic_DNA. DR EMBL; AY564853; AAS73864.1; -; Genomic_DNA. DR EMBL; AY564854; AAS73865.1; -; Genomic_DNA. DR EMBL; AY564855; AAS73866.1; -; Genomic_DNA. DR EMBL; AY564856; AAS73867.1; -; Genomic_DNA. DR EMBL; AY564857; AAS73868.1; -; Genomic_DNA. DR EMBL; AY564858; AAS73869.1; -; Genomic_DNA. DR EMBL; AY564859; AAS73870.1; -; Genomic_DNA. DR EMBL; AY564860; AAS73871.1; -; Genomic_DNA. DR EMBL; AY564861; AAS73872.1; -; Genomic_DNA. DR EMBL; AY564862; AAS73873.1; -; Genomic_DNA. DR EMBL; AY564863; AAS73874.1; -; Genomic_DNA. DR EMBL; AY564864; AAS73875.1; -; Genomic_DNA. DR EMBL; AY564865; AAS73876.1; -; Genomic_DNA. DR EMBL; AY564866; AAS73877.1; -; Genomic_DNA. DR EMBL; AY564867; AAS73878.1; -; Genomic_DNA. DR EMBL; AY564868; AAS73879.1; -; Genomic_DNA. DR EMBL; AY564869; AAS73880.1; -; Genomic_DNA. DR EMBL; AY564870; AAS73881.1; -; Genomic_DNA. DR EMBL; AY564871; AAS73882.1; -; Genomic_DNA. DR EMBL; AY564872; AAS73883.1; -; Genomic_DNA. DR EMBL; AY564873; AAS73884.1; -; Genomic_DNA. DR EMBL; AY564874; AAS73885.1; -; Genomic_DNA. DR EMBL; AY564875; AAS73886.1; -; Genomic_DNA. DR EMBL; AY564876; AAS73887.1; -; Genomic_DNA. DR EMBL; AY564877; AAS73888.1; -; Genomic_DNA. DR EMBL; AY564878; AAS73889.1; -; Genomic_DNA. DR EMBL; AY564879; AAS73890.1; -; Genomic_DNA. DR EMBL; AY564880; AAS73891.1; -; Genomic_DNA. DR EMBL; AY564881; AAS73892.1; -; Genomic_DNA. DR EMBL; AY564882; AAS73893.1; -; Genomic_DNA. DR EMBL; AY564883; AAS73894.1; -; Genomic_DNA. DR EMBL; AY564884; AAS73895.1; -; Genomic_DNA. DR EMBL; AY564885; AAS73896.1; -; Genomic_DNA. DR EMBL; AY564886; AAS73897.1; -; Genomic_DNA. DR EMBL; AY564887; AAS73898.1; -; Genomic_DNA. DR EMBL; AY564888; AAS73899.1; -; Genomic_DNA. DR EMBL; AY564889; AAS73900.1; -; Genomic_DNA. DR EMBL; AY564890; AAS73901.1; -; Genomic_DNA. DR EMBL; AY564891; AAS73902.1; -; Genomic_DNA. DR EMBL; AY564892; AAS73903.1; -; Genomic_DNA. DR EMBL; AY564893; AAS73904.1; -; Genomic_DNA. DR EMBL; AY564894; AAS73905.1; -; Genomic_DNA. DR EMBL; AY564895; AAS73906.1; -; Genomic_DNA. DR EMBL; AY564896; AAS73907.1; -; Genomic_DNA. DR EMBL; AY564897; AAS73908.1; -; Genomic_DNA. DR EMBL; AY564898; AAS73909.1; -; Genomic_DNA. DR EMBL; AY564899; AAS73910.1; -; Genomic_DNA. DR EMBL; AY564900; AAS73911.1; -; Genomic_DNA. DR EMBL; AY564901; AAS73912.1; -; Genomic_DNA. DR EMBL; AY564902; AAS73913.1; -; Genomic_DNA. DR EMBL; AY564903; AAS73914.1; -; Genomic_DNA. DR EMBL; AY564904; AAS73915.1; -; Genomic_DNA. DR EMBL; AY564905; AAS73916.1; -; Genomic_DNA. DR EMBL; AY564906; AAS73917.1; -; Genomic_DNA. DR EMBL; AY564907; AAS73918.1; -; Genomic_DNA. DR EMBL; AY564908; AAS73919.1; -; Genomic_DNA. DR EMBL; AY564909; AAS73920.1; -; Genomic_DNA. DR EMBL; AY564910; AAS73921.1; -; Genomic_DNA. DR EMBL; AY564911; AAS73922.1; -; Genomic_DNA. DR EMBL; AY564912; AAS73923.1; -; Genomic_DNA. DR EMBL; AY564913; AAS73924.1; -; Genomic_DNA. DR EMBL; AY564914; AAS73925.1; -; Genomic_DNA. DR EMBL; AY564915; AAS73926.1; -; Genomic_DNA. DR EMBL; AY564916; AAS73927.1; -; Genomic_DNA. DR EMBL; AY564917; AAS73928.1; -; Genomic_DNA. DR EMBL; AY564918; AAS73929.1; -; Genomic_DNA. DR EMBL; AY564919; AAS73930.1; -; Genomic_DNA. DR EMBL; AY564920; AAS73931.1; -; Genomic_DNA. DR EMBL; AY564921; AAS73932.1; -; Genomic_DNA. DR EMBL; AY564922; AAS73933.1; -; Genomic_DNA. DR EMBL; AY564925; AAS73936.1; -; Genomic_DNA. DR EMBL; AY564926; AAS73937.1; -; Genomic_DNA. DR EMBL; AY564927; AAS73938.1; -; Genomic_DNA. DR EMBL; AY564928; AAS73939.1; -; Genomic_DNA. DR EMBL; AY564929; AAS73940.1; -; Genomic_DNA. DR EMBL; AY564930; AAS73941.1; -; Genomic_DNA. DR EMBL; AY564931; AAS73942.1; -; Genomic_DNA. DR EMBL; AY564932; AAS73943.1; -; Genomic_DNA. DR EMBL; AY564933; AAS73944.1; -; Genomic_DNA. DR EMBL; AY564934; AAS73945.1; -; Genomic_DNA. DR EMBL; AY564935; AAS73946.1; -; Genomic_DNA. DR EMBL; AY564936; AAS73947.1; -; Genomic_DNA. DR EMBL; AY564937; AAS73948.1; -; Genomic_DNA. DR EMBL; AY564938; AAS73949.1; -; Genomic_DNA. DR EMBL; AY564939; AAS73950.1; -; Genomic_DNA. DR EMBL; AY564940; AAS73951.1; -; Genomic_DNA. DR EMBL; AY564941; AAS73952.1; -; Genomic_DNA. DR EMBL; AY564942; AAS73953.1; -; Genomic_DNA. DR EMBL; AY564943; AAS73954.1; -; Genomic_DNA. DR EMBL; AY564944; AAS73955.1; -; Genomic_DNA. DR EMBL; AY564945; AAS73956.1; -; Genomic_DNA. DR EMBL; AY564946; AAS73957.1; -; Genomic_DNA. DR EMBL; AY564947; AAS73958.1; -; Genomic_DNA. DR EMBL; AY564948; AAS73959.1; -; Genomic_DNA. DR EMBL; AY564949; AAS73960.1; -; Genomic_DNA. DR EMBL; AY564950; AAS73961.1; -; Genomic_DNA. DR EMBL; AY564951; AAS73962.1; -; Genomic_DNA. DR EMBL; AY564952; AAS73963.1; -; Genomic_DNA. DR EMBL; AY564953; AAS73964.1; -; Genomic_DNA. DR EMBL; AY564954; AAS73965.1; -; Genomic_DNA. DR EMBL; AY564955; AAS73966.1; -; Genomic_DNA. DR EMBL; AY564956; AAS73967.1; -; Genomic_DNA. DR EMBL; AY564958; AAS73968.1; -; Genomic_DNA. DR EMBL; AY564959; AAS73969.1; -; Genomic_DNA. DR EMBL; AY564960; AAS73970.1; -; Genomic_DNA. DR EMBL; AY564961; AAS73971.1; -; Genomic_DNA. DR EMBL; AY564962; AAS73972.1; -; Genomic_DNA. DR EMBL; AY564963; AAS73973.1; -; Genomic_DNA. DR EMBL; AY564964; AAS73974.1; -; Genomic_DNA. DR EMBL; AY564965; AAS73975.1; -; Genomic_DNA. DR EMBL; AY564966; AAS73976.1; -; Genomic_DNA. DR EMBL; AY564967; AAS73977.1; -; Genomic_DNA. DR EMBL; AY564968; AAS73978.1; -; Genomic_DNA. DR EMBL; AY564969; AAS73979.1; -; Genomic_DNA. DR EMBL; AY564971; AAS73981.1; -; Genomic_DNA. DR EMBL; AY564972; AAS73982.1; -; Genomic_DNA. DR EMBL; AY564973; AAS73983.1; -; Genomic_DNA. DR EMBL; AY564974; AAS73984.1; -; Genomic_DNA. DR EMBL; AY564975; AAS73985.1; -; Genomic_DNA. DR EMBL; AY564976; AAS73986.1; -; Genomic_DNA. DR EMBL; AY564977; AAS73987.1; -; Genomic_DNA. DR EMBL; AY565171; AAS74181.1; -; Genomic_DNA. DR EMBL; AY565172; AAS74182.1; -; Genomic_DNA. DR EMBL; AY565173; AAS74183.1; -; Genomic_DNA. DR EMBL; AY565174; AAS74184.1; -; Genomic_DNA. DR EMBL; AY565175; AAS74185.1; -; Genomic_DNA. DR EMBL; AY565176; AAS74186.1; -; Genomic_DNA. DR EMBL; AY565177; AAS74187.1; -; Genomic_DNA. DR EMBL; AY565178; AAS74188.1; -; Genomic_DNA. DR EMBL; AY565179; AAS74189.1; -; Genomic_DNA. DR EMBL; AY565180; AAS74190.1; -; Genomic_DNA. DR EMBL; AY565181; AAS74191.1; -; Genomic_DNA. DR EMBL; AY565182; AAS74192.1; -; Genomic_DNA. DR EMBL; AY565183; AAS74193.1; -; Genomic_DNA. DR EMBL; AY565184; AAS74194.1; -; Genomic_DNA. DR EMBL; AY565185; AAS74195.1; -; Genomic_DNA. DR EMBL; AY565186; AAS74196.1; -; Genomic_DNA. DR EMBL; AY565187; AAS74197.1; -; Genomic_DNA. DR EMBL; AY565188; AAS74198.1; -; Genomic_DNA. DR EMBL; AY565189; AAS74199.1; -; Genomic_DNA. DR EMBL; AY565190; AAS74200.1; -; Genomic_DNA. DR EMBL; AY565191; AAS74201.1; -; Genomic_DNA. DR EMBL; AY565192; AAS74202.1; -; Genomic_DNA. DR EMBL; AY565193; AAS74203.1; -; Genomic_DNA. DR EMBL; AY565194; AAS74204.1; -; Genomic_DNA. DR EMBL; AY565195; AAS74205.1; -; Genomic_DNA. DR EMBL; AY565196; AAS74206.1; -; Genomic_DNA. DR EMBL; AY565197; AAS74207.1; -; Genomic_DNA. DR EMBL; AY565198; AAS74208.1; -; Genomic_DNA. DR EMBL; AY565199; AAS74209.1; -; Genomic_DNA. DR EMBL; AY565200; AAS74210.1; -; Genomic_DNA. DR EMBL; AY565201; AAS74211.1; -; Genomic_DNA. DR EMBL; AY565202; AAS74212.1; -; Genomic_DNA. DR EMBL; AY565203; AAS74213.1; -; Genomic_DNA. DR EMBL; AY565204; AAS74214.1; -; Genomic_DNA. DR EMBL; AY565205; AAS74215.1; -; Genomic_DNA. DR EMBL; AY565206; AAS74216.1; -; Genomic_DNA. DR EMBL; AY565207; AAS74217.1; -; Genomic_DNA. DR EMBL; AY565208; AAS74218.1; -; Genomic_DNA. DR EMBL; AY565209; AAS74219.1; -; Genomic_DNA. DR EMBL; AY565210; AAS74220.1; -; Genomic_DNA. DR EMBL; AY565211; AAS74221.1; -; Genomic_DNA. DR EMBL; AY565212; AAS74222.1; -; Genomic_DNA. DR EMBL; AY565213; AAS74223.1; -; Genomic_DNA. DR EMBL; AY565214; AAS74224.1; -; Genomic_DNA. DR EMBL; AY565215; AAS74225.1; -; Genomic_DNA. DR EMBL; AY565216; AAS74226.1; -; Genomic_DNA. DR EMBL; AY565217; AAS74227.1; -; Genomic_DNA. DR EMBL; AY565218; AAS74228.1; -; Genomic_DNA. DR EMBL; AY565219; AAS74229.1; -; Genomic_DNA. DR EMBL; AY565220; AAS74230.1; -; Genomic_DNA. DR EMBL; AY565221; AAS74231.1; -; Genomic_DNA. DR EMBL; AY565222; AAS74232.1; -; Genomic_DNA. DR EMBL; AY565223; AAS74233.1; -; Genomic_DNA. DR EMBL; AY565224; AAS74234.1; -; Genomic_DNA. DR EMBL; AY565225; AAS74235.1; -; Genomic_DNA. DR EMBL; AY565226; AAS74236.1; -; Genomic_DNA. DR EMBL; AY565227; AAS74237.1; -; Genomic_DNA. DR EMBL; AY565228; AAS74238.1; -; Genomic_DNA. DR EMBL; AY565229; AAS74239.1; -; Genomic_DNA. DR EMBL; AY565230; AAS74240.1; -; Genomic_DNA. DR EMBL; AY565231; AAS74241.1; -; Genomic_DNA. DR EMBL; AY565232; AAS74242.1; -; Genomic_DNA. DR EMBL; AY565233; AAS74243.1; -; Genomic_DNA. DR EMBL; AY565234; AAS74244.1; -; Genomic_DNA. DR EMBL; AY565235; AAS74245.1; -; Genomic_DNA. DR EMBL; AY565236; AAS74246.1; -; Genomic_DNA. DR EMBL; AY565237; AAS74247.1; -; Genomic_DNA. DR EMBL; AY565238; AAS74248.1; -; Genomic_DNA. DR EMBL; AY565239; AAS74249.1; -; Genomic_DNA. DR EMBL; AY565240; AAS74250.1; -; Genomic_DNA. DR EMBL; AY565241; AAS74251.1; -; Genomic_DNA. DR EMBL; AY565242; AAS74252.1; -; Genomic_DNA. DR EMBL; AY565243; AAS74253.1; -; Genomic_DNA. DR EMBL; AY565244; AAS74254.1; -; Genomic_DNA. DR EMBL; AY565245; AAS74255.1; -; Genomic_DNA. DR EMBL; AY565246; AAS74256.1; -; Genomic_DNA. DR EMBL; AY565247; AAS74257.1; -; Genomic_DNA. DR EMBL; AY565248; AAS74258.1; -; Genomic_DNA. DR EMBL; AY565249; AAS74259.1; -; Genomic_DNA. DR EMBL; AY565250; AAS74260.1; -; Genomic_DNA. DR EMBL; AY565251; AAS74261.1; -; Genomic_DNA. DR EMBL; AY565252; AAS74262.1; -; Genomic_DNA. DR EMBL; AY565253; AAS74263.1; -; Genomic_DNA. DR EMBL; AY565254; AAS74264.1; -; Genomic_DNA. DR EMBL; AY565255; AAS74265.1; -; Genomic_DNA. DR EMBL; AY565256; AAS74266.1; -; Genomic_DNA. DR EMBL; AY565257; AAS74267.1; -; Genomic_DNA. DR EMBL; AY565258; AAS74268.1; -; Genomic_DNA. DR EMBL; AY565259; AAS74269.1; -; Genomic_DNA. DR EMBL; AY565260; AAS74270.1; -; Genomic_DNA. DR EMBL; AY565261; AAS74271.1; -; Genomic_DNA. DR EMBL; AY565262; AAS74272.1; -; Genomic_DNA. DR EMBL; AY565264; AAS74274.1; -; Genomic_DNA. DR EMBL; AY565265; AAS74275.1; -; Genomic_DNA. DR EMBL; AY565266; AAS74276.1; -; Genomic_DNA. DR EMBL; AY565267; AAS74277.1; -; Genomic_DNA. DR EMBL; AY565268; AAS74278.1; -; Genomic_DNA. DR EMBL; AY565269; AAS74279.1; -; Genomic_DNA. DR EMBL; AY565270; AAS74280.1; -; Genomic_DNA. DR EMBL; AY565271; AAS74281.1; -; Genomic_DNA. DR EMBL; AY565272; AAS74282.1; -; Genomic_DNA. DR EMBL; AY565273; AAS74283.1; -; Genomic_DNA. DR EMBL; AY565274; AAS74284.1; -; Genomic_DNA. DR EMBL; AY565275; AAS74285.1; -; Genomic_DNA. DR EMBL; AY565276; AAS74286.1; -; Genomic_DNA. DR EMBL; AY565277; AAS74287.1; -; Genomic_DNA. DR EMBL; AY565278; AAS74288.1; -; Genomic_DNA. DR EMBL; AY565279; AAS74289.1; -; Genomic_DNA. DR EMBL; AY565280; AAS74290.1; -; Genomic_DNA. DR EMBL; AY565281; AAS74291.1; -; Genomic_DNA. DR EMBL; AY565282; AAS74292.1; -; Genomic_DNA. DR EMBL; AY565283; AAS74293.1; -; Genomic_DNA. DR EMBL; AY565284; AAS74294.1; -; Genomic_DNA. DR EMBL; AY565285; AAS74295.1; -; Genomic_DNA. DR EMBL; AY565286; AAS74296.1; -; Genomic_DNA. DR EMBL; AY565287; AAS74297.1; -; Genomic_DNA. DR EMBL; AY565288; AAS74298.1; -; Genomic_DNA. DR EMBL; AY565289; AAS74299.1; -; Genomic_DNA. DR EMBL; AY565290; AAS74300.1; -; Genomic_DNA. DR EMBL; AY565291; AAS74301.1; -; Genomic_DNA. DR EMBL; AY565292; AAS74302.1; -; Genomic_DNA. DR EMBL; AY565293; AAS74303.1; -; Genomic_DNA. DR EMBL; AY565294; AAS74304.1; -; Genomic_DNA. DR EMBL; AY565295; AAS74305.1; -; Genomic_DNA. DR EMBL; AY565296; AAS74306.1; -; Genomic_DNA. DR EMBL; AY565297; AAS74307.1; -; Genomic_DNA. DR EMBL; AY565298; AAS74308.1; -; Genomic_DNA. DR EMBL; AY565299; AAS74309.1; -; Genomic_DNA. DR EMBL; AY565300; AAS74310.1; -; Genomic_DNA. DR EMBL; AY565301; AAS74311.1; -; Genomic_DNA. DR EMBL; AY565302; AAS74312.1; -; Genomic_DNA. DR EMBL; AY565303; AAS74313.1; -; Genomic_DNA. DR EMBL; AY565304; AAS74314.1; -; Genomic_DNA. DR EMBL; AY565305; AAS74315.1; -; Genomic_DNA. DR EMBL; AY565306; AAS74316.1; -; Genomic_DNA. DR EMBL; AY565307; AAS74317.1; -; Genomic_DNA. DR EMBL; AY565308; AAS74318.1; -; Genomic_DNA. DR EMBL; AY565309; AAS74319.1; -; Genomic_DNA. DR EMBL; AY565310; AAS74320.1; -; Genomic_DNA. DR EMBL; AY565311; AAS74321.1; -; Genomic_DNA. DR EMBL; AY565312; AAS74322.1; -; Genomic_DNA. DR EMBL; AY565313; AAS74323.1; -; Genomic_DNA. DR EMBL; AY565314; AAS74324.1; -; Genomic_DNA. DR EMBL; AY565315; AAS74325.1; -; Genomic_DNA. DR EMBL; AY565316; AAS74326.1; -; Genomic_DNA. DR EMBL; AY565317; AAS74327.1; -; Genomic_DNA. DR EMBL; AY565318; AAS74328.1; -; Genomic_DNA. DR EMBL; AY565319; AAS74329.1; -; Genomic_DNA. DR EMBL; AY565320; AAS74330.1; -; Genomic_DNA. DR EMBL; AY565321; AAS74331.1; -; Genomic_DNA. DR EMBL; AY565322; AAS74332.1; -; Genomic_DNA. DR EMBL; AY565323; AAS74333.1; -; Genomic_DNA. DR EMBL; AY565324; AAS74334.1; -; Genomic_DNA. DR EMBL; AY565325; AAS74335.1; -; Genomic_DNA. DR EMBL; AY565326; AAS74336.1; -; Genomic_DNA. DR EMBL; AY565327; AAS74337.1; -; Genomic_DNA. DR EMBL; AY565328; AAS74338.1; -; Genomic_DNA. DR EMBL; AY565329; AAS74339.1; -; Genomic_DNA. DR EMBL; AY565330; AAS74340.1; -; Genomic_DNA. DR EMBL; AY565331; AAS74341.1; -; Genomic_DNA. DR EMBL; AY565332; AAS74342.1; -; Genomic_DNA. DR EMBL; AY565333; AAS74343.1; -; Genomic_DNA. DR EMBL; AY565334; AAS74344.1; -; Genomic_DNA. DR EMBL; AY565335; AAS74345.1; -; Genomic_DNA. DR EMBL; AY565336; AAS74346.1; -; Genomic_DNA. DR EMBL; AY565337; AAS74347.1; -; Genomic_DNA. DR EMBL; AY565338; AAS74348.1; -; Genomic_DNA. DR EMBL; AY565339; AAS74349.1; -; Genomic_DNA. DR EMBL; AY565340; AAS74350.1; -; Genomic_DNA. DR EMBL; AY565341; AAS74351.1; -; Genomic_DNA. DR EMBL; AY565342; AAS74352.1; -; Genomic_DNA. DR EMBL; AY565343; AAS74353.1; -; Genomic_DNA. DR EMBL; AY565344; AAS74354.1; -; Genomic_DNA. DR EMBL; AY565345; AAS74355.1; -; Genomic_DNA. DR EMBL; AY565346; AAS74356.1; -; Genomic_DNA. DR EMBL; AY565347; AAS74357.1; -; Genomic_DNA. DR EMBL; AY565348; AAS74358.1; -; Genomic_DNA. DR EMBL; AY565349; AAS74359.1; -; Genomic_DNA. DR EMBL; AY565350; AAS74360.1; -; Genomic_DNA. DR EMBL; AY565351; AAS74361.1; -; Genomic_DNA. DR EMBL; AY565352; AAS74362.1; -; Genomic_DNA. DR EMBL; AY565353; AAS74363.1; -; Genomic_DNA. DR EMBL; AY565354; AAS74364.1; -; Genomic_DNA. DR EMBL; AY565355; AAS74365.1; -; Genomic_DNA. DR EMBL; AY565356; AAS74366.1; -; Genomic_DNA. DR EMBL; AY565357; AAS74367.1; -; Genomic_DNA. DR EMBL; AY565358; AAS74368.1; -; Genomic_DNA. DR EMBL; AY565359; AAS74369.1; -; Genomic_DNA. DR EMBL; AY565360; AAS74370.1; -; Genomic_DNA. DR EMBL; AY565361; AAS74371.1; -; Genomic_DNA. DR EMBL; AY565362; AAS74372.1; -; Genomic_DNA. DR EMBL; AY565363; AAS74373.1; -; Genomic_DNA. DR EMBL; AY565364; AAS74374.1; -; Genomic_DNA. DR EMBL; AY565365; AAS74375.1; -; Genomic_DNA. DR EMBL; AY565366; AAS74376.1; -; Genomic_DNA. DR EMBL; AY565367; AAS74377.1; -; Genomic_DNA. DR EMBL; AY565368; AAS74378.1; -; Genomic_DNA. DR PIR; S19155; S19155. DR UniGene; Dm.4703; -. DR HSSP; P08913; 1HLL. DR Ensembl; CG16720; Drosophila melanogaster. DR FlyBase; FBgn0004168; 5-HT1A. DR GO; GO:0001586; F:5-HT1 receptor activity; NAS. DR GO; GO:0007198; P:serotonin receptor, adenylate cyclase inhib...; IDA. DR GO; GO:0007208; P:serotonin receptor, phospholipase C activat...; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Complete proteome; G-protein coupled receptor; Glycoprotein; Membrane; KW Polymorphism; Receptor; Transducer; Transmembrane. FT CHAIN 1 834 5-hydroxytryptamine receptor 2A. FT /FTId=PRO_0000068962. FT TOPO_DOM 1 230 Extracellular (Potential). FT TRANSMEM 231 253 1 (Potential). FT TOPO_DOM 254 263 Cytoplasmic (Potential). FT TRANSMEM 264 285 2 (Potential). FT TOPO_DOM 286 300 Extracellular (Potential). FT TRANSMEM 301 322 3 (Potential). FT TOPO_DOM 323 341 Cytoplasmic (Potential). FT TRANSMEM 342 364 4 (Potential). FT TOPO_DOM 365 391 Extracellular (Potential). FT TRANSMEM 392 413 5 (Potential). FT TOPO_DOM 414 752 Cytoplasmic (Potential). FT TRANSMEM 753 776 6 (Potential). FT TOPO_DOM 777 785 Extracellular (Potential). FT TRANSMEM 786 808 7 (Potential). FT TOPO_DOM 809 834 Cytoplasmic (Potential). FT COMPBIAS 108 136 Ala-rich. FT COMPBIAS 707 723 Gln-rich. FT CARBOHYD 68 68 N-linked (GlcNAc...) (Potential). FT CARBOHYD 97 97 N-linked (GlcNAc...) (Potential). FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential). FT CARBOHYD 175 175 N-linked (GlcNAc...) (Potential). FT CARBOHYD 183 183 N-linked (GlcNAc...) (Potential). FT CARBOHYD 194 194 N-linked (GlcNAc...) (Potential). FT CARBOHYD 203 203 N-linked (GlcNAc...) (Potential). FT CARBOHYD 209 209 N-linked (GlcNAc...) (Potential). FT DISULFID 299 378 By similarity. FT VARIANT 29 32 Missing (in strain: CA-128). FT VARIANT 46 46 E -> Q (in strain: NC-066). FT VARIANT 49 49 E -> V (in strain: NC-036 and NC-123). FT VARIANT 51 51 D -> E (in strain: CA-002, CA-008, CA- FT 009, CA-011, CA-013, CA-015, CA-026, CA- FT 031, CA-033, CA-034, CA-035, CA-037, CA- FT 040, CA-048, CA-052, CA-055, CA-057, CA- FT 060, CA-061, CA-063, CA-064, CA-065, CA- FT 069, CA-072, CA-073, CA-075, CA-088, CA- FT 090, CA-093, CA-096, CA-100, CA-114, CA- FT 120, CA-127, CA-129, CA-132, CA-133, CA- FT 140, CA-142, CA-145, CA-147, NC-003, NC- FT 006, NC-010, NC-011, NC-014, NC-015, NC- FT 021, NC-033, NC-034, NC-036, NC-040, NC- FT 042, NC-044, NC-046, NC-047, NC-051, NC- FT 052, NC-054, NC-057, NC-066, NC-069, NC- FT 071, NC-073, NC-081, NC-084, NC-086, NC- FT 089, NC-092, NC-094, NC-096, NC-097, NC- FT 101, NC-103, NC-104, NC-107, NC-108, NC- FT 118, NC-119, NC-121, NC-123, NC-127, NC- FT 128, NC-129, NC-134, NC-136, NC-137, NC- FT 138, NC-141, NC-144 and NC-148). FT VARIANT 52 52 D -> E (in strain: NC-103 and NC-118). FT VARIANT 54 54 A -> G (in strain: NC-061). FT VARIANT 76 76 S -> T (in strain: NC-012, NC-023, NC- FT 037, NC-038, NC-039, NC-124 and NC-131). FT VARIANT 86 86 S -> T (in strain: CA-008, CA-009, CA- FT 013, CA-026, CA-031, CA-033, CA-035, CA- FT 037, CA-040, CA-048, CA-052, CA-057, CA- FT 060, CA-061, CA-063, CA-065, CA-072, CA- FT 073, CA-088, CA-093, CA-096, CA-100, CA- FT 114, CA-120, CA-129, CA-132, CA-133, CA- FT 140, CA-147, NC-011, NC-015, NC-021, NC- FT 033, NC-034, NC-040, NC-042, NC-044, NC- FT 046, NC-047, NC-051, NC-052, NC-054, NC- FT 057, NC-069, NC-084, NC-089, NC-092, NC- FT 094, NC-097, NC-103, NC-107, NC-119, NC- FT 121, NC-127, NC-128, NC-129, NC-134, NC- FT 137, NC-138, NC-141, NC-144 and NC-148). FT VARIANT 91 91 P -> Q (in strain: CA-030, CA-068, CA- FT 091, NC-008, NC-025, NC-043, NC-048, NC- FT 060, NC-075, NC-088, NC-091, NC-114, NC- FT 116 and NC-135). FT VARIANT 96 96 V -> A (in strain: CA-008, CA-009, CA- FT 011, CA-013, CA-015, CA-026, CA-031, CA- FT 033, CA-034, CA-035, CA-037, CA-040, CA- FT 048, CA-052, CA-055, CA-057, CA-060, CA- FT 061, CA-063, CA-064, CA-065, CA-069, CA- FT 072, CA-073, CA-075, CA-088, CA-090, CA- FT 093, CA-095, CA-096, CA-100, CA-114, CA- FT 120, CA-129, CA-132, CA-133, CA-140, CA- FT 147, NC-010, NC-011, NC-012, NC-014, NC- FT 015, NC-021, NC-023, NC-033, NC-034, NC- FT 036, NC-037, NC-038, NC-039, NC-040, NC- FT 042, NC-044, NC-046, NC-047, NC-051, NC- FT 052, NC-054, NC-057, NC-066, NC-069, NC- FT 073, NC-081, NC-084, NC-086, NC-089, NC- FT 092, NC-094, NC-096, NC-097, NC-101, NC- FT 103, NC-104, NC-107, NC-108, NC-118, NC- FT 119, NC-121, NC-123, NC-124, NC-127, NC- FT 128, NC-129, NC-131, NC-134, NC-136, NC- FT 137, NC-138, NC-141, NC-144, NC-148 and FT Oregon-R). FT VARIANT 143 143 A -> T (in strain: CA-064). FT VARIANT 146 146 S -> T (in strain: CA-008, CA-026, CA- FT 033, CA-035, CA-037, CA-048, CA-052, CA- FT 057, CA-060, CA-063, CA-065, CA-072, CA- FT 088, CA-090, CA-096, CA-100, CA-114, CA- FT 120, CA-132, CA-140, CA-147, NC-011, NC- FT 014, NC-033, NC-034, NC-040, NC-042, NC- FT 044, NC-046, NC-047, NC-051, NC-052, NC- FT 054, NC-057, NC-069, NC-084, NC-092, NC- FT 094, NC-096, NC-103, NC-105, NC-107, NC- FT 108, NC-118, NC-119, NC-121, NC-125, NC- FT 126, NC-127, NC-129, NC-138, NC-144 and FT NC-148). FT VARIANT 171 171 A -> V (in strain: CA-008, CA-009, CA- FT 026, CA-031, CA-033, CA-035, CA-037, CA- FT 048, CA-052, CA-057, CA-060, CA-061, CA- FT 063, CA-065, CA-072, CA-088, CA-096, CA- FT 100, CA-114, CA-120, CA-132, CA-140, CA- FT 147, NC-011, NC-034, NC-040, NC-042, NC- FT 044, NC-046, NC-047, NC-051, NC-052, NC- FT 054, NC-057, NC-069, NC-084, NC-092, NC- FT 094, NC-103, NC-107, NC-119, NC-121, NC- FT 127, NC-129, NC-138, NC-144 and NC-148). FT VARIANT 182 182 G -> D (in strain: NC-066). FT VARIANT 184 184 D -> Y (in strain: NC-086, NC-104 and NC- FT 010). FT VARIANT 196 196 S -> N (in strain: NC-114). FT VARIANT 198 198 Q -> H (in strain: CA-001, CA-009, CA- FT 011, CA-013, CA-015, CA-026, CA-030, CA- FT 031, CA-033, CA-034, CA-035, CA-037, CA- FT 040, CA-046, CA-048, CA-052, CA-055, CA- FT 057, CA-060, CA-061, CA-063, CA-065, CA- FT 066, CA-068, CA-069, CA-072, CA-073, CA- FT 075, CA-088, CA-090, CA-091, CA-093, CA- FT 095, CA-096, CA-100, CA-114, CA-120, CA- FT 132, CA-133, CA-140, CA-147, NC-008, NC- FT 011, NC-014, NC-015, NC-025, NC-034, NC- FT 040, NC-042, NC-043, NC-044, NC-046, NC- FT 047, NC-048, NC-051, NC-052, NC-054, NC- FT 057, NC-060, NC-066, NC-069, NC-073, NC- FT 075, NC-081, NC-084, NC-088, NC-091, NC- FT 092, NC-094, NC-096, NC-101, NC-103, NC- FT 107, NC-108, NC-110, NC-113, NC-114, NC- FT 115, NC-116, NC-118, NC-119, NC-121, NC- FT 123, NC-127, NC-128, NC-129, NC-135, NC- FT 136, NC-137, NC-138, NC-139, NC-142, NC- FT 144, NC-146, NC-148 and Oregon-R). FT VARIANT 213 213 S -> G (in strain: CA-015). FT VARIANT 531 531 Q -> L (in strain: NC-104). FT VARIANT 536 536 T -> A (in strain: CA-011, CA-017, CA- FT 018, CA-062, CA-130, NC-022, NC-026, NC- FT 049 and NC-073). FT VARIANT 547 550 APSG -> GPMGPL (in strain: CA-013, CA-026 FT and CA-093). FT VARIANT 571 571 E -> V (in strain: CA-002, CA-003, CA- FT 008, CA-011, CA-012, CA-015, CA-023, CA- FT 027, CA-030, CA-031, CA-034, CA-035, CA- FT 037, CA-043, CA-044, CA-045, CA-046, CA- FT 048, CA-052, CA-055, CA-057, CA-058, CA- FT 063, CA-064, CA-065, CA-066, CA-068, CA- FT 070, CA-072, CA-073, CA-075, CA-081, CA- FT 083, CA-087, CA-088, CA-089, CA-091, CA- FT 096, CA-100, CA-105, CA-114, CA-120, CA- FT 123, CA-128, CA-129, CA-133, CA-140, CA- FT 145, CA-147, CA-148, NC-001, NC-002, NC- FT 003, NC-010, NC-011, NC-012, NC-013, NC- FT 015, NC-023, NC-024, NC-025, NC-027, NC- FT 028, NC-029, NC-030, NC-032, NC-033, NC- FT 034, NC-036, NC-040, NC-041, NC-042, NC- FT 043, NC-044, NC-046, NC-047, NC-048, NC- FT 050, NC-051, NC-052, NC-054, NC-057, NC- FT 059, NC-060, NC-061, NC-066, NC-069, NC- FT 071, NC-072, NC-074, NC-075, NC-077, NC- FT 079, NC-080, NC-081, NC-084, NC-086, NC- FT 087, NC-088, NC-089, NC-091, NC-092, NC- FT 094, NC-098, NC-101, NC-103, NC-104, NC- FT 107, NC-109, NC-110, NC-111, NC-112, NC- FT 113, NC-114, NC-115, NC-116, NC-119, NC- FT 121, NC-124, NC-127, NC-128, NC-129, NC- FT 131, NC-133, NC-134, NC-135, NC-136, NC- FT 137, NC-138, NC-144, NC-146, NC-147, NC- FT 148 and NC-149). FT VARIANT 585 585 T -> K (in strain: NC-026). FT VARIANT 588 588 T -> M (in strain: Berkeley, CA-009, CA- FT 010, CA-013, CA-026, CA-041, CA-060, CA- FT 063, CA-066, CA-086, CA-093, CA-113, CA- FT 137, CA-145, NC-006, NC-008, NC-021, NC- FT 064, NC-067, NC-123, NC-142 and NC-150). FT VARIANT 589 589 T -> R (in strain: CA-040, CA-056, CA- FT 115, CA-118, CA-126, CA-132, CA-142, NC- FT 005, NC-037, NC-038, NC-039, NC-053, NC- FT 068, NC-095, NC-100, NC-105, NC-125, NC- FT 126 and NC-139). FT VARIANT 648 648 A -> V (in strain: CA-023, CA-048, NC- FT 015, NC-110, NC-128, NC-133 and NC-137). FT VARIANT 657 657 Q -> P (in strain: CA-130). FT VARIANT 682 682 S -> W (in strain: CA-043, CA-058 and CA- FT 105). FT VARIANT 688 688 T -> I (in strain: CA-088). FT VARIANT 692 692 S -> T (in strain: NC-104). FT VARIANT 706 706 P -> T (in strain: NC-001). FT VARIANT 716 717 Missing (in strain: CA-002, CA-009, CA- FT 010, CA-011, CA-017, CA-018, CA-023, CA- FT 030, CA-031, CA-037, CA-040, CA-041, CA- FT 044, CA-045, CA-047, CA-048, CA-052, CA- FT 056, CA-057, CA-062, CA-068, CA-070, CA- FT 075, CA-086, CA-087, CA-088, CA-089, CA- FT 091, CA-095, CA-096, CA-100, CA-113, CA- FT 114, CA-115, CA-118, CA-120, CA-126, CA- FT 127, CA-129, CA-132, CA-133, CA-136, CA- FT 140, CA-142, CA-145, CA-147, NC-001, NC- FT 003, NC-004, NC-005, NC-011, NC-015, NC- FT 017, NC-021, NC-022, NC-025, NC-033, NC- FT 034, NC-036, NC-037, NC-038, NC-039, NC- FT 040, NC-042, NC-044, NC-046, NC-048, NC- FT 049, NC-051, NC-052, NC-053, NC-054, NC- FT 057, NC-059, NC-068, NC-069, NC-070, NC- FT 071, NC-079, NC-080, NC-084, NC-086, NC- FT 087, NC-088, NC-089, NC-091, NC-092, NC- FT 094, NC-095, NC-100, NC-101, NC-104, NC- FT 105, NC-107, NC-109, NC-110, NC-111, NC- FT 112, NC-113, NC-114, NC-115, NC-116, NC- FT 119, NC-121, NC-123, NC-125, NC-126, NC- FT 128, NC-129, NC-133, NC-134, NC-135, NC- FT 136, NC-137, NC-138, NC-139, NC-142, NC- FT 144, NC-146, NC-147, NC-148, NC-149 and FT NC-150;). FT VARIANT 716 716 Q -> H (in strain: NC-032). FT VARIANT 716 716 Q -> QH (in strain: NC-047). FT VARIANT 717 719 QQQ -> H (in strain: CA-069, NC-096 and FT NC-108). FT CONFLICT 135 135 R -> W (in Ref. 1). FT CONFLICT 400 400 L -> M (in Ref. 1). SQ SEQUENCE 834 AA; 89521 MW; D3E27389921BD04F CRC64; MAHETSFNDA LDYIYIANSM NDRAFLIAEP HPEQPNVDGQ DQDDAELEEL DDMAVTDDGQ LEDTNNNNNS KRYYSSGKRR ADFIGSLALK PPPTDVNTTT TTAGSPLATA ALAAAAASAS VAAAAARITA KAAHRALTTK QDATSSPASS PALQLIDMDN NYTNVAVGLG AMLLNDTLLL EGNDSSLFGE MLANRSGQLD LINGTGGLNV TTSKVAEDDF TQLLRMAVTS VLLGLMILVT IIGNVFVIAA IILERNLQNV ANYLVASLAV ADLFVACLVM PLGAVYEISQ GWILGPELCD IWTSCDVLCC TASILHLVAI AVDRYWAVTN IDYIHSRTSN RVFMMIFCVW TAAVIVSLAP QFGWKDPDYL QRIEQQKCMV SQDVSYQVFA TCCTFYVPLL VILALYWKIY QTARKRIHRR RPRPVDAAVN NNQPDGGAAT DTKLHRLRLR LGRFSTAKSK TGSAVGVSGP ASGGRALGLV DGNSTNTVNT VEDTEFSSSN VDSKSRAGVE APSTSGNQIA TVSHLVALAK QQGKSTAKSS AAVNGMAPSG RQEDDGQRPE HGEQEDREEL EDQDEQVGPQ PTTATSATTA AGTNESEDQC KANGVEVLED PQLQQQLEQV QQLQKSVKSG GGGGASTSNA TTITSISALS PQTPTSQGVG IAAAAAGPMT AKTSTLTSCN QSHPLCGTAN ESPSTPEPRS RQPTTPQQQP HQQAHQQQQQ QQQLSSIANP MQKVNKRKET LEAKRERKAA KTLAIITGAF VVCWLPFFVM ALTMPLCAAC QISDSVASLF LWLGYFNSTL NPVIYTIFSP EFRQAFKRIL FGGHRPVHYR SGKL // ID 5HT2B_DROME STANDARD; PRT; 617 AA. AC P28286; Q9V8Q3; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 3. DT 04-APR-2006, entry version 44. DE 5-hydroxytryptamine receptor 2B (5-HT receptor) (Serotonin receptor DE 2B). GN Name=5-HT1B; Synonyms=5HT-R2B; ORFNames=CG15113; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=92155185; PubMed=1310937; RA Saudou F., Boschert U., Amlaiky N., Plassat J.-L., Hen R.; RT "A family of Drosophila serotonin receptors with distinct RT intracellular signalling properties and expression patterns."; RL EMBO J. 11:7-17(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins which inhibit adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- CAUTION: Ref.1 sequence differs from that shown due to chimeric CC DNA sequence. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11490; CAA77571.1; ALT_SEQ; mRNA. DR EMBL; AE003797; AAF57610.4; -; Genomic_DNA. DR PIR; S19156; S19156. DR UniGene; Dm.2573; -. DR HSSP; P08913; 1HLL. DR Ensembl; CG15113; Drosophila melanogaster. DR FlyBase; FBgn0004572; 5-HT1B. DR GO; GO:0001586; F:5-HT1 receptor activity; NAS. DR GO; GO:0007198; P:serotonin receptor, adenylate cyclase inhib...; IDA. DR GO; GO:0007208; P:serotonin receptor, phospholipase C activat...; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Complete proteome; G-protein coupled receptor; Glycoprotein; Membrane; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 617 5-hydroxytryptamine receptor 2B. FT /FTId=PRO_0000068963. FT TOPO_DOM 1 95 Extracellular (Potential). FT TRANSMEM 96 116 1 (Potential). FT TOPO_DOM 117 128 Cytoplasmic (Potential). FT TRANSMEM 129 149 2 (Potential). FT TOPO_DOM 150 164 Extracellular (Potential). FT TRANSMEM 165 185 3 (Potential). FT TOPO_DOM 186 205 Cytoplasmic (Potential). FT TRANSMEM 206 226 4 (Potential). FT TOPO_DOM 227 256 Extracellular (Potential). FT TRANSMEM 257 277 5 (Potential). FT TOPO_DOM 278 534 Cytoplasmic (Potential). FT TRANSMEM 535 555 6 (Potential). FT TOPO_DOM 556 570 Extracellular (Potential). FT TRANSMEM 571 591 7 (Potential). FT TOPO_DOM 592 617 Cytoplasmic (Potential). FT CARBOHYD 31 31 N-linked (GlcNAc...) (Potential). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 58 58 N-linked (GlcNAc...) (Potential). FT DISULFID 163 242 By similarity. FT CONFLICT 61 61 I -> V (in Ref. 1). FT CONFLICT 332 332 T -> M (in Ref. 1). FT CONFLICT 424 424 L -> V (in Ref. 1). SQ SEQUENCE 617 AA; 67530 MW; DD0E1AB7706FD844 CRC64; MLKTVTTAMA AGDDDVPASI LEIELPAILL NESLFIELNG NLTQLVDTTS NLSQIVWNRS INGNGNSNTF DLVDDEQERA AVEFWLLVKM IAMAVVLGLM ILVTIIGNVF VIAAIILERN LQNVANYLVA SLAVADLFVA CLVMPLGAVY EISNGWILGP ELCDIWTSCD VLCCTASILH LVAIAADRYW TVTNIDYNNL RTPRRVFLMI FCVWFAALIV SLAPQFGWKD PDYMKRIEEQ HCMVSQDVGY QIFATCCTFY VPLLVILFLY WKIYIIARKR IQRRAQKSFN VTLTETDCDS AVRELKKERS KRRAERKRLE AGERTPVDGD GTGGQLQRRT RKRMRICFGR NTNTANVVAG SEGAVARSMA AIAVDFASLA ITREETEFST SNYDNKSHAG TELTTVSSDA DDYRTSNANE IITLSQQVAH ATQHHLIASH LNAITPLAQS IAMGGVGCLT TTTPSEKALS GAGTVAGAVA GGSGSGSGEE GAGTEGKNAG VGLGGVLASI ANPHQKLAKR RQLLEAKRER KAAQTLAIIT GAFVICWLPF FVMALTMSLC KECEIHTAVA SLFLWLGYFN STLNPVIYTI FNPEFRRAFK RILFGRKAAA RARSAKI // ID 5HTR_LYMST STANDARD; PRT; 509 AA. AC Q25414; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 07-FEB-2006, entry version 29. DE 5-hydroxytryptamine receptor (5-HT receptor) (Serotonin receptor). OS Lymnaea stagnalis (Great pond snail). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Pulmonata; Basommatophora; OC Lymnaeoidea; Lymnaeidae; Lymnaea. OX NCBI_TaxID=6523; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93126323; PubMed=8093556; RA Sugamori K.S., Sunahara R.K., Guan H.-C., Bulloch A.G., Tensen C.P., RA Seeman P., Niznik H.B., van Tol H.H.; RT "Serotonin receptor cDNA cloned from Lymnaea stagnalis."; RL Proc. Natl. Acad. Sci. U.S.A. 90:11-15(1993). CC -!- FUNCTION: This is a receptor for 5-hydroxytryptamine (serotonin), CC a biogenic hormone that function as a neurotransmitter, a hormone, CC and a mitogen. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L06803; AAA29290.1; -; mRNA. DR PIR; A47174; A47174. DR HSSP; P08913; 1HLL. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 509 5-hydroxytryptamine receptor. FT /FTId=PRO_0000068987. FT TOPO_DOM 1 99 Extracellular (Potential). FT TRANSMEM 100 122 1 (Potential). FT TOPO_DOM 123 132 Cytoplasmic (Potential). FT TRANSMEM 133 154 2 (Potential). FT TOPO_DOM 155 169 Extracellular (Potential). FT TRANSMEM 170 191 3 (Potential). FT TOPO_DOM 192 210 Cytoplasmic (Potential). FT TRANSMEM 211 233 4 (Potential). FT TOPO_DOM 234 259 Extracellular (Potential). FT TRANSMEM 260 281 5 (Potential). FT TOPO_DOM 282 432 Cytoplasmic (Potential). FT TRANSMEM 433 456 6 (Potential). FT TOPO_DOM 457 465 Extracellular (Potential). FT TRANSMEM 466 488 7 (Potential). FT TOPO_DOM 489 509 Cytoplasmic (Potential). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT CARBOHYD 47 47 N-linked (GlcNAc...) (Potential). FT CARBOHYD 58 58 N-linked (GlcNAc...) (Potential). FT CARBOHYD 68 68 N-linked (GlcNAc...) (Potential). FT CARBOHYD 72 72 N-linked (GlcNAc...) (Potential). FT CARBOHYD 78 78 N-linked (GlcNAc...) (Potential). FT DISULFID 168 246 By similarity. SQ SEQUENCE 509 AA; 56902 MW; D283696C8C50B1B8 CRC64; MANFTFGDLA LDVARMGGLA STPSGLRSTG LTTPGLSPTG LVTSDFNDSY GLTGQFINGS HSSRSRDNAS ANDTSATNMT DDRYWSLTVY SHEHLVLTSV ILGLFVLCCI IGNCFVIAAV MLERSLHNVA NYLILSLAVA DLMVAVLVMP LSVVSEISKV WFLHSEVCDM WISVDVLCCT ASILHLVAIA MDRYWAVTSI DYIRRRSARR ILLMIMVVWI VALFISIPPL FGWRDPNNDP DKTGTCIISQ DKGYTIFSTV GAFYLPMLVM MIIYIRIWLV ARSRIRKDKF QMTKARLKTE ETTLVASPKT EYSVVSDCNG CNSPDSTTEK KKRRAPFKSY GCSPRPERKK NRAKKLPENA NGVNSNSSSS ERLKQIQIET AEAFANGCAE EASIAMLERQ CNNGKKISSN DTPYSRTREK LELKRERKAA RTLAIITGAF LICWLPFFII ALIGPFVDPE GIPPFARSFV LWLGYFNSLL NPIIYTIFSP EFRSAFQKIL FGKYRRGHR // ID 5HT5B_MOUSE STANDARD; PRT; 370 AA. AC P31387; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 18-APR-2006, entry version 48. DE 5-hydroxytryptamine 5B receptor (5-HT-5B) (Serotonin receptor 5B). GN Name=Htr5b; Synonyms=5ht5b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=93196607; PubMed=8450829; RA Matthes H., Boschert U., Amlaiky N., Grailhe R., Plassat J.-L., RA Muscatelli F., Mattei M.-G., Hen R.; RT "Mouse 5-hydroxytryptamine5A and 5-hydroxytryptamine5B receptors RT define a new family of serotonin receptors: cloning, functional RT expression, and chromosomal localization."; RL Mol. Pharmacol. 43:313-319(1993). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins. Probably involved in CC anxiety and depression. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in the central nervous CC system; in the hippocampus, habenula, and the doral raphe. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X69867; CAA49501.1; -; mRNA. DR PIR; I48231; I48231. DR UniGene; Mm.4833; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSMUSG00000050534; Mus musculus. DR MGI; MGI:96284; Htr5b. DR LinkHub; P31387; -. DR InterPro; IPR000431; 5HT5B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00519; 5HT5BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 370 5-hydroxytryptamine 5B receptor. FT /FTId=PRO_0000068972. FT TOPO_DOM 1 52 Extracellular (Potential). FT TRANSMEM 53 75 1 (Potential). FT TOPO_DOM 76 90 Cytoplasmic (Potential). FT TRANSMEM 91 111 2 (Potential). FT TOPO_DOM 112 128 Extracellular (Potential). FT TRANSMEM 129 150 3 (Potential). FT TOPO_DOM 151 171 Cytoplasmic (Potential). FT TRANSMEM 172 194 4 (Potential). FT TOPO_DOM 195 211 Extracellular (Potential). FT TRANSMEM 212 232 5 (Potential). FT TOPO_DOM 233 295 Cytoplasmic (Potential). FT TRANSMEM 296 316 6 (Potential). FT TOPO_DOM 317 333 Extracellular (Potential). FT TRANSMEM 334 354 7 (Potential). FT TOPO_DOM 355 370 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT DISULFID 127 205 By similarity. SQ SEQUENCE 370 AA; 41201 MW; 0553C62B12DAAD84 CRC64; MEVSNLSGAT PGLAFPPGPE SCSDSPSSGR SMGSTPGGLI LPGREPPFSA FTVLVVTLLV LLIAATFLWN LLVLVTILRV RAFHRVPHNL VASTAVSDVL VAVLVMPLSL VSELSAGRRW QLGRSLCHVW ISFDVLCCTA SIWNVAAIAL DRYWTITRHL QYTLRTRSRA SALMIAITWA LSALIALAPL LFGWGEAYDA RLQRCQVSQE PSYAVFSTCG AFYLPLAVVL FVYWKIYKAA KFRFGRRRRA VVPLPATTQA KEAPPESEMV FTARRRATVT FQTSGDSWRE QKEKRAAMMV GILIGVFVLC WIPFFLTELI SPLCACSLPP IWKSIFLWLG YSNSFFNPLI YTAFNKNYNN AFKSLFTKQR // ID GPR18_BALAM STANDARD; PRT; 379 AA. AC Q93127; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 07-MAR-2006, entry version 47. DE Probable G-protein coupled receptor No18. OS Balanus amphitrite (Barnacle). OC Eukaryota; Metazoa; Arthropoda; Crustacea; Maxillopoda; Cirripedia; OC Thoracica; Sessilia; Balanidae; Balanus. OX NCBI_TaxID=32267; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Darwin; RX MEDLINE=97183669; PubMed=9031635; DOI=10.1016/S0378-1119(96)00608-7; RA Kawahara H., Isoai A., Shizuri Y.; RT "Molecular cloning of a putative serotonin receptor gene from RT barnacle, Balanus amphitrite."; RL Gene 184:245-250(1997). CC -!- FUNCTION: Probable G-protein coupled receptor for an amine. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D83547; BAA12013.1; -; Genomic_DNA. DR PIR; JC6178; JC6178. DR HSSP; P08913; 1HLL. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR002002; Octopmn_rcpt. DR PANTHER; PTHR19266:SF124; Octopmn_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00664; OCTOPAMINER. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 379 Probable G-protein coupled receptor No18. FT /FTId=PRO_0000069660. FT TOPO_DOM 5 36 Extracellular (Potential). FT TRANSMEM 37 58 1 (Potential). FT TOPO_DOM 59 68 Cytoplasmic (Potential). FT TRANSMEM 69 90 2 (Potential). FT TOPO_DOM 91 107 Extracellular (Potential). FT TRANSMEM 108 128 3 (Potential). FT TOPO_DOM 129 148 Cytoplasmic (Potential). FT TRANSMEM 149 171 4 (Potential). FT TOPO_DOM 172 196 Extracellular (Potential). FT TRANSMEM 197 218 5 (Potential). FT TOPO_DOM 219 303 Cytoplasmic (Potential). FT TRANSMEM 304 325 6 (Potential). FT TOPO_DOM 326 340 Extracellular (Potential). FT TRANSMEM 341 362 7 (Potential). FT TOPO_DOM 363 375 Cytoplasmic (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT DISULFID 105 184 By similarity. SQ SEQUENCE 379 AA; 42373 MW; DBD483758BA953C2 CRC64; MSGGEASITG RTAPELNASA APLDDERELG ETVAATALLL AIILVTIVGN SLVIISVFTY RPLRSVQNFF VVSLAVADLT VALFVLPLNV AYRLLNQWLL GSYLCQMWLT CDILCCTSSI LNLCVIALDR YWAITDPINY AQKRTIRRVN TMIAAVWALS LVISVPPLLG WNDWPAQFTE DTPCTLTQER LFVVYSSSGS FFIPLIIMSV VYAKIFFATK RRLRERTRKL GTLAVPAPPQ RTSSRPLAEL ESVASQEDET EPSPEPEPLS SRADKPANGI SVHQFIEEKQ RISLSKERKA ARVLGVIMGV FVVCWLPFFL MYAIVPFCTN CAPPSQRVVD FVTWLGYVNS SLNPIIYTIY NKDFRTAFSR LLRCDRRMS // ID OAR_BOMMO STANDARD; PRT; 479 AA. AC Q17232; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 07-MAR-2006, entry version 36. DE Octopamine receptor. OS Bombyx mori (Silk moth). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Bombycidae; Bombyx. OX NCBI_TaxID=7091; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Antenna; RX MEDLINE=97166608; PubMed=9014328; DOI=10.1016/S0965-1748(96)00031-8; RA von Nickisch-Rosenegk E., Krieger J., Kubick S., Laage R., Strobel J., RA Strotmann J., Breer H.; RT "Cloning of biogenic amine receptors from moths (Bombyx mori and RT Heliothis virescens)."; RL Insect Biochem. Mol. Biol. 26:817-827(1996). CC -!- FUNCTION: Receptor for octopamine. Octopamine (OA) is a CC neurotransmitter, neurohormone, and neuromodulator in CC invertebrates. The activity of this receptor is mediated by G CC proteins which activate adenylyl cyclase (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X95607; CAA64865.1; -; mRNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR002002; Octopmn_rcpt. DR PANTHER; PTHR19266:SF124; Octopmn_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00664; OCTOPAMINER. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 479 Octopamine receptor. FT /FTId=PRO_0000069952. FT TOPO_DOM 1 57 Extracellular (Potential). FT TRANSMEM 58 80 1 (Potential). FT TOPO_DOM 81 90 Cytoplasmic (Potential). FT TRANSMEM 91 112 2 (Potential). FT TOPO_DOM 113 129 Extracellular (Potential). FT TRANSMEM 130 150 3 (Potential). FT TOPO_DOM 151 170 Cytoplasmic (Potential). FT TRANSMEM 171 193 4 (Potential). FT TOPO_DOM 194 218 Extracellular (Potential). FT TRANSMEM 219 240 5 (Potential). FT TOPO_DOM 241 407 Cytoplasmic (Potential). FT TRANSMEM 408 429 6 (Potential). FT TOPO_DOM 430 441 Extracellular (Potential). FT TRANSMEM 442 462 7 (Potential). FT TOPO_DOM 463 479 Cytoplasmic (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 16 16 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 479 AA; 54518 MW; CADA024567EC3620 CRC64; MGQAATHDAN NYTSINYTEI YDVIEDEKDV CAVADEPNIP CSFGISLAVP EWEAICTAII LTMIIISTVV GNILVILSVF TYKPLRIVQN FFIVSLAVAD LTVAILVLPL NVAYSILGQW VFGIYVCKMW LTCDIMCCTS SILNLCAIAL DRYWAITDPI NYAQKRTLER VLFMIGIVWI LSLVISSPPL LGWNDWPEVF EPDTPCRLTS QPGFVIFSSS GSFYIPLVIM TVVYFEIYLA TKKRLRDRAK ATKISTISSG RNKYETKESD PNDQDSVSSD ANPNEHQGGT RLVAENEKKH RTRKLTPKKK PKRRYWSKDD KSHNKLIIPI LSNENSVTDI GENLENRNTS SESNSKETHE DNMIEITEAA PVKIQKRPKQ NQTNAVYQFI EEKQRISLTR ERRAARTLGI IMGVFVVCWL PFFVIYLVIP FCVSCCLSNK FINFITWLGY VNSALNPLIY TIFNMDFRRA FKKLLFIKC // ID ADRA2_LABOS STANDARD; PRT; 432 AA. AC Q91081; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 21-MAR-2006, entry version 33. DE Alpha-2 adrenergic receptor (Alpha-2 adrenoceptor) (Alpha-2 DE adrenoreceptor). OS Labrus ossifagus (Cuckoo wrasse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei; OC Labridae; Labrus. OX NCBI_TaxID=30800; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=94035926; PubMed=7693288; RA Svensson S.P.S., Bailey T.J., Pepperl D.J., Grundstroem N., RA Ala-Uotila S., Scheinin M., Karlsson J.O.G., Regan J.W.; RT "Cloning and expression of a fish alpha 2-adrenoceptor."; RL Br. J. Pharmacol. 110:54-60(1993). CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- CC induced inhibition of adenylate cyclase through the action of G CC proteins. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U07743; AAA17386.1; -; Unassigned_DNA. DR PIR; I50829; I50829. DR HSSP; P08913; 1HLL. DR InterPro; IPR000735; Adren_rcpt_A2C. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00560; ADRENRGCA2CR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 432 Alpha-2 adrenergic receptor. FT /FTId=PRO_0000069110. FT TOPO_DOM 1 32 Extracellular (Potential). FT TRANSMEM 33 57 1 (Potential). FT TOPO_DOM 58 69 Cytoplasmic (Potential). FT TRANSMEM 70 95 2 (Potential). FT TOPO_DOM 96 105 Extracellular (Potential). FT TRANSMEM 106 128 3 (Potential). FT TOPO_DOM 129 149 Cytoplasmic (Potential). FT TRANSMEM 150 172 4 (Potential). FT TOPO_DOM 173 188 Extracellular (Potential). FT TRANSMEM 189 212 5 (Potential). FT TOPO_DOM 213 356 Cytoplasmic (Potential). FT TRANSMEM 357 380 6 (Potential). FT TOPO_DOM 381 393 Extracellular (Potential). FT TRANSMEM 394 413 7 (Potential). FT TOPO_DOM 414 432 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 18 18 N-linked (GlcNAc...) (Potential). FT DISULFID 105 183 By similarity. SQ SEQUENCE 432 AA; 48563 MW; 0A42FAF9849FA8BA CRC64; MDPLNATGMD AFTAIHLNAS WSADSGYSLA AIASIAALVS FLILFTVVGN ILVVIAVLTS RALKAPQNLF LVSLATADIL VATLVMPFSL ANELMGYWYF GKVWCGIYLA LDVLFCTSSI VHLCAISLDR YWSVTQAVEY NLKRTPKRVK CIIVIVWLIS AFISSPPLLS IDSNNYISSQ PQCMLNDDTW YILSSSMASF FAPCLIMILV YIRIYQVAKT RTRSMSGKEP RPDGVTQTEN GLNKANSPCH GDRENGHCQC PPTPSQRTVT IGQQTDDADM DESFSSEGKG HKPQRQDSQR AKRPGLKKSS ISKQSARISR VSNKSVDLFA SRRKRRRSSI AEKKVSQARE KRFTFVLAVV MGVFVVCWFP FFFSYSLHAV CRDYCKIPDT LFKFFWIGYC NSSLNPAIYT IFNRDFRRAF QKILCKSWKK SF // ID ADA2C_DIDMA STANDARD; PRT; 469 AA. AC P35405; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 21-MAR-2006, entry version 37. DE Alpha-2C adrenergic receptor (Alpha-2C adrenoceptor) (Alpha-2C DE adrenoreceptor). GN Name=ADRA2C; OS Didelphis marsupialis virginiana (North American opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Didelphis. OX NCBI_TaxID=9267; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX MEDLINE=94158793; PubMed=7509437; RA Blaxall H.S., Cerutis D., Hass N.A., Iversen L.J., Bylund D.B.; RT "Cloning and expression of the alpha 2C-adrenergic receptor from the RT OK cell line."; RL Mol. Pharmacol. 45:176-181(1994). RN [2] RP SEQUENCE REVISION TO 60; 75; 110; 143; 326-332; 365 AND 432. RA Bylund D.B.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- CC induced inhibition of adenylate cyclase through the action of G CC proteins. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U04310; AAA17566.2; -; mRNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR000735; Adren_rcpt_A2C. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00560; ADRENRGCA2CR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphorylation; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 469 Alpha-2C adrenergic receptor. FT /FTId=PRO_0000069104. FT TOPO_DOM 1 41 Extracellular (Potential). FT TRANSMEM 42 62 1 (Potential). FT TOPO_DOM 63 72 Cytoplasmic (Potential). FT TRANSMEM 73 93 2 (Potential). FT TOPO_DOM 94 109 Extracellular (Potential). FT TRANSMEM 110 130 3 (Potential). FT TOPO_DOM 131 154 Cytoplasmic (Potential). FT TRANSMEM 155 175 4 (Potential). FT TOPO_DOM 176 195 Extracellular (Potential). FT TRANSMEM 196 216 5 (Potential). FT TOPO_DOM 217 386 Cytoplasmic (Potential). FT TRANSMEM 387 407 6 (Potential). FT TOPO_DOM 408 427 Extracellular (Potential). FT TRANSMEM 428 448 7 (Potential). FT TOPO_DOM 449 469 Cytoplasmic (Potential). FT COMPBIAS 274 293 His-rich (basic). FT SITE 116 116 Implicated in ligand binding (By FT similarity). FT SITE 199 199 Implicated in catechol agonist binding FT and receptor activation (By similarity). FT SITE 203 203 Implicated in catechol agonist binding FT and receptor activation (By similarity). FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 20 20 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. SQ SEQUENCE 469 AA; 53223 MW; 6F97D3718CC15C18 CRC64; MDLQLTTNST DSGDRGGSSN ESLQRQPPSQ YSPAEVAGLA AVVSFLIVFT IVGNVLVVIA VLTSRALKAP QNLFQVSLAS ADILVATLVM PFSLANELMN YWYFGKVWCV IYLALDVLFC TSSIVHLCAI SLDRYWSVTQ AVEYNLKRTP RRIKGIIVTV WLISAVISFP PLISLYRDPE DDLYPQCELN DETWYILSSC IGSFFAPCII MVLVYVRIYR VAKLRTRTLS EKRTVPEGSS QTENGLSRPP VGAGPSTAAA AAASLRLQAG ENGHYHLHHH HHHLHHHHHH HHHQLRKSAE LEDIELEESS TSENRRRRRS REEAAARKGS RGFSFSFSST KGGQSAGAGS RLSRASNRSL EFFSTHRRRK RSSLCRRKVT QAREKRFTFV LAVVMGVFVV CWFPFFFTYS LYGICREACQ VPETLFKFFF WIGYCNSSLN PVIYTIFNQD FRRSFKHILF KKKKKTSLQ // ID ADA2A_HUMAN STANDARD; PRT; 450 AA. AC P08913; Q2XN99; Q86TH8; Q9BZK1; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 3. DT 18-APR-2006, entry version 77. DE Alpha-2A adrenergic receptor (Alpha-2A adrenoceptor) (Alpha-2A DE adrenoreceptor) (Alpha-2AAR) (Alpha-2 adrenergic receptor subtype DE C10). GN Name=ADRA2A; Synonyms=ADRA2R, ADRAR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89308571; PubMed=2568356; RA Fraser C.M., Arakawa S., McCombie W.R., Venter J.C.; RT "Cloning, sequence analysis, and permanent expression of a human alpha RT 2-adrenergic receptor in Chinese hamster ovary cells. Evidence for RT independent pathways of receptor coupling to adenylate cyclase RT attenuation and activation."; RL J. Biol. Chem. 264:11754-11761(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Platelet; RX MEDLINE=88042789; PubMed=2823383; RA Kobilka B.K., Matsui H., Kobilka T.S., Yang-Feng T.L., Francke U., RA Caron M.G., Lefkowitz R.J., Regan J.W.; RT "Cloning, sequencing, and expression of the gene coding for the human RT platelet alpha 2-adrenergic receptor."; RL Science 238:650-656(1987). RN [3] RP SEQUENCE REVISION TO 333-365. RX MEDLINE=91009167; PubMed=2170371; RA Guyer C.A., Horstman D.A., Wilson A.L., Clark J.D., Kragoe E.J. Jr., RA Limbird L.E.; RT "Cloning, sequencing, and expression of the gene encoding the porcine RT alpha 2-adrenergic receptor. Allosteric modulation by Na+, H+, and RT amiloride analogs."; RL J. Biol. Chem. 265:17307-17317(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Castellano M., Giacche' M., Rossi F., Rivadossi F., Perani C., RA Beschi M., Agabiti Rosei E.; RT "A search for genetic variability in the human alpha-2 adrenergic RT receptor on chromosome 10."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-251. RX PubMed=10948191; DOI=10.1074/jbc.M004550200; RA Small K.M., Forbes S.L., Brown K.M., Liggett S.B.; RT "An Asn to Lys polymorphism in the third intracellular loop of the RT human alpha 2A-adrenergic receptor imparts enhanced agonist-promoted RT Gi coupling."; RL J. Biol. Chem. 275:38518-38523(2000). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Mao Z.-M., Tang K., Li B.-M., Jing N.-H.; RT "Cloning and expression of human alpha-2A adrenergic receptor in SY5Y RT cells."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Liu L., Yuan L.; RT "Human alpha-2A adrenergic receptor gene and the genotype of -1296 RT nucleotide and motionsickness."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-251. RA Rieder M.J., Johanson E.J., da Ponte S.H., Hastings N.C., Ahearn M.O., RA Bertucci C.B., Wong M.W., Yi Q., Nickerson D.A.; RT "SeattleSNPs. NHLBI HL66682 program for genomic applications, UW- RT FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu)."; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=PNS, and Testis; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [11] RP NUCLEOTIDE SEQUENCE OF 77-209. RX MEDLINE=91192139; PubMed=1849485; DOI=10.1016/0014-5793(91)80301-I; RA Chhajlani V., Rangel N., Uhlen S., Wikberg J.E.S.; RT "Identification of an additional gene belonging to the alpha 2 RT adrenergic receptor family in the human genome by PCR."; RL FEBS Lett. 280:241-244(1991). RN [12] RP MUTAGENESIS OF PHE-412. RX MEDLINE=91332079; PubMed=1678390; RA Suryanarayana S., Daunt D.A., von Zastrow M., Kobilka B.K.; RT "A point mutation in the seventh hydrophobic domain of the alpha 2 RT adrenergic receptor increases its affinity for a family of beta RT receptor antagonists."; RL J. Biol. Chem. 266:15488-15492(1991). RN [13] RP MUTAGENESIS OF ASPARTIC ACID AND SERINE RESIDUES. RX MEDLINE=91342598; PubMed=1678850; RA Wang C.-D., Buck M.A., Fraser C.M.; RT "Site-directed mutagenesis of alpha 2a-adrenergic receptors: RT Identification of amino acids involved in ligand binding and receptor RT activation by agonists."; RL Mol. Pharmacol. 40:168-179(1991). RN [14] RP STRUCTURE BY NMR OF 118-149. RX MEDLINE=21885815; PubMed=11888275; DOI=10.1021/bi015811+; RA Chung D.A., Zuiderweg E.R., Fowler C.B., Soyer O.S., Mosberg H.I., RA Neubig R.R.; RT "NMR structure of the second intracellular loop of the alpha 2A RT adrenergic receptor: evidence for a novel cytoplasmic helix."; RL Biochemistry 41:3596-3604(2002). CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- CC induced inhibition of adenylate cyclase through the action of G CC proteins. The rank order of potency for agonists of this receptor CC is oxymetazoline > clonidine > epinephrine > norepinephrine > CC phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin = CC p-octopamine. For antagonists, the rank order is yohimbine > CC phentolamine = mianserine > chlorpromazine = spiperone = prazosin CC > propanolol > alprenolol = pindolol. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M23533; AAA51665.1; -; Genomic_DNA. DR EMBL; M18415; AAA51664.1; -; Genomic_DNA. DR EMBL; AF262016; AAG00447.2; -; Genomic_DNA. DR EMBL; AF281308; AAF91441.1; -; Genomic_DNA. DR EMBL; AF316894; AAK01634.1; -; Genomic_DNA. DR EMBL; AF284095; AAK26743.1; -; mRNA. DR EMBL; AY032736; AAK51162.1; -; Genomic_DNA. DR EMBL; DQ285607; ABB72683.1; -; Genomic_DNA. DR EMBL; AL158163; CAH72817.1; -; Genomic_DNA. DR EMBL; BC035047; AAH35047.1; -; mRNA. DR EMBL; BC050414; AAH50414.2; -; mRNA. DR PIR; A34169; A34169. DR UniGene; Hs.249159; -. DR PDB; 1HLL; NMR; A=118-149. DR PDB; 1HO9; NMR; A=118-149. DR PDB; 1HOD; NMR; A=118-149. DR PDB; 1HOF; NMR; A=118-149. DR Ensembl; ENSG00000150594; Homo sapiens. DR HGNC; HGNC:281; ADRA2A. DR MIM; 104210; gene. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; TAS. DR GO; GO:0015459; F:potassium channel regulator activity; TAS. DR GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; TAS. DR GO; GO:0000187; P:activation of MAPK activity; TAS. DR GO; GO:0006928; P:cell motility; TAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS. DR GO; GO:0007194; P:negative regulation of adenylate cyclase ac...; TAS. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS. DR GO; GO:0007265; P:Ras protein signal transduction; TAS. DR GO; GO:0007266; P:Rho protein signal transduction; TAS. DR GO; GO:0007165; P:signal transduction; TAS. DR InterPro; IPR001946; Adren_rcpt_A2Aa. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00558; ADRENRGCA2AR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW 3D-structure; Direct protein sequencing; G-protein coupled receptor; KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphorylation; KW Polymorphism; Receptor; Transducer; Transmembrane. FT CHAIN 1 450 Alpha-2A adrenergic receptor. FT /FTId=PRO_0000069080. FT TOPO_DOM 1 33 Extracellular (Potential). FT TRANSMEM 34 59 1 (Potential). FT TOPO_DOM 60 70 Cytoplasmic (Potential). FT TRANSMEM 71 96 2 (Potential). FT TOPO_DOM 97 106 Extracellular (Potential). FT TRANSMEM 107 129 3 (Potential). FT TOPO_DOM 130 149 Cytoplasmic (Potential). FT TRANSMEM 150 173 4 (Potential). FT TOPO_DOM 174 192 Extracellular (Potential). FT TRANSMEM 193 217 5 (Potential). FT TOPO_DOM 218 374 Cytoplasmic (Potential). FT TRANSMEM 375 399 6 (Potential). FT TOPO_DOM 400 406 Extracellular (Potential). FT TRANSMEM 407 430 7 (Potential). FT TOPO_DOM 431 450 Cytoplasmic (Potential). FT SITE 113 113 Implicated in ligand binding. FT SITE 200 200 Implicated in catechol agonist binding FT and receptor activation. FT SITE 204 204 Implicated in catechol agonist binding FT and receptor activation. FT LIPID 442 442 S-palmitoyl cysteine (By similarity). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). FT DISULFID 106 188 By similarity. FT VARIANT 251 251 N -> K (rare polymorphism; frequency in FT Caucasians 0.004 and in African-Americans FT 0.05; 40% increase in agonist-promoted Gi FT coupling; dbSNP:1800035). FT /FTId=VAR_014957. FT MUTAGEN 79 79 D->N: No change in binding affinity. FT eliminates guanine nucleotide-sensitive FT agonist binding. FT MUTAGEN 113 113 D->N: No binding to yohimbine. Increase FT in adenylate cyclase activity. FT MUTAGEN 130 130 D->N: Lower affinity for agonists. FT Eliminates guanine nucleotide-sensitive FT agonist binding. FT MUTAGEN 200 200 S->A: Lower affinity for agonists. No FT change in guanine nucleotide-sensitive FT agonist binding. FT MUTAGEN 204 204 S->A: Lower affinity for agonists. FT Reduced guanine nucleotide-sensitive FT agonist binding. FT MUTAGEN 412 412 F->N: 350-fold reduced affinity for FT alpha-2 antagonist yohimbine, 3000-fold FT increase for beta-antagonist alprenolol. FT CONFLICT 104 104 A -> T (in Ref. 2). FT CONFLICT 124 124 L -> P (in Ref. 11). FT CONFLICT 157 157 V -> C (in Ref. 2). FT CONFLICT 333 365 PRRGPGATGIGTPAAGPGEERVGAAKASRWRGR -> RGAG FT RGRRGSGRRLQGRGRSASGLPRRRAGAGG (in Ref. 1 FT and 2). FT CONFLICT 368 368 R -> L (in Ref. 2). FT HELIX 119 128 FT TURN 129 129 FT HELIX 130 139 FT HELIX 140 142 SQ SEQUENCE 450 AA; 48957 MW; A703CF262F04E8AC CRC64; MGSLQPDAGN ASWNGTEAPG GGARATPYSL QVTLTLVCLA GLLMLLTVFG NVLVIIAVFT SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY FGKAWCEIYL ALDVLFCTSS IVHLCAISLD RYWSITQAIE YNLKRTPRRI KAIIITVWVI SAVISFPPLI SIEKKGGGGG PQPAEPRCEI NDQKWYVISS CIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDAVA APPGGTERRP NGLGPERSAG PGGAEAEPLP TQLNGAPGEP APAGPRDTDA LDLEESSSSD HAERPPGPRR PERGPRGKGK ARASQVKPGD SLPRRGPGAT GIGTPAAGPG EERVGAAKAS RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLTAVG CSVPRTLFKF FFWFGYCNSS LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV // ID ADA2B_BRARE STANDARD; PRT; 510 AA. AC Q90WY5; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 04-APR-2006, entry version 25. DE Alpha-2B adrenergic receptor (Alpha-2B adrenoceptor) (Alpha-2B DE adrenoreceptor) (Alpha(2B)AR). GN Name=adra2b; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12949138; DOI=10.1093/molbev/msg224; RA Ruuskanen J.O., Xhaard H., Marjamaki A., Salaneck E., Salminen T., RA Yan Y.-L., Postlethwait J.H., Johnson M.S., Larhammar D., Scheinin M.; RT "Identification of duplicated fourth alpha2-adrenergic receptor RT subtype by cloning and mapping of five receptor genes in zebrafish."; RL Mol. Biol. Evol. 21:14-28(2004). RN [2] RP FUNCTION, AND 3D-STRUCTURE MODELING. RX PubMed=15655522; DOI=10.1038/sj.bjp.0706057; RA Ruuskanen J.O., Laurila J., Xhaard H., Rantanen V.-V., Vuoriluoto K., RA Wurster S., Marjamaki A., Vainio M., Johnson M.S., Scheinin M.; RT "Conserved structural, pharmacological and functional properties among RT the three human and five zebrafish alpha2-adrenoceptors."; RL Br. J. Pharmacol. 144:165-177(2005). CC -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- CC induced inhibition of adenylate cyclase through the action of G CC proteins. The order of potency for this receptor is norepinephrine CC > epinephrine. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY048970; AAL07509.1; -; Genomic_DNA. DR UniGene; Dr.45849; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSDARG00000019819; Danio rerio. DR ZFIN; ZDB-GENE-021010-2; adra2b. DR GO; GO:0005887; C:integral to plasma membrane; IC. DR GO; GO:0004938; F:alpha2-adrenergic receptor activity; IDA. DR GO; GO:0007194; P:negative regulation of adenylate cyclase ac...; IDA. DR InterPro; IPR000207; Adren_rcpt_A2B. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00559; ADRENRGCA2BR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 510 Alpha-2B adrenergic receptor. FT /FTId=PRO_0000069102. FT TOPO_DOM 1 41 Extracellular (Potential). FT TRANSMEM 42 67 1 (Potential). FT TOPO_DOM 68 78 Cytoplasmic (Potential). FT TRANSMEM 79 104 2 (Potential). FT TOPO_DOM 105 114 Extracellular (Potential). FT TRANSMEM 115 137 3 (Potential). FT TOPO_DOM 138 159 Cytoplasmic (Potential). FT TRANSMEM 160 184 4 (Potential). FT TOPO_DOM 185 200 Extracellular (Potential). FT TRANSMEM 201 224 5 (Potential). FT TOPO_DOM 225 432 Cytoplasmic (Potential). FT TRANSMEM 433 456 6 (Potential). FT TOPO_DOM 457 465 Extracellular (Potential). FT TRANSMEM 466 489 7 (Potential). FT TOPO_DOM 490 510 Cytoplasmic (Potential). FT COMPBIAS 326 346 Lys-rich. FT SITE 121 121 Implicated in ligand binding (By FT similarity). FT SITE 207 207 Implicated in catechol agonist binding FT (By similarity). FT SITE 211 211 Implicated in catechol agonist binding FT (By similarity). FT LIPID 502 502 S-palmitoyl cysteine (Potential). FT CARBOHYD 16 16 N-linked (GlcNAc...) (Potential). FT CARBOHYD 27 27 N-linked (GlcNAc...) (Potential). FT DISULFID 114 195 By similarity. SQ SEQUENCE 510 AA; 55971 MW; 1CB07C0AFC6DE3D3 CRC64; MDSPCPVAVG LPGHTNGTGG TSSPTCNQSM IKLAPYSPEA TAAFATAITL MMLITIVGNI LVIIAVLTSR SLRGPQNLFL VSLAAADILV ATLIIPFSLA NELMGYWYFR SVWCEIYLAL DVLFCTSSIV HLCAISLDRY MSISRAVTYG PKRTPKRIKC AILVVWLISA VISFPPLLSM NKNKGGGESG ALPQCQLNDE RWYILYSTIG SFFAPCLIMI LVYMRIYQIA KQRTRCPPGE PRKEAPANAT TPQHKIQNGR GDETPGTLQK KARPPTLAVS QVESVQQAAN TPIANNLLQA PSTTLTPTTP CPSPSPSNSS EVAPSKSKEG KKEKKKKKNN KNKNKKEPDN NNGESMSSDS DTEQGGRGLE VPCTPTMTPS GIHSPATMQK YRDMIATAKG AKLVARKAKQ DGTPNSARRK AMVNREKRFT FVLAVVIGVF VICWFPFFFS YSLQAVCPES CALPEPLFKF FFWIGYCNSC LNPVIYTIFN KDFRRAFKKI LCKNTKGTFF // ID DRD2_BOVIN STANDARD; PRT; 444 AA. AC P20288; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 04-APR-2006, entry version 55. DE D(2) dopamine receptor (Dopamine D2 receptor). GN Name=DRD2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT). RX MEDLINE=90136899; PubMed=2137198; DOI=10.1038/343266a0; RA Chio C.L., Hess G.F., Graham R.S., Huff R.M.; RT "A second molecular form of D2 dopamine receptor in rat and bovine RT caudate nucleus."; RL Nature 343:266-269(1990). CC -!- FUNCTION: This is one of the five types (D1 to D5) of receptors CC for dopamine. The activity of this receptor is mediated by G CC proteins which inhibit adenylyl cyclase. CC -!- SUBUNIT: Interacts with neurabin-2, CADPS, CADPS2 and CLIC6 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P20288-1; Sequence=Displayed; CC Name=Short; CC IsoId=P20288-2; Sequence=VSP_001869; CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X51657; CAA35970.1; -; mRNA. DR PIR; S08163; DYBOD2. DR UniGene; Bt.4300; -. DR InterPro; IPR001922; Dopa_D2_rcpt. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00567; DOPAMINED2R. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Membrane; Receptor; Transducer; Transmembrane. FT CHAIN 1 444 D(2) dopamine receptor. FT /FTId=PRO_0000069384. FT TOPO_DOM 1 37 Extracellular (Potential). FT TRANSMEM 38 60 1 (Potential). FT TOPO_DOM 61 71 Cytoplasmic (Potential). FT TRANSMEM 72 97 2 (Potential). FT TOPO_DOM 98 108 Extracellular (Potential). FT TRANSMEM 109 130 3 (Potential). FT TOPO_DOM 131 151 Cytoplasmic (Potential). FT TRANSMEM 152 174 4 (Potential). FT TOPO_DOM 175 186 Extracellular (Potential). FT TRANSMEM 187 210 5 (Potential). FT TOPO_DOM 211 374 Cytoplasmic (Potential). FT TRANSMEM 375 398 6 (Potential). FT TOPO_DOM 399 406 Extracellular (Potential). FT TRANSMEM 407 430 7 (Potential). FT TOPO_DOM 431 444 Cytoplasmic (Potential). FT REGION 211 374 Interaction with neurabin-2 (By FT similarity). FT SITE 193 193 Implicated in catechol agonist binding FT (By similarity). FT SITE 194 194 Implicated in receptor activation (By FT similarity). FT SITE 197 197 Implicated in receptor activation (By FT similarity). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 23 23 N-linked (GlcNAc...) (Potential). FT DISULFID 107 182 By similarity. FT VARSPLIC 242 270 Missing (in isoform Short). FT /FTId=VSP_001869. SQ SEQUENCE 444 AA; 50672 MW; 67437197629301C7 CRC64; MDPLNLSWYD DDPESRNWSR PFNGSEGKAD RPPYNYYAML LTLLIFVIVF GNVLVCMAVS REKALQTTTN YLIVSLAVAD LLVATLVMPW VVYLEVVGEW KFSRIHCDIF VTLDVMMCTA SILNLCAISI DRYTAVAMPM LYNTRYSSKR RVTVMIAIVW VLSFTISCPM LFGLNNTDQN ECIIANPAFV VYSSIVSFYV PFIVTLLVYI KIYIVLRRRR KRVNTKRSSR AFRANLKAPL KGNCTHPEDM KLCTVIMKSN GSFPVNRRRV EAARRAQELE MEMLSSTSPP ERTRYSPIPP SHHQLTLPDP SHHGLHSTPD SPAKPEKNGH AKTVNPKIAK IFEIQSMPNG KTRTSLKTMS RRKLSQQKEK KATQMLAIVL GVFIICWLPF FITHILNIHC DCNIPPVLYS AFTWLGYVNS AVNPIIYTTF NIEFRKAFLK ILHC // ID DRD3_HUMAN STANDARD; PRT; 400 AA. AC P35462; Q4VBM8; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 18-APR-2006, entry version 55. DE D(3) dopamine receptor. GN Name=DRD3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX MEDLINE=91274966; PubMed=2129115; RA Giros B., Martres M.-P., Sokoloff P., Schwartz J.-C.; RT "Gene cloning of human dopaminergic D3 receptor and identification of RT its chromosome."; RL C. R. Acad. Sci. III, Sci. Vie 311:501-508(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Fishburn C.S., Park B.-H., Fuchs S.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RX MEDLINE=94022291; PubMed=8415635; RA Schmauss C., Haroutunian V., Davis K.L., Davidson M.; RT "Selective loss of dopamine D3-type receptor mRNA expression in RT parietal and motor cortices of patients with chronic schizophrenia."; RL Proc. Natl. Acad. Sci. U.S.A. 90:8942-8946(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RC TISSUE=Brain; RX MEDLINE=95050745; PubMed=7961889; RA Liu K., Bergson C., Levenson R., Schmauss C.; RT "On the origin of mRNA encoding the truncated dopamine D3-type RT receptor D3nf and detection of D3nf-like immunoreactivity in human RT brain."; RL J. Biol. Chem. 269:29220-29226(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-9. RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP VARIANT GLY-9. RA Lannfelt T., Sokoloff P., Martres M.-P., Pilon C., Giros B., RA Joensson E., Sedvall G., Schwartz J.-C.; RT "Amino-acid substitution in the dopamine D3 receptor as useful RT polymorphism for investigating psychiatric disorders."; RL Psychiatr. Genet. 2:249-256(1992). RN [7] RP VARIANT GLY-9. RX MEDLINE=97186429; PubMed=9034004; RX DOI=10.1002/(SICI)1096-8628(19970221)74:1<40::AID-AJMG9>3.0.CO;2-Z; RA Chen C.-H., Liu M.-Y., Wei F.-C., Koong F.-J., Hwu H.-G., Hsiao K.-J.; RT "Further evidence of no association between Ser9Gly polymorphism of RT dopamine D3 receptor gene and schizophrenia."; RL Am. J. Med. Genet. 74:40-43(1997). RN [8] RP VARIANT GLY-9. RX MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [9] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: This is one of the five types (D1 to D5) of receptors CC for dopamine. The activity of this receptor is mediated by G CC proteins which inhibit adenylyl cyclase. CC -!- SUBUNIT: Interacts with CLIC6 (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=D3; CC IsoId=P35462-1; Sequence=Displayed; CC Name=2; Synonyms=D3nf; CC IsoId=P35462-2; Sequence=VSP_001872; CC -!- TISSUE SPECIFICITY: Brain. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U32499; AAA73929.1; -; mRNA. DR EMBL; L20469; AAA03543.1; -; mRNA. DR EMBL; L35903; AAA64369.1; ALT_SEQ; Genomic_DNA. DR EMBL; L35902; AAA64369.1; JOINED; Genomic_DNA. DR EMBL; BC095510; AAH95510.1; -; mRNA. DR EMBL; A19667; CAA01483.1; -; Unassigned_DNA. DR PIR; A48258; A48258. DR PIR; G01977; G01977. DR UniGene; Hs.121478; -. DR Ensembl; ENSG00000151577; Homo sapiens. DR HGNC; HGNC:3024; DRD3. DR MIM; 126451; gene. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0004952; F:dopamine receptor activity; TAS. DR GO; GO:0007610; P:behavior; TAS. DR GO; GO:0007212; P:dopamine receptor signaling pathway; TAS. DR InterPro; IPR001620; DopaD3_rcpt. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00568; DOPAMINED3R. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; G-protein coupled receptor; Glycoprotein; KW Membrane; Polymorphism; Receptor; Transducer; Transmembrane. FT CHAIN 1 400 D(3) dopamine receptor. FT /FTId=PRO_0000069397. FT TOPO_DOM 1 32 Extracellular (Potential). FT TRANSMEM 33 55 1 (Potential). FT TOPO_DOM 56 66 Cytoplasmic (Potential). FT TRANSMEM 67 92 2 (Potential). FT TOPO_DOM 93 104 Extracellular (Potential). FT TRANSMEM 105 126 3 (Potential). FT TOPO_DOM 127 149 Cytoplasmic (Potential). FT TRANSMEM 150 172 4 (Potential). FT TOPO_DOM 173 185 Extracellular (Potential). FT TRANSMEM 186 209 5 (Potential). FT TOPO_DOM 210 329 Cytoplasmic (Potential). FT TRANSMEM 330 351 6 (Potential). FT TOPO_DOM 352 366 Extracellular (Potential). FT TRANSMEM 367 388 7 (Potential). FT TOPO_DOM 389 400 Cytoplasmic (Potential). FT CARBOHYD 12 12 N-linked (GlcNAc...) (Potential). FT CARBOHYD 19 19 N-linked (GlcNAc...) (Potential). FT CARBOHYD 97 97 N-linked (GlcNAc...) (Potential). FT CARBOHYD 173 173 N-linked (GlcNAc...) (Potential). FT DISULFID 103 181 By similarity. FT VARSPLIC 288 400 PTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKAT FT QMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHVSPELYSATT FT WLGYVNSALNPVIYTTFNIEFRKAFLKILSC -> ATSGEE FT GNPNGGHCAWGLHCLLAALLLDPCSQYPLPDMPRVPRALQC FT HDMAGLRE (in isoform 2). FT /FTId=VSP_001872. FT VARIANT 9 9 S -> G (in dbSNP:6280). FT /FTId=VAR_003463. FT CONFLICT 396 396 K -> L (in Ref. 5; AAH95510). SQ SEQUENCE 400 AA; 44225 MW; 2CDA789D78378DDA CRC64; MASLSQLSSH LNYTCGAENS TGASQARPHA YYALSYCALI LAIVFGNGLV CMAVLKERAL QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR ICCDVFVTLD VMMCTASILN LCAISIDRYT AVVMPVHYQH GTGQSSCRRV ALMITAVWVL AFAVSCPLLF GFNTTGDPTV CSISNPDFVI YSSVVSFYLP FGVTVLVYAR IYVVLKQRRR KRILTRQNSQ CNSVRPGFPQ QTLSPDPAHL ELKRYYSICQ DTALGGPGFQ ERGGELKREE KTRNSLSPTI APKLSLEVRK LSNGRLSTSL KLGPLQPRGV PLREKKATQM VAIVLGAFIV CWLPFFLTHV LNTHCQTCHV SPELYSATTW LGYVNSALNP VIYTTFNIEF RKAFLKILSC // ID DRD2L_DROME STANDARD; PRT; 506 AA. AC Q8IS44; Q59E80; Q59E81; Q59E82; Q6AWL2; Q8IS43; Q8IS45; Q9W5X7; AC Q9W5X8; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 04-APR-2006, entry version 22. DE Dopamine D2-like receptor (DD2R). GN Name=D2R; ORFNames=CG17004; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 461; 506 AND 606), FUNCTION, RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Head; RX MEDLINE=22295047; PubMed=12391323; DOI=10.1073/pnas.202498299; RA Hearn M.G., Ren Y., McBride E.W., Reveillaud I., Beinborn M., RA Kopin A.S.; RT "A Drosophila dopamine 2-like receptor: molecular characterization and RT identification of multiple alternatively spliced variants."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14554-14559(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Receptor for dopamine. The activity of this receptor is CC mediated by G proteins which inhibit adenylyl cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=506; Synonyms=D, DD2R-506; CC IsoId=Q8IS44-1; Sequence=Displayed; CC Name=606; Synonyms=C, DD2R-606; CC IsoId=Q8IS44-2; Sequence=VSP_050757; CC Note=Ref.1 (AAN15955) sequence is in conflict in positions: CC 440:D->E; CC Name=461; Synonyms=A, DD2R-461; CC IsoId=Q8IS44-3; Sequence=VSP_050756; CC Name=B; CC IsoId=Q8IS44-4; Sequence=VSP_015396, VSP_015397, VSP_015398; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highest expression is in adult heads. CC -!- DEVELOPMENTAL STAGE: Expressed in larva, pupae and adult. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY150862; AAN15955.1; -; mRNA. DR EMBL; AY150863; AAN15956.1; -; mRNA. DR EMBL; AY150864; AAN15957.1; -; mRNA. DR EMBL; AE002611; AAF45375.2; -; Genomic_DNA. DR EMBL; AE002611; AAX52462.1; -; Genomic_DNA. DR EMBL; AE002611; AAX52463.1; -; Genomic_DNA. DR EMBL; AE002611; AAX52464.1; -; Genomic_DNA. DR EMBL; BT015236; AAT94465.1; -; mRNA. DR UniGene; Dm.17266; -. DR HSSP; P08913; 1HLL. DR Ensembl; CG17004; Drosophila melanogaster. DR FlyBase; FBgn0053517; D2R. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004952; F:dopamine receptor activity; IDA. DR GO; GO:0007212; P:dopamine receptor signaling pathway; IDA. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; Complete proteome; G-protein coupled receptor; KW Glycoprotein; Membrane; Receptor; Transducer; Transmembrane. FT CHAIN 1 506 Dopamine D2-like receptor. FT /FTId=PRO_0000069395. FT TOPO_DOM 1 78 Extracellular (Potential). FT TRANSMEM 79 99 1 (Potential). FT TOPO_DOM 100 117 Cytoplasmic (Potential). FT TRANSMEM 118 138 2 (Potential). FT TOPO_DOM 139 151 Extracellular (Potential). FT TRANSMEM 152 172 3 (Potential). FT TOPO_DOM 173 194 Cytoplasmic (Potential). FT TRANSMEM 195 215 4 (Potential). FT TOPO_DOM 216 232 Extracellular (Potential). FT TRANSMEM 233 253 5 (Potential). FT TOPO_DOM 254 431 Cytoplasmic (Potential). FT TRANSMEM 432 452 6 (Potential). FT TOPO_DOM 453 470 Extracellular (Potential). FT TRANSMEM 471 491 7 (Potential). FT TOPO_DOM 492 506 Cytoplasmic (Potential). FT CARBOHYD 15 15 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 56 56 N-linked (GlcNAc...) (Potential). FT CARBOHYD 59 59 N-linked (GlcNAc...) (Potential). FT CARBOHYD 63 63 N-linked (GlcNAc...) (Potential). FT DISULFID 149 226 By similarity. FT VARSPLIC 1 132 Missing (in isoform B). FT /FTId=VSP_015396. FT VARSPLIC 133 137 AVYFL -> MSAPK (in isoform B). FT /FTId=VSP_015397. FT VARSPLIC 358 403 NVAMKPLSFVRYGVQEAMTLARNDSTLSTTSKTSSRKDKKN FT SQASR -> K (in isoform 461). FT /FTId=VSP_050756. FT VARSPLIC 358 358 N -> NSVVAQITTQPQLVVADPNGNHDSGYAASNVDDVLA FT GVAPASASAATSAAPRSSGSPPDSPLPSGATLQRSSVSSQR FT RPTGDESPKRGEPALRSVGVDNSS (in isoform FT 606). FT /FTId=VSP_050757. FT VARSPLIC 358 358 N -> NSVVAQITTQPQLVVADPNGNHDSGYAASNVDDVLA FT GVAPASASAATSAAPRSSGSPPDSPLPSGATLQRSSVSSQR FT RPTGDDSPKRGEPALS (in isoform B). FT /FTId=VSP_015398. SQ SEQUENCE 506 AA; 56478 MW; CF0EEA88BB0D3DC4 CRC64; MLLLENFNDY FPNYNGSTVS GTSTIAPGVA ITGSRGSGLL LEQNLTGLYL DGYRLNCTNE TLNLTDSCGE LRVVDHNYWA LILILFPILT LFGNILVILS VCRERSLQTV TNYFIVSLAI ADLLVAVVVM PFAVYFLVNG AWALPDVVCD FYIAMDVICS TSSIFNLVAI SIDRYIAVTQ PIKYAKHKNS RRVCLTILLV WAISAAIGSP IVLGLNNTPN REPDVCAFYN ADFILYSSLS SFYIPCIIMV FLYWNIFKAL RSRARKQRAA RKPHLSELTG GSVIENIAQT RRLAETALDS SRHASRILPD EAATNTASGS NEEEDENAIS PDIDDCHVIV NDKSTEFMLA TVVEETGNVA MKPLSFVRYG VQEAMTLARN DSTLSTTSKT SSRKDKKNSQ ASRFTIYKVH KASKKKREKS SAKKERKATK TLAIVLGVFL FCWLPFFSCN IMDAMCAKFK KDCRPGLTAY MMTTWLGYIN SFVNPVIYTI FNPEFRKAFK KIMHMG // ID OAR1_LYMST STANDARD; PRT; 638 AA. AC O77408; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 18-APR-2006, entry version 31. DE Octopamine receptor 1 (OA1). OS Lymnaea stagnalis (Great pond snail). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Pulmonata; Basommatophora; OC Lymnaeoidea; Lymnaeidae; Lymnaea. OX NCBI_TaxID=6523; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RC TISSUE=CNS; RX MEDLINE=97347296; PubMed=9203635; RA Gerhardt C.C., Bakker R.A., Piek G.J., Planta R.J., Vreugdenhil E., RA Leysen J.E., van Heerikhuizen H.; RT "Molecular cloning and pharmacological characterization of a molluscan RT octopamine receptor."; RL Mol. Pharmacol. 51:293-300(1997). CC -!- FUNCTION: G-protein coupled receptor for octopamine (OA), which is CC a neurotransmitter, neurohormone, and neuromodulator in CC invertebrates. Activation of this receptor by octopamine induces CC an increase in both inositol phosphates and cyclic AMP. The CC coupling to adenylyl cyclase seems to be less efficient than the CC coupling to phospholipase C. The rank order of potency for CC agonists is p-synephrine >= clonidine > p-octopamine = CC xylomethazoline = phenylephrine = oxymetazoline > B-HT920 > CC serotonin = p-tyramine > epinephrine > norepinephrine > CC methoxamine = dopamine = histamine. For antagonists, the rank CC order is yohimbine > chlopromazine / spiperone > phentolamine > CC mianserine > rauwolscine > prazosin > alprenolol / propanolol > CC pindolol. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U62771; AAC61296.1; -; mRNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000995; Musac_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00243; MUSCARINICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 638 Octopamine receptor 1. FT /FTId=PRO_0000069956. FT TOPO_DOM 1 28 Extracellular (Potential). FT TRANSMEM 29 53 Potential. FT TOPO_DOM 54 64 Cytoplasmic (Potential). FT TRANSMEM 65 87 Potential. FT TOPO_DOM 88 102 Extracellular (Potential). FT TRANSMEM 103 124 Potential. FT TOPO_DOM 125 147 Cytoplasmic (Potential). FT TRANSMEM 148 167 Potential. FT TOPO_DOM 168 239 Extracellular (Potential). FT TRANSMEM 240 259 Potential. FT TOPO_DOM 260 520 Cytoplasmic (Potential). FT TRANSMEM 521 545 Potential. FT TOPO_DOM 546 551 Extracellular (Potential). FT TRANSMEM 552 575 Potential. FT TOPO_DOM 576 638 Cytoplasmic (Potential). FT CARBOHYD 178 178 N-linked (GlcNAc...) (Potential). FT CARBOHYD 207 207 N-linked (GlcNAc...) (Potential). FT CARBOHYD 215 215 N-linked (GlcNAc...) (Potential). FT DISULFID 101 230 By similarity. SQ SEQUENCE 638 AA; 70001 MW; 65FA928B5C01D34F CRC64; MSRDIFMKRL RLHLLFDEVA MVTHIVGDVL SSVLLCAVVL LVLVGNTLVV AAVATSRKLR TVTNVFIVNL ACADLLLGVL VLPFSAVNEI KDVWIFGHVW CQVWLAVDVW LCTASILNLC CISLDRYLAI TRPIRYPGLM SAKRAKTLVA GVWLFSFVIC CPPLIGWNDG GDGIMDYNGT TATPIPVTTT QTPVTGRDDV LCDNGFNYST NSNMNTTCTY SGDSSLSTTC ELTNSRGYRI YAALGSFFIP MLVMVFFYLQ IYRAAVKTIS AYAKGELKTK YSVRENGSKT NSVTLRIHRG GRGPSTGSSV YRHGSTYGGS AAGAATREGC GDKDAAGGRR FGRQEMDSHL PVRKCRSSDA SLVTLTGLKC EIIDNGNAKH GPISELIKGR GKSFFWRKEK KRSVGGERES FENSTRNGRS TRAKLCGGRC LAIETDICSS GECSPRTKRI KEHARATQHN SLPVTPSLSS QNEETDAVFV RGTSNSEYKP RRSRLSAHKP GHAMRLHMQK FNREKKAAKT LAIIVGAFIM CWMPFFTIYL VGAFCENCIS PIVFSVAFWL GYCNSAMNPC VYALFSRDFR FAFRKLLTCS CKAWSKNRSF RPQTSDVPAI QLHCATQDDA KSSSDIGPTA SGGNGGYT // ID 5HT7R_XENLA STANDARD; PRT; 425 AA. AC Q91559; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 04-APR-2006, entry version 39. DE 5-hydroxytryptamine 7 receptor (5-HT-7) (Serotonin receptor 7). GN Name=htr7; Synonyms=5ht7; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skin; RX MEDLINE=96172463; PubMed=8589994; RA Nelson C.S., Cone R.D., Robbins L.S., Allen C.N., Adelman J.P.; RT "Cloning and expression of a 5HT7 receptor from Xenopus laevis."; RL Recept. Channels 3:61-70(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that stimulate adenylate CC cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U10161; AAA96812.1; -; mRNA. DR UniGene; Xl.1034; -. DR HSSP; P29274; 1MMH. DR InterPro; IPR001069; 5HT_7_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PANTHER; PTHR19266:SF115; 5HT7_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00652; 5HT7RECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 425 5-hydroxytryptamine 7 receptor. FT /FTId=PRO_0000068982. FT TOPO_DOM 1 70 Extracellular (Potential). FT TRANSMEM 71 97 1 (Potential). FT TOPO_DOM 98 107 Cytoplasmic (Potential). FT TRANSMEM 108 133 2 (Potential). FT TOPO_DOM 134 145 Extracellular (Potential). FT TRANSMEM 146 167 3 (Potential). FT TOPO_DOM 168 187 Cytoplasmic (Potential). FT TRANSMEM 188 211 4 (Potential). FT TOPO_DOM 212 226 Extracellular (Potential). FT TRANSMEM 227 249 5 (Potential). FT TOPO_DOM 250 324 Cytoplasmic (Potential). FT TRANSMEM 325 348 6 (Potential). FT TOPO_DOM 349 360 Extracellular (Potential). FT TRANSMEM 361 383 7 (Potential). FT TOPO_DOM 384 425 Cytoplasmic (Potential). FT LIPID 397 397 S-palmitoyl cysteine (Potential). FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT DISULFID 144 220 By similarity. SQ SEQUENCE 425 AA; 48017 MW; C42C75ACB4A1A255 CRC64; MLIQVQPSHL TDTNLSLHSA KPSSDHQNLL PSEFMTERPL NTTEQDLTAL NHTEKPDCGK ELLLYGDTEK IVIGVVLSII TLFTIAGNAL VIISVCIVKK LRQPSNYLVV SLAAADLSVA VAVMPFVIIT DLVGGEWLFG KVFCNVFIAM DVMCCTASIM TLCVISVDRY LGITRPLTYP ARQNGKLMAK MVFIVWLLSA SITLPPLFGW AKNVNVERVC LISQDFGYTV YSTAVAFYIP MTVMLVMYQR IFVAAKISAE KHKFVNIPRL YEQEGIYCLE DKLPPKKNSK KKKAVEEFAS LSKLIRQDRK NISIFKREQK AARTLGIIVG AFTFCWLPFF LLSTARPFIC GIMCSCMPLR LERTLLWLGY TNSLINPLIY AFFNRDLRTT FWNLLRCKYT NINRRLSAAS MHEALKVTER HEGIL // ID OCTB2_DROME STANDARD; PRT; 536 AA. AC Q4LBB9; Q9VG53; Q9VG54; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 2. DT 21-MAR-2006, entry version 10. DE Octopamine receptor beta-2 (DmOct-beta-12). GN Name=Oct-beta-2; ORFNames=CG6989; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Head; RX PubMed=15998303; DOI=10.1111/j.1471-4159.2005.03251.x; RA Maqueira B., Chatwin H., Evans P.D.; RT "Identification and characterization of a novel family of Drosophila RT beta-adrenergic-like octopamine G-protein coupled receptors."; RL J. Neurochem. 94:547-560(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: Receptor for octopamine. Octopamine (OA) is a CC neurotransmitter, neurohormone, and neuromodulator in CC invertebrates. The activity of this receptor is mediated by G CC proteins which activate adenylyl cyclase (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- CAUTION: Ref.2 sequence differs from that shown due to erroneous CC gene model prediction. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ880689; CAI56430.1; -; mRNA. DR EMBL; AE003696; AAF54834.1; ALT_SEQ; Genomic_DNA. DR EMBL; AE003696; AAF54835.1; ALT_SEQ; Genomic_DNA. DR HSSP; P08913; 1HLL. DR Ensembl; CG6989; Drosophila melanogaster. DR FlyBase; FBgn0038063; CG6989. DR GO; GO:0016021; C:integral to membrane; ISS. DR GO; GO:0004989; F:octopamine receptor activity; ISS. DR GO; GO:0007189; P:G-protein signaling, adenylate cyclase acti...; ISS. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Complete proteome; G-protein coupled receptor; Glycoprotein; Membrane; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 536 Octopamine receptor beta-2. FT /FTId=PRO_0000069960. FT TOPO_DOM 1 157 Extracellular (Potential). FT TRANSMEM 158 178 1 (Potential). FT TOPO_DOM 179 190 Cytoplasmic (Potential). FT TRANSMEM 191 211 2 (Potential). FT TOPO_DOM 212 233 Extracellular (Potential). FT TRANSMEM 234 256 3 (Potential). FT TOPO_DOM 257 270 Cytoplasmic (Potential). FT TRANSMEM 271 291 4 (Potential). FT TOPO_DOM 292 320 Extracellular (Potential). FT TRANSMEM 321 341 5 (Potential). FT TOPO_DOM 342 412 Cytoplasmic (Potential). FT TRANSMEM 413 433 6 (Potential). FT TOPO_DOM 434 444 Extracellular (Potential). FT TRANSMEM 445 465 7 (Potential). FT TOPO_DOM 466 536 Cytoplasmic (Potential). FT CARBOHYD 18 18 N-linked (GlcNAc...) (Potential). FT CARBOHYD 92 92 N-linked (GlcNAc...) (Potential). FT CARBOHYD 113 113 N-linked (GlcNAc...) (Potential). FT CARBOHYD 126 126 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 536 AA; 60379 MW; 67599A6DAC41280F CRC64; MLLCDGLGPE PPRQRHRNRT SAARIRKRPK CCCGDGGSGN QAEQPGGIVS NPISYGQSLT TLARVTAAAL TTAAMLHTTN ALAATGSSSA SNSSTGGIAL PLGTATPATH ELNATQPFGG SGLNFNESGA GLSDHHHHQQ HNPDEDWLDN IVWVFKAFVM LLIIIAAICG NLLVIISVMR VRKLRVITNY FVVSLAMADI MVAIMAMTFN FSVQVTGRWN FSPFLCDLWN SLDVYFSTAS ILHLCCISVD RYYAIVKPLK YPISMTKRVV GIMLLNTWIS PALLSFLPIF IGWYTTPQHQ QFVIQNPTQC SFVVNKYYAV ISSSISFWIP CTIMIFTYLA IFREANRQEK QLMMRHGNAM LMHRPSMQPS GEALSGSGSS KTLTLHEVEQ EHTPTKDKHL IKMKREHKAA RTLGIIMGTF ILCWLPFFLW YTLSMTCEEC QVPDIVVSIL FWIGYFNSTL NPLIYAYFNR DFREAFRNTL LCLFCNWWKD RHLPLDIDIR RSSLRYDQRA KSVYSESYLN STTPSHRRQS QMVDNL // ID OCTB1_DROME STANDARD; PRT; 508 AA. AC Q9VCZ3; Q4LBC0; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 04-APR-2006, entry version 37. DE Octopamine receptor beta-1 (DmOct-beta-1R) (DmOA2). GN Name=oa2; Synonyms=Oct-beta-1; ORFNames=CG6919; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DEVELOPMENTAL RP STAGE. RX PubMed=15816867; DOI=10.1111/j.1471-4159.2005.03034.x; RA Balfanz S., Struenker T., Frings S., Baumann A.; RT "A family of octopamine receptors that specifically induce cyclic AMP RT production or Ca2+ release in Drosophila melanogaster."; RL J. Neurochem. 93:440-451(2005). RN [2] RP ERRATUM. RA Balfanz S., Struenker T., Frings S., Baumann A.; RL J. Neurochem. 94:1168-1168(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B). RC TISSUE=Head; RX PubMed=15998303; DOI=10.1111/j.1471-4159.2005.03251.x; RA Maqueira B., Chatwin H., Evans P.D.; RT "Identification and characterization of a novel family of Drosophila RT beta-adrenergic-like octopamine G-protein coupled receptors."; RL J. Neurochem. 94:547-560(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: Receptor for octopamine. Octopamine (OA) is a CC neurotransmitter, neurohormone, and neuromodulator in CC invertebrates. The activity of this receptor is mediated by G CC proteins which activate adenylyl cyclase. Octopamine does not CC cause Ca(2+) release in oa2-expressing cells. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein CC (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q9VCZ3-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9VCZ3-2; Sequence=VSP_051833, VSP_051834; CC -!- DEVELOPMENTAL STAGE: Expressed in adult, pupae, third instar CC larvae, and 0-4 hour and 0-18 hour old embryos. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ617526; CAE84925.1; -; mRNA. DR EMBL; AJ880687; CAI56428.1; -; mRNA. DR EMBL; AJ880688; CAI56429.1; -; mRNA. DR EMBL; AE003739; AAF56012.1; -; Genomic_DNA. DR UniGene; Dm.16604; -. DR HSSP; P08913; 1HLL. DR Ensembl; CG6919; Drosophila melanogaster. DR FlyBase; FBgn0038980; oa2. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004989; F:octopamine receptor activity; IDA. DR GO; GO:0007189; P:G-protein signaling, adenylate cyclase acti...; IDA. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; Complete proteome; G-protein coupled receptor; KW Glycoprotein; Membrane; Receptor; Transducer; Transmembrane. FT CHAIN 1 508 Octopamine receptor beta-1. FT /FTId=PRO_0000069959. FT TOPO_DOM 1 111 Extracellular (Potential). FT TRANSMEM 112 132 1 (Potential). FT TOPO_DOM 133 139 Cytoplasmic (Potential). FT TRANSMEM 140 160 2 (Potential). FT TOPO_DOM 161 186 Extracellular (Potential). FT TRANSMEM 187 209 3 (Potential). FT TOPO_DOM 210 223 Cytoplasmic (Potential). FT TRANSMEM 224 244 4 (Potential). FT TOPO_DOM 245 270 Extracellular (Potential). FT TRANSMEM 271 291 5 (Potential). FT TOPO_DOM 292 351 Cytoplasmic (Potential). FT TRANSMEM 352 372 6 (Potential). FT TOPO_DOM 373 383 Extracellular (Potential). FT TRANSMEM 384 404 7 (Potential). FT TOPO_DOM 405 508 Cytoplasmic (Potential). FT CARBOHYD 164 164 N-linked (GlcNAc...) (Potential). FT VARSPLIC 421 421 S -> T (in isoform B). FT /FTId=VSP_051833. FT VARSPLIC 422 508 Missing (in isoform B). FT /FTId=VSP_051834. SQ SEQUENCE 508 AA; 56855 MW; 02C7C335676EAEF0 CRC64; MTLLQRLQAM SATTTRTILE GSISSFGGGT NEPLASKIPV LEESASHARY LKFIADGLID EGLGSAVGSG SSIAVSVEDV VAGQAQDIQA SEGSTDDADG SSHLALVFVK CFIIGFIILA AILGNMLVIV SVMRHRKLRI ITNYFVVSLA VADMLVALCA MTFNASVMIS GKWMFGSVMC DMWNSFDVYF STASIMHLCC ISVDRYYAIV QPLDYPLIMT QRRVFIMLLM VWLSPALLSF LPICSGWYTT TENYKYLKSN PHICEFKVNK AYAIVSSSMS FWIPGIVMLS MYYRIYQEAD RQERLVYRSK VAALLLEKHL QISQIPKPRP SIQVEQSTIS TMRRERKAAR TLGIIMSAFL ICWLPFFLWY IVSSLCDSCI TPRLLVGILF WIGYFNSALN PIIYAYFNRD FRAAFKKTLK SLFPYAFYFC RRGRGRDDDR DLEFGGPSRR GTNGAQRTGS GSAEMANCVN STASSEIHMS VMRARQYAVN VTPTTDAQMQ QLHPLYTN // ID HRH2_GORGO STANDARD; PRT; 359 AA. AC Q76MS7; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 18-APR-2006, entry version 17. DE Histamine H2 receptor (H2R) (Gastric receptor I). GN Name=HRH2; OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The H2 subclass of histamine receptors mediates gastric CC acid secretion. Also appears to regulate gastrointestinal motility CC and intestinal secretion. Possible role in regulating cell growth CC and differentiation. The activity of this receptor is mediated by CC G proteins which activate adenylyl cyclase and, through a separate CC G protein-dependent mechanism, the phosphoinositide/protein kinase CC (PKC) signaling pathway (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041386; BAA94471.1; -; Genomic_DNA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000503; Hist_H2_rcpt. DR PANTHER; PTHR19266:SF49; H2_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00531; HISTAMINEH2R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 359 Histamine H2 receptor. FT /FTId=PRO_0000069683. FT TOPO_DOM 1 22 Extracellular (Potential). FT TRANSMEM 23 44 1 (Potential). FT TOPO_DOM 45 57 Cytoplasmic (Potential). FT TRANSMEM 58 81 2 (Potential). FT TOPO_DOM 82 92 Extracellular (Potential). FT TRANSMEM 93 114 3 (Potential). FT TOPO_DOM 115 134 Cytoplasmic (Potential). FT TRANSMEM 135 159 4 (Potential). FT TOPO_DOM 160 180 Extracellular (Potential). FT TRANSMEM 181 204 5 (Potential). FT TOPO_DOM 205 234 Cytoplasmic (Potential). FT TRANSMEM 235 258 6 (Potential). FT TOPO_DOM 259 267 Extracellular (Potential). FT TRANSMEM 268 289 7 (Potential). FT TOPO_DOM 290 359 Cytoplasmic (Potential). FT SITE 98 98 Essential for histamine binding (By FT similarity). FT SITE 186 186 Essential for tiotidine binding and FT implicated in H2 selectivity (By FT similarity). FT SITE 190 190 Implicated in histamine binding (By FT similarity). FT LIPID 305 305 S-palmitoyl cysteine (By similarity). FT CARBOHYD 4 4 N-linked (GlcNAc...) (Potential). FT DISULFID 91 174 By similarity. SQ SEQUENCE 359 AA; 40098 MW; 9835AE2BA60B9B0F CRC64; MAPNGTASSF CLDSTACKIT ITVVLAVLIL ITVAGNVVVC LAVGLNRRLR NLTNCFIVSL AITDLLLGLL VLPFSAIYQL SCKWSFGKVF CNIYTSLDVM LCTASILNLF MISLDRYCAV MDPLRYPVLV TPVRVAISLV LIWVISITLS FLSIHLGWNS RNETSKGNHT TSKCKVQVNE VYGLVDGLVT FYLPLLIMCI TYYRIFKVAR DQAKRINHIS SWKAATIREH KATVTLAAVM GAFIICWFPY FTAFVYRGLR GDDAINEVLE AIVLWLGYAN SALNPILYAA LNRDFRTGYQ QLFCCRLANR NSHKTSLRSN ASQLSRTQSR EPRQQEEKPL KLQVWSGTEV TAPQGATDR // ID ADRB1_MELGA STANDARD; PRT; 483 AA. AC P07700; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 21-MAR-2006, entry version 54. DE Beta-1 adrenergic receptor (Beta-1 adrenoceptor) (Beta-1 DE adrenoreceptor) (Beta-T). GN Name=ADRB1; OS Meleagris gallopavo (Common turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Meleagris. OX NCBI_TaxID=9103; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86313664; PubMed=3018746; RA Yarden Y., Rodriguez H., Wong S.K.-F., Brandt D.R., May D.C., RA Burnier J., Harkins R.N., Chen E.Y., Ramachandran J., Ullrich A., RA Ross E.M.; RT "The avian beta-adrenergic receptor: primary structure and membrane RT topology."; RL Proc. Natl. Acad. Sci. U.S.A. 83:6795-6799(1986). RN [2] RP STRUCTURE BY NMR OF 345-359. RX MEDLINE=95129696; PubMed=7828722; DOI=10.1016/0014-5793(94)01409-T; RA Jung H., Windhaber R., Palm D., Schnackerz K.D.; RT "NMR and circular dichroism studies of synthetic peptides derived from RT the third intracellular loop of the beta-adrenoceptor."; RL FEBS Lett. 358:133-136(1995). CC -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine- CC induced activation of adenylate cyclase through the action of G CC proteins. This receptor binds epinephrine and norepinephrine with CC approximatively equal affinity. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Homologous desensitization of the receptor is mediated by its CC phosphorylation by beta-adrenergic receptor kinase. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M14379; AAA49627.1; -; mRNA. DR PIR; A25896; A25896. DR PDB; 1DEP; NMR; @=345-359. DR InterPro; IPR000507; Adrgc_rcpt_B1. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PANTHER; PTHR19266:SF58; Adrgc_receptorB1; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW 3D-structure; G-protein coupled receptor; Glycoprotein; Lipoprotein; KW Membrane; Palmitate; Phosphorylation; Receptor; Transducer; KW Transmembrane. FT CHAIN 1 483 Beta-1 adrenergic receptor. FT /FTId=PRO_0000069120. FT TOPO_DOM 1 43 Extracellular (Potential). FT TRANSMEM 44 67 1 (Potential). FT TOPO_DOM 68 77 Cytoplasmic (Potential). FT TRANSMEM 78 94 2 (Potential). FT TOPO_DOM 95 115 Extracellular (Potential). FT TRANSMEM 116 137 3 (Potential). FT TOPO_DOM 138 159 Cytoplasmic (Potential). FT TRANSMEM 160 189 4 (Potential). FT TOPO_DOM 190 205 Extracellular (Potential). FT TRANSMEM 206 228 5 (Potential). FT TOPO_DOM 229 290 Cytoplasmic (Potential). FT TRANSMEM 291 315 6 (Potential). FT TOPO_DOM 316 321 Extracellular (Potential). FT TRANSMEM 322 344 7 (Potential). FT TOPO_DOM 345 483 Cytoplasmic (Potential). FT LIPID 358 358 S-palmitoyl cysteine (By similarity). FT CARBOHYD 14 14 N-linked (GlcNAc...) (Probable). FT DISULFID 114 192 By similarity. FT HELIX 347 358 SQ SEQUENCE 483 AA; 54078 MW; B11A7E71F6CCE3E4 CRC64; MGDGWLPPDC GPHNRSGGGG ATAAPTGSRQ VSAELLSQQW EAGMSLLMAL VVLLIVAGNV LVIAAIGRTQ RLQTLTNLFI TSLACADLVM GLLVVPFGAT LVVRGTWLWG SFLCECWTSL DVLCVTASIE TLCVIAIDRY LAITSPFRYQ SLMTRARAKV IICTVWAISA LVSFLPIMMH WWRDEDPQAL KCYQDPGCCD FVTNRAYAIA SSIISFYIPL LIMIFVYLRV YREAKEQIRK IDRCEGRFYG SQEQPQPPPL PQHQPILGNG RASKRKTSRV MAMREHKALK TLGIIMGVFT LCWLPFFLVN IVNVFNRDLV PDWLFVFFNW LGYANSAFNP IIYCRSPDFR KAFKRLLCFP RKADRRLHAG GQPAPLPGGF ISTLGSPEHS PGGTWSDCNG GTRGGSESSL EERHSKTSRS ESKMEREKNI LATTRFYCTF LGNGDKAVFC TVLRIVKLFE DATCTCPHTH KLKMKWRFKQ HQA // ID ADRB1_BOVIN STANDARD; PRT; 467 AA. AC Q9TT96; Q9TUB4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 02-MAY-2006, entry version 44. DE Beta-1 adrenergic receptor (Beta-1 adrenoceptor) (Beta-1 DE adrenoreceptor). GN Name=ADRB1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Ha S.H., Baik M.G., Choi Y.J.; RT "Cloning of beta adrenergic receptor from Korean cattle."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-367. RC STRAIN=Korean; TISSUE=Adipocyte; RA Ha S.H.; RT "Cloning and characterization of beta adrenergic receptor from Korean RT native cattle."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine- CC induced activation of adenylate cyclase through the action of G CC proteins. This receptor binds epinephrine and norepinephrine with CC approximately equal affinity (By similarity). CC -!- SUBUNIT: Interacts with GOPC and DLG4 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). Localized at the plasma membrane. Found in the CC Golgi upon GOPC overexpression (By similarity). CC -!- DOMAIN: The PDZ domain-binding motif mediates competitive CC interactions with GOPC and DLG4 and plays a role in subcellular CC location of the receptor (By similarity). CC -!- PTM: Homologous desensitization of the receptor is mediated by its CC phosphorylation by beta-adrenergic receptor kinase (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF188187; AAF21435.1; -; Genomic_DNA. DR EMBL; AF095852; AAF01674.1; -; Genomic_DNA. DR UniGene; Bt.27278; -. DR InterPro; IPR000507; Adrgc_rcpt_B1. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PANTHER; PTHR19266:SF58; Adrgc_receptorB1; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00561; ADRENRGCB1AR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 467 Beta-1 adrenergic receptor. FT /FTId=PRO_0000069115. FT TOPO_DOM 1 59 Extracellular (Potential). FT TRANSMEM 60 83 1 (Potential). FT TOPO_DOM 84 96 Cytoplasmic (Potential). FT TRANSMEM 97 121 2 (Potential). FT TOPO_DOM 122 132 Extracellular (Potential). FT TRANSMEM 133 153 3 (Potential). FT TOPO_DOM 154 177 Cytoplasmic (Potential). FT TRANSMEM 178 198 4 (Potential). FT TOPO_DOM 199 224 Extracellular (Potential). FT TRANSMEM 225 245 5 (Potential). FT TOPO_DOM 246 312 Cytoplasmic (Potential). FT TRANSMEM 313 333 6 (Potential). FT TOPO_DOM 334 344 Extracellular (Potential). FT TRANSMEM 345 365 7 (Potential). FT TOPO_DOM 366 467 Cytoplasmic (Potential). FT MOTIF 464 467 PDZ-Binding (By similarity). FT LIPID 380 380 S-palmitoyl cysteine (By similarity). FT CARBOHYD 15 15 N-linked (GlcNAc...) (Potential). FT DISULFID 131 209 By similarity. FT CONFLICT 122 122 G -> D (in Ref. 1). FT CONFLICT 156 156 R -> H (in Ref. 1). FT CONFLICT 200 200 G -> R (in Ref. 1). FT CONFLICT 208 208 R -> G (in Ref. 1). FT CONFLICT 235 235 V -> A (in Ref. 1). FT CONFLICT 299 299 P -> S (in Ref. 1). SQ SEQUENCE 467 AA; 50137 MW; D929E79ADDF4039F CRC64; MGAGVLALGA SEPCNLSSAA PVPDGAATAA RLLVPASPPA SLLTSASEGP PLPSQQWTAG MGLLMAFIVL LIVVGNVLVL VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC TVWAISALVS FLPIFMQWWG DKDAKASRCY NDPECCDFII NEGYAITSSV VSFYVPLCIM AFVYLRVFRE AQKQVKKIDS CERRFLSGPA RLPSPAPSPG PPLPAATVAN GRANKRRPPR LVALREQKAL KTLGIIMGVF TLCWLPFFLA NVVKAFHRDL VPDRLFVFFN WLGYANSAFN PIIYCRSPDF RKAFQRLLCC ARRAACGSHA AAGDPPRALG CLAVARPSPS PGAASDDDDD DDEDDVGAAP PVRLLEPWAG YNGGAAANSD SSPDEPSRAG CASESKV // ID ADRB3_CAPHI STANDARD; PRT; 405 AA. AC Q9XT57; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 21-MAR-2006, entry version 38. DE Beta-3 adrenergic receptor (Beta-3 adrenoceptor) (Beta-3 DE adrenoreceptor). GN Name=ADRB3; Synonyms=B3AR; OS Capra hircus (Goat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Capra. OX NCBI_TaxID=9925; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=20292453; PubMed=10834601; RA Forrest R.H., Hickford J.G.H.; RT "Rapid communication: nucleotide sequences of the bovine, caprine, and RT ovine beta3-adrenergic receptor genes."; RL J. Anim. Sci. 78:1397-1398(2000). CC -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine- CC induced activation of adenylate cyclase through the action of G CC proteins. Beta-3 is involved in the regulation of lipolysis and CC thermogenesis. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF109929; AAD26148.1; -; Genomic_DNA. DR HSSP; P29274; 1MMH. DR InterPro; IPR000681; Adrgc_rcpt_B3. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PANTHER; PTHR19266:SF55; Adrgc_receptorB3; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00563; ADRENRGCB3AR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 405 Beta-3 adrenergic receptor. FT /FTId=PRO_0000069140. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 63 1 (Potential). FT TOPO_DOM 64 72 Cytoplasmic (Potential). FT TRANSMEM 73 91 2 (Potential). FT TOPO_DOM 92 111 Extracellular (Potential). FT TRANSMEM 112 133 3 (Potential). FT TOPO_DOM 134 155 Cytoplasmic (Potential). FT TRANSMEM 156 178 4 (Potential). FT TOPO_DOM 179 203 Extracellular (Potential). FT TRANSMEM 204 225 5 (Potential). FT TOPO_DOM 226 292 Cytoplasmic (Potential). FT TRANSMEM 293 314 6 (Potential). FT TOPO_DOM 315 326 Extracellular (Potential). FT TRANSMEM 327 347 7 (Potential). FT TOPO_DOM 348 405 Cytoplasmic (Potential). FT LIPID 361 361 S-palmitoyl cysteine (By similarity). FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 26 26 N-linked (GlcNAc...) (Potential). FT DISULFID 110 189 By similarity. SQ SEQUENCE 405 AA; 43126 MW; 776B81756BF5556F CRC64; MAPWPPRNSS LTPWPDIPTL APNTANASGL PGVPWAVALA GALLALAVLA IVGGNLLVIV AIARTPRLQT MTNVFVTSLA TADLVVGLLV VPPGATLALT GHWPLGVTGC ELWTSVDVLC VTASIETLCA LAVDRYLAVT NPLRYGALVT KRRARAAVVL VWVVSAAVSF APIMSKWWRV GADAEAQRCH SNPRCCTFAS NMPYALLSSS VSFYLPLLVM LFVYARVFVV ATRQLRLLRR ELGRFPPEES PPAPSRSGSP GPAGPYASPA GVPSYGRRPA RLLPLREHRA LRTLGLIMGT FTLCWLPFFV VNVVRALGGP SLVSGPTFLA LNWLGYANSA FNPLIYCRSP DFQSAFRRLL CRCRPEEHLA AASPPRAPSG APRVLTSPAG PRQPSPLDGA SCGLS // ID ADRB2_ONCMY STANDARD; PRT; 409 AA. AC Q8UUY8; DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 21-MAR-2006, entry version 27. DE Beta-2 adrenergic receptor (Beta-2 adrenoceptor) (Beta-2 DE adrenoreceptor). GN Name=ADRB2; OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX MEDLINE=21600913; PubMed=11737201; RA Nickerson J.G., Dugan S.G., Drouin G., Moon T.W.; RT "A putative beta2-adrenoceptor from the rainbow trout (Oncorhynuchus RT mykiss). Molecular characterization and pharmacology."; RL Eur. J. Biochem. 268:6465-6472(2001). CC -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine- CC induced activation of adenylate cyclase through the action of G CC proteins. The beta-2-adrenergic receptor binds epinephrine with an CC approximately 30-fold greater affinity than it does norepinephrine CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and red and CC white muscle, with lower levels of expression in the gills, heart, CC kidney and spleen. CC -!- PTM: Lacks the regulatory protein kinase A phosphorylation sites CC within the G-protein binding domain that mediate desensitization CC and are present in mammalian homologs. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY044093; AAK94672.1; -; mRNA. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0004941; F:beta2-adrenergic receptor activity; NAS. DR GO; GO:0007190; P:adenylate cyclase activation; NAS. DR InterPro; IPR000332; Adrgc_rcpt_B2. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR PANTHER; PTHR19266:SF57; Adrgc_receptorB2; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 409 Beta-2 adrenergic receptor. FT /FTId=PRO_0000069137. FT TOPO_DOM 1 37 Extracellular (Potential). FT TRANSMEM 38 61 Potential. FT TOPO_DOM 62 74 Cytoplasmic (Potential). FT TRANSMEM 75 98 Potential. FT TOPO_DOM 99 109 Extracellular (Potential). FT TRANSMEM 110 132 Potential. FT TOPO_DOM 133 153 Cytoplasmic (Potential). FT TRANSMEM 154 177 Potential. FT TOPO_DOM 178 199 Extracellular (Potential). FT TRANSMEM 200 223 Potential. FT TOPO_DOM 224 282 Cytoplasmic (Potential). FT TRANSMEM 283 306 Potential. FT TOPO_DOM 307 318 Extracellular (Potential). FT TRANSMEM 319 337 Potential. FT TOPO_DOM 338 409 Cytoplasmic (Potential). FT SITE 116 116 Implicated in catechol agonist and FT antagonist binding (By similarity). FT SITE 207 207 Implicated in catechol agonist binding FT (By similarity). FT SITE 210 210 Implicated in catechol agonist binding FT (By similarity). FT LIPID 349 349 S-palmitoyl cysteine (By similarity). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 20 20 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. SQ SEQUENCE 409 AA; 45098 MW; AEFFA8BC71574BD2 CRC64; MENVSTPAVF NLSDLSVEMN SSSRQWSYSE YSEAVAVLLG ILMALLVMCI VFGNVLVITA IVRFQRLQTV TNMFITSLAC ADLVMGLLVV PFGACYILLN TWHFGSFLCE FWTAADVLCV TASIETLCVI ALDRYLAITS PLRYPSLLTK RKACVVVVTV WGVAALISFL PIHMKWWVSD EPEALSCLED AHCCDFNTNA AYAVASSVVS FYIPLAVMAF VYGRVFQEAR KQLEKIRGSE GRFHAQMIDN NQGQDGGDGS GGGGGNGKRP KFCLKEHKAL KTLGIIMGTF TLCWLPFFVL NVVVTIWKVD NIKMPFRILN WIGYANSAFN PLIYCRSPEF RYAFQEILCL RGAAFPTNGY IYRGHSLRLS PKDKPGSLSN NVGTVELGSL SSVTNINGYC NNPPLASIV // ID DRD1C_XENLA STANDARD; PRT; 465 AA. AC P42291; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-MAR-2006, entry version 36. DE D(1C) dopamine receptor. OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95024150; PubMed=7937989; RA Sugamori K.S., Demchyshyn L.L., Chung M., Niznik H.B.; RT "D1A, D1B, and D1C dopamine receptors from Xenopus laevis."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10536-10540(1994). CC -!- FUNCTION: This is one of the five types (D1 to D5) of receptors CC for dopamine. The activity of this receptor is mediated by G CC proteins which activate adenylyl cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Brain and kidney. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U07865; AAA50830.1; -; Genomic_DNA. DR PIR; I51661; I51661. DR HSSP; P08913; 1HLL. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 465 D(1C) dopamine receptor. FT /FTId=PRO_0000069381. FT TOPO_DOM 1 30 Extracellular (Potential). FT TRANSMEM 31 54 1 (Potential). FT TOPO_DOM 55 65 Cytoplasmic (Potential). FT TRANSMEM 66 92 2 (Potential). FT TOPO_DOM 93 101 Extracellular (Potential). FT TRANSMEM 102 124 3 (Potential). FT TOPO_DOM 125 143 Cytoplasmic (Potential). FT TRANSMEM 144 168 4 (Potential). FT TOPO_DOM 169 193 Extracellular (Potential). FT TRANSMEM 194 219 5 (Potential). FT TOPO_DOM 220 264 Cytoplasmic (Potential). FT TRANSMEM 265 291 6 (Potential). FT TOPO_DOM 292 309 Extracellular (Potential). FT TRANSMEM 310 334 7 (Potential). FT TOPO_DOM 335 465 Cytoplasmic (Potential). FT LIPID 344 344 S-palmitoyl cysteine (By similarity). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT DISULFID 101 187 By similarity. SQ SEQUENCE 465 AA; 52641 MW; F41DF85AF0D2F869 CRC64; MENFSIFNVT VNVWHADLDV GNSDLSLRAL TGLLLSLLIL STLLGNTLVC LAVIKFRHLR SKVTNFFVIS LAVSDLFVAL LVMPWKAVTE VAGFWVFGDF CDTWVAFDIM CSTASILNLC IISLDRYWAI ASPFRYERKM TQRVAFIMIG VAWTLSILIS FIPVQLSWHK SHEADEELNG VNHTENCDSS LNRTYAISSS LISFYIPVVI MIGTYTRIYR IAQTQIRRIS SLERAVEHAQ RCSSRLSNEN SLKTSFRKET KVLKTLSIIM GVFVFCWLPF FVLNCMIPFC HMNLPGQNEP EPPCVSETTF NIFVWFGWAN SSLNPVIYAF NADFRKAFTT ILGCNRFCSS NNVEAVNFSN ELVSYHHDTT FQKDIPVTFN NSHLPNVVDQ DQEVLEGTCF DKVSVLSTSH GTRSQKNLHL PAGVQFECEA EITLETITPF TSTGPLECLP QLVADEDRHY TTKLY // ID DRD5_MOUSE STANDARD; PRT; 478 AA. AC Q8BLD9; Q61439; Q80UB7; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-MAY-2006, entry version 26. DE D(1B) dopamine receptor (D(5) dopamine receptor). GN Name=Drd5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-252. RX MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100; RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E., RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C., RA Bergmann J.E., Gaitanaris G.A.; RT "The G protein-coupled receptor repertoires of human and mouse."; RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-298. RC TISSUE=Testis; RX MEDLINE=94116980; PubMed=8288218; RA Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I., RA Copeland N.G., Jenkins N.A.; RT "Identification, chromosomal location, and genome organization of RT mammalian G-protein-coupled receptors."; RL Genomics 18:175-184(1993). CC -!- FUNCTION: This is one of the five types (D1 to D5) of receptors CC for dopamine. The activity of this receptor is mediated by G CC proteins which activate adenylyl cyclase (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK045456; BAC32378.1; -; mRNA. DR EMBL; AY255563; AAO85075.1; -; mRNA. DR EMBL; L20330; AAA16844.1; -; mRNA. DR PIR; A48909; A48909. DR UniGene; Mm.167154; -. DR HSSP; P08913; 1HLL. DR MGI; MGI:94927; Drd5. DR GO; GO:0019226; P:transmission of nerve impulse; IMP. DR InterPro; IPR000497; Dopa_1B_rcpt. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00566; DOPAMINED1BR. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Receptor; Transducer; Transmembrane. FT CHAIN 1 478 D(1B) dopamine receptor. FT /FTId=PRO_0000069407. FT TOPO_DOM 1 38 Extracellular (Potential). FT TRANSMEM 39 64 1 (Potential). FT TOPO_DOM 65 75 Cytoplasmic (Potential). FT TRANSMEM 76 102 2 (Potential). FT TOPO_DOM 103 111 Extracellular (Potential). FT TRANSMEM 112 134 3 (Potential). FT TOPO_DOM 135 153 Cytoplasmic (Potential). FT TRANSMEM 154 179 4 (Potential). FT TOPO_DOM 180 215 Extracellular (Potential). FT TRANSMEM 216 240 5 (Potential). FT TOPO_DOM 241 289 Cytoplasmic (Potential). FT TRANSMEM 290 317 6 (Potential). FT TOPO_DOM 318 335 Extracellular (Potential). FT TRANSMEM 336 357 7 (Potential). FT TOPO_DOM 358 478 Cytoplasmic (Potential). FT LIPID 370 370 S-palmitoyl cysteine (By similarity). FT CARBOHYD 7 7 N-linked (GlcNAc...) (Potential). FT DISULFID 111 211 By similarity. FT CONFLICT 231 231 P -> L (in Ref. 3). SQ SEQUENCE 478 AA; 53076 MW; D39165BC558131DF CRC64; MLPPGRNGTA HRARLGLQRQ LAQVDAPGGS AAPLGPAQVV TAGLLTLLIV WTLLGNVLVC AAIVRSRHLR AKMTNIFIVS LAVSDLFVAL LVMPWKAVAE VAGYWPFGAF CDIWVAFDIM CSTASILNLC IISVDRYWAI SRPFRYERKM TQRVALVMVA LAWTLSILIS FIPVQLNWHR DKAGSQGREG LLSNETPWEE GWELDGRTEN CDSSLNRTYA ISSSLISFYI PVAIMIVTYT RIYRIAQVQI RRISSLERAA EHAQSCRSRG ACEPDPSLRA SIKKETKVFK TLSVIMGVFV CCWLPFFILN CMVPFCSSGD AQGPRTGFPC VSETTFDIFV WFGWANSSLN PIIYAFNADF RKVFAQLLGC SHLCFRTPVQ TVNISNELIS YNQDTVFHRE IAAAYVHMIP NAVSSGDREV GEEEEAEEEG PFDHMSQISP TTPDGDLAAE SVWELDCEEE VSLGKISPLT PNCFHKTA // ID DOPR1_DROME STANDARD; PRT; 511 AA. AC P41596; Q24038; Q9VFM1; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 04-APR-2006, entry version 44. DE Dopamine receptor 1 precursor (D-DOP1) (dDA1). GN Name=DopR; Synonyms=DopR1, DopR35EF; ORFNames=CG9652; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Berlin; TISSUE=Head; RX MEDLINE=95041081; PubMed=7953290; RA Gotzes F., Balfanz S., Baumann A.; RT "Primary structure and functional characterization of a Drosophila RT dopamine receptor with high homology to human D1/5 receptors."; RL Recept. Channels 2:131-141(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE OF 127-511, FUNCTION, AND DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; TISSUE=Head; RX MEDLINE=95237365; PubMed=7720859; DOI=10.1016/0014-5793(95)00224-W; RA Sugamori K.S., Demchyshyn L.L., McConkey F., Forte M.A., Niznik H.B.; RT "A primordial dopamine D1-like adenylyl cyclase-linked receptor from RT Drosophila melanogaster displaying poor affinity for benzazepines."; RL FEBS Lett. 362:131-138(1995). CC -!- FUNCTION: Receptor for dopamine. The activity of this receptor is CC mediated by G proteins which activate adenylyl cyclase. Might be CC involved in the processing of visual information and/or visual CC learning. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Somata of the optic lobes. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC -!- MISCELLANEOUS: Potency of neurotransmitter agonists in stimulating CC cAMP production and the lack of stimulation by other transmitters CC and metabolites suggests this is a D1-like receptor. Low homology CC to vertebrate D1 receptors suggests this may be a progenitor of CC the D1 receptor subfamily. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X77234; CAA54451.1; -; mRNA. DR EMBL; AE003703; AAF55030.2; -; Genomic_DNA. DR EMBL; U22106; AAA85716.1; -; mRNA. DR PIR; S44275; S44275. DR PIR; S68780; S68780. DR UniGene; Dm.3077; -. DR Ensembl; CG9652; Drosophila melanogaster. DR FlyBase; FBgn0011582; DopR. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Complete proteome; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Phosphorylation; Receptor; Signal; KW Transducer; Transmembrane. FT SIGNAL 1 19 Potential. FT CHAIN 20 511 Dopamine receptor 1. FT /FTId=PRO_0000012718. FT TOPO_DOM 20 142 Extracellular (Potential). FT TRANSMEM 143 169 1 (Potential). FT TOPO_DOM 170 179 Cytoplasmic (Potential). FT TRANSMEM 180 206 2 (Potential). FT TOPO_DOM 207 216 Extracellular (Potential). FT TRANSMEM 217 239 3 (Potential). FT TOPO_DOM 240 258 Cytoplasmic (Potential). FT TRANSMEM 259 279 4 (Potential). FT TOPO_DOM 280 310 Extracellular (Potential). FT TRANSMEM 311 331 5 (Potential). FT TOPO_DOM 332 391 Cytoplasmic (Potential). FT TRANSMEM 392 412 6 (Potential). FT TOPO_DOM 413 427 Extracellular (Potential). FT TRANSMEM 428 450 7 (Potential). FT TOPO_DOM 451 511 Cytoplasmic (Potential). FT LIPID 468 468 S-palmitoyl cysteine (Potential). FT LIPID 469 469 S-palmitoyl cysteine (Potential). FT CARBOHYD 53 53 N-linked (GlcNAc...) (Potential). FT CARBOHYD 63 63 N-linked (GlcNAc...) (Potential). FT CARBOHYD 74 74 N-linked (GlcNAc...) (Potential). FT CARBOHYD 117 117 N-linked (GlcNAc...) (Potential). FT CARBOHYD 123 123 N-linked (GlcNAc...) (Potential). FT DISULFID 216 302 By similarity. FT CONFLICT 171 172 ER -> DG (in Ref. 1). FT CONFLICT 175 175 R -> P (in Ref. 1). SQ SEQUENCE 511 AA; 56170 MW; F044C00EDBF14749 CRC64; MYTPHPFGFL IILVPMTNAM RAIAAIAAGV GSVAATVATS TTSSISSSTT IINTSSATTI GGNHTSGSTG FSTNSTLLDA DHLPLQLTTA KVDLDIEIDI QLLTNGYDGT TLTSFYNESS WTNASEMDTI VGEEPEPLSL VSIVVVGIFL SVLIFLSVAG NILVCLAIYT ERSLRRIGNL FLASLAIADL FVASLVMTFA GVNDLLGYWI FGAQFCDTWV AFDVMCSTAS ILNLCAISMD RYIHIKDPLR YGRWVTRRVA VITIAAIWLL AAFVSFVPIS LGIHRPDQPL IFEDNGKKYP TCALDLTPTY AVVSSCISFY FPCVVMIGIY CRLYCYAQKH VKSIKAVTRP GEVAEKQRYK SIRRPKNQPK KFKVRNLHTH SSPYHVSDHK AAVTVGVIMG VFLICWVPFF CVNITAAFCK TCIGGQTFKI LTWLGYSNSA FNPIIYSIFN KEFRDAFKRI LTMRNPWCCA QDVGNIHPRN SDRFITDYAA KNVVVMNSGR SSAELEQVSA I // ID TAAR9_MOUSE STANDARD; PRT; 348 AA. AC Q5QD04; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 18-APR-2006, entry version 17. DE Trace amine-associated receptor 9. GN Name=Taar9; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6; RX PubMed=15718104; DOI=10.1016/j.ygeno.2004.11.010; RA Lindemann L., Ebeling M., Kratochwil N.A., Bunzow J.R., Grandy D.K., RA Hoener M.C.; RT "Trace amine-associated receptors form structurally and functionally RT distinct subfamilies of novel G protein-coupled receptors."; RL Genomics 85:372-385(2005). CC -!- FUNCTION: Orphan receptor. Could be a receptor for trace amines. CC Trace amines are biogenic amines present in very low levels in CC mammalian tissues. Although some trace amines have clearly defined CC roles as neurotransmitters in invertebrates, the extent to which CC they function as true neurotransmitters in vertebrates has CC remained speculative. Trace amines are likely to be involved in a CC variety of physiological functions that have yet to be fully CC understood (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY702340; AAV70149.1; -; Genomic_DNA. DR UniGene; Mm.300923; -. DR Ensembl; ENSMUSG00000037424; Mus musculus. DR MGI; MGI:3527454; Taar9. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR009133; Trac_amin_rcpt_1. DR InterPro; IPR009132; Trace_amine_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01831; TRACEAMINE1R. DR PRINTS; PR01830; TRACEAMINER. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 348 Trace amine-associated receptor 9. FT /FTId=PRO_0000070182. FT TOPO_DOM 1 33 Extracellular (Potential). FT TRANSMEM 34 54 1 (Potential). FT TOPO_DOM 55 68 Cytoplasmic (Potential). FT TRANSMEM 69 89 2 (Potential). FT TOPO_DOM 90 107 Extracellular (Potential). FT TRANSMEM 108 128 3 (Potential). FT TOPO_DOM 129 147 Cytoplasmic (Potential). FT TRANSMEM 148 168 4 (Potential). FT TOPO_DOM 169 197 Extracellular (Potential). FT TRANSMEM 198 218 5 (Potential). FT TOPO_DOM 219 259 Cytoplasmic (Potential). FT TRANSMEM 260 280 6 (Potential). FT TOPO_DOM 281 294 Extracellular (Potential). FT TRANSMEM 295 315 7 (Potential). FT TOPO_DOM 316 348 Cytoplasmic (Potential). FT CARBOHYD 19 19 N-linked (GlcNAc...) (Potential). FT DISULFID 105 190 By similarity. SQ SEQUENCE 348 AA; 38901 MW; 0164AAF9C5474BA8 CRC64; MTSDFSPEPP MELCYENVNG SCIKSSYAPW PRAILYGVLG LGALLAVFGN LLVIIAILHF KQLHTPTNFL VASLACADFL VGVTVMPFST VRSVESCWYF GESYCKFHTC FDTSFCFASL FHLCCISIDR YIAVTDPLTY PTKFTVSVSG LCIALSWFFS VTYSFSIFYT GANEEGIEEL VVALTCVGGC QAPLNQNWVL LCFLLFFLPT VVMVFLYGRI FLVAKYQARK IEGTANQAQA SSESYKERVA KRERKAAKTL GIAMAAFLVS WLPYIIDAVI DAYMNFITPA YVYEILVWCV YYNSAMNPLI YAFFYPWFRK AIKLIVSGKV FRADSSTTNL FSEEAGAG // ID TAAR5_HUMAN STANDARD; PRT; 337 AA. AC O14804; Q4VBL1; Q5VUQ3; Q6NTA8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 2. DT 02-MAY-2006, entry version 40. DE Trace amine-associated receptor 5 (Putative neurotransmitter DE receptor). GN Name=TAAR5; Synonyms=PNR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX MEDLINE=98125534; PubMed=9464258; DOI=10.1006/bbrc.1997.7591; RA Zeng Z., Fan P., Rand E., Kyaw H., Su K., Madike V., Carter K.C., RA Li Y.; RT "Cloning of a putative human neurotransmitter receptor expressed in RT skeletal muscle and brain."; RL Biochem. Biophys. Res. Commun. 242:575-578(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15718104; DOI=10.1016/j.ygeno.2004.11.010; RA Lindemann L., Ebeling M., Kratochwil N.A., Bunzow J.R., Grandy D.K., RA Hoener M.C.; RT "Trace amine-associated receptors form structurally and functionally RT distinct subfamilies of novel G protein-coupled receptors."; RL Genomics 85:372-385(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: Orphan receptor. Ligands are likely small molecules, CC either sharing some similarities with trace amine as, e.g. CC derivatives of indolamines (such as 5-methoxytryptamine) or of CC phenylethylamines (such as phenylethanolamine) or being any kind CC of metabolite of amino acids or biogenic amine neurotransmitters. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in skeletal CC muscle and selected areas of the brain, such amygdala, CC hippocampus, caudate nucleus, thalamus and hypothalamus. Weak CC expression is also find in substantia nigra. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF021818; AAC39581.1; -; mRNA. DR EMBL; AY702306; AAV70123.1; -; Genomic_DNA. DR EMBL; AL513524; CAH72100.1; -; Genomic_DNA. DR EMBL; BC069171; AAH69171.1; -; mRNA. DR EMBL; BC095541; AAH95541.1; -; mRNA. DR PIR; JC5832; JC5832. DR UniGene; Hs.248198; -. DR Ensembl; ENSG00000135569; Homo sapiens. DR HGNC; HGNC:30236; TAAR5. DR MIM; 607405; gene. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS. DR GO; GO:0007165; P:signal transduction; TAS. DR GO; GO:0007268; P:synaptic transmission; TAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR009132; Trace_amine_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01830; TRACEAMINER. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 337 Trace amine-associated receptor 5. FT /FTId=PRO_0000070154. FT TOPO_DOM 1 34 Extracellular (Potential). FT TRANSMEM 35 55 1 (Potential). FT TOPO_DOM 56 70 Cytoplasmic (Potential). FT TRANSMEM 71 91 2 (Potential). FT TOPO_DOM 92 109 Extracellular (Potential). FT TRANSMEM 110 130 3 (Potential). FT TOPO_DOM 131 154 Cytoplasmic (Potential). FT TRANSMEM 155 175 4 (Potential). FT TOPO_DOM 176 204 Extracellular (Potential). FT TRANSMEM 205 225 5 (Potential). FT TOPO_DOM 226 253 Cytoplasmic (Potential). FT TRANSMEM 254 274 6 (Potential). FT TOPO_DOM 275 284 Extracellular (Potential). FT TRANSMEM 285 307 7 (Potential). FT TOPO_DOM 308 337 Cytoplasmic (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 99 192 By similarity. FT CONFLICT 16 16 F -> L (in Ref. 4; AAH95541). FT CONFLICT 40 40 A -> T (in Ref. 1). FT CONFLICT 80 80 D -> N (in Ref. 4; AAH69171). FT CONFLICT 257 257 A -> V (in Ref. 1). FT CONFLICT 332 332 V -> A (in Ref. 4; AAH95541). SQ SEQUENCE 337 AA; 38242 MW; 251DB41A13A5535A CRC64; MRAVFIQGAE EHPAAFCYQV NGSCPRTVHT LGIQLVIYLA CAAGMLIIVL GNVFVAFAVS YFKALHTPTN FLLLSLALAD MFLGLLVLPL STIRSVESCW FFGDFLCRLH TYLDTLFCLT SIFHLCFISI DRHCAICDPL LYPSKFTVRV ALRYILAGWG VPAAYTSLFL YTDVVETRLS QWLEEMPCVG SCQLLLNKFW GWLNFPLFFV PCLIMISLYV KIFVVATRQA QQITTLSKSL AGAAKHERKA AKTLGIAVGI YLLCWLPFTI DTMVDSLLHF ITPPLVFDIF IWFAYFNSAC NPIIYVFSYQ WFRKALKLTL SQKVFSPQTR TVDLYQE // ID TAAR3_MOUSE STANDARD; PRT; 343 AA. AC Q5QD16; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 18-APR-2006, entry version 17. DE Trace amine-associated receptor 3. GN Name=Taar3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6; RX PubMed=15718104; DOI=10.1016/j.ygeno.2004.11.010; RA Lindemann L., Ebeling M., Kratochwil N.A., Bunzow J.R., Grandy D.K., RA Hoener M.C.; RT "Trace amine-associated receptors form structurally and functionally RT distinct subfamilies of novel G protein-coupled receptors."; RL Genomics 85:372-385(2005). CC -!- FUNCTION: Orphan receptor. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY702327; AAV70137.1; -; Genomic_DNA. DR UniGene; Mm.379737; -. DR Ensembl; ENSMUSG00000069708; Mus musculus. DR MGI; MGI:3527427; Taar3. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR009132; Trace_amine_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01830; TRACEAMINER. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 343 Trace amine-associated receptor 3. FT /FTId=PRO_0000070150. FT TOPO_DOM 1 35 Extracellular (Potential). FT TRANSMEM 36 56 1 (Potential). FT TOPO_DOM 57 68 Cytoplasmic (Potential). FT TRANSMEM 69 89 2 (Potential). FT TOPO_DOM 90 150 Extracellular (Potential). FT TRANSMEM 151 168 3 (Potential). FT TOPO_DOM 169 172 Cytoplasmic (Potential). FT TRANSMEM 173 193 4 (Potential). FT TOPO_DOM 194 198 Extracellular (Potential). FT TRANSMEM 199 223 5 (Potential). FT TOPO_DOM 224 257 Cytoplasmic (Potential). FT TRANSMEM 258 278 6 (Potential). FT TOPO_DOM 279 287 Extracellular (Potential). FT TRANSMEM 288 308 7 (Potential). FT TOPO_DOM 309 343 Cytoplasmic (Potential). FT CARBOHYD 18 18 N-linked (GlcNAc...) (Potential). FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential). FT DISULFID 104 189 By similarity. SQ SEQUENCE 343 AA; 38745 MW; 2A3F7D7BFC93AABF CRC64; MDLIYIPEDL SSCPKFGNKS CPPTNRSFRV RMIMYLFMTG AMVITIFGNL VIIISISHFK QLHSPTNFLI LSMATTDFLL GFVIMPYSMV RSVESCWYFG DSFCKFHASF DMMLSLTSIF HLCSIAIDRF YAVCDPLHYT TTMTVSMIKR LLAFCWAAPA LFSFGLVLSE ANVSGMQSYE ILVACFNFCA LTFNKFWGTI LFTTCFFTPG SIMVGIYGKI FIVSRRHARA LSDMPANTKG AVGKNLSKKK DRKAAKTLGI VMGVFLACWL PCFLAVLIDP YLDYSTPIIV LDLLVWLGYF NSTCNPLIHG FFYPWFRKAL QFIVSGKIFR SNSDTANLFP EAH // ID TAAR1_HUMAN STANDARD; PRT; 339 AA. AC Q96RJ0; Q3MIH8; Q5VUQ1; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 18-APR-2006, entry version 37. DE Trace amine-associated receptor 1 (Trace amine receptor 1) (TaR-1). GN Name=TAAR1; Synonyms=TA1, TAR1, TRAR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=21374364; PubMed=11459929; DOI=10.1073/pnas.151105198; RA Borowsky B., Adham N., Jones K.A., Raddatz R., Artymyshyn R., RA Ogozalek K.L., Durkin M.M., Lakhlani P.P., Bonini J.A., Pathirana S., RA Boyle N., Pu X., Kouranova E., Lichtblau H., Ochoa F.Y., RA Branchek T.A., Gerald C.; RT "Trace amines: identification of a family of mammalian G protein- RT coupled receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8966-8971(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=21580235; PubMed=11723224; RA Bunzow J.R., Sonders M.S., Arttamangkul S., Harrison L.M., Zhang G., RA Quigley D.I., Darland T., Suchland K.L., Pasumamula S., Kennedy J.L., RA Olson S.B., Magenis R.E., Amara S.G., Grandy D.K.; RT "Amphetamine, 3,4-methylenedioxymethamphetamine, lysergic acid RT diethylamide, and metabolites of the catecholamine neurotransmitters RT are agonists of a rat trace amine receptor."; RL Mol. Pharmacol. 60:1181-1188(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kopatz S.A., Aronstam R.S., Sharma S.V.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Placenta; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP FUNCTION. RX PubMed=15718104; DOI=10.1016/j.ygeno.2004.11.010; RA Lindemann L., Ebeling M., Kratochwil N.A., Bunzow J.R., Grandy D.K., RA Hoener M.C.; RT "Trace amine-associated receptors form structurally and functionally RT distinct subfamilies of novel G protein-coupled receptors."; RL Genomics 85:372-385(2005). CC -!- FUNCTION: Receptor for trace amines, including beta- CC phenylethylamine (b-PEA), p-tyramine (p-TYR), octopamine and CC tryptamine, with highest affinity for b-PEA and p-TYR. CC Unresponsive to classical biogenic amines, such as epinephrine and CC histamine and only partially activated by dopamine and serotonine. CC Trace amines are biogenic amines present in very low levels in CC mammalian tissues. Although some trace amines have clearly defined CC roles as neurotransmitters in invertebrates, the extent to which CC they function as true neurotransmitters in vertebrates has CC remained speculative. Trace amines are likely to be involved in a CC variety of physiological functions that have yet to be fully CC understood. The signal transduced by this receptor is mediated by CC the G(s)-class of G-proteins which activate adenylate cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Detected in low levels in discrete regions CC within the central nervous system and in several peripheral CC tissues. Moderately expressed in stomach. Low levels in amygdala, CC kidney, and lung, and small intestin. Trace amounts in cerebellum, CC dorsal root ganglia, hippocampus, hypothalamus, liver, medulla, CC pancreas, pituitary, pontine reticular formation, prostate, CC skeletal muscle, and spleen. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF380185; AAK71236.1; -; Genomic_DNA. DR EMBL; AF200627; AAG17112.1; -; Genomic_DNA. DR EMBL; AY180374; AAO22154.1; -; mRNA. DR EMBL; AL513524; CAH72104.1; -; Genomic_DNA. DR EMBL; BC101825; AAI01826.1; -; mRNA. DR UniGene; Hs.375030; -. DR Ensembl; ENSG00000146399; Homo sapiens. DR HGNC; HGNC:17734; TAAR1. DR MIM; 609333; gene. DR LinkHub; Q96RJ0; -. DR GO; GO:0016021; C:integral to membrane; IC. DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR009133; Trac_amin_rcpt_1. DR InterPro; IPR009132; Trace_amine_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01831; TRACEAMINE1R. DR PRINTS; PR01830; TRACEAMINER. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 339 Trace amine-associated receptor 1. FT /FTId=PRO_0000070141. FT TOPO_DOM 1 25 Extracellular (Potential). FT TRANSMEM 26 46 1 (Potential). FT TOPO_DOM 47 59 Cytoplasmic (Potential). FT TRANSMEM 60 80 2 (Potential). FT TOPO_DOM 81 98 Extracellular (Potential). FT TRANSMEM 99 119 3 (Potential). FT TOPO_DOM 120 136 Cytoplasmic (Potential). FT TRANSMEM 137 157 4 (Potential). FT TOPO_DOM 158 188 Extracellular (Potential). FT TRANSMEM 189 209 5 (Potential). FT TOPO_DOM 210 252 Cytoplasmic (Potential). FT TRANSMEM 253 273 6 (Potential). FT TOPO_DOM 274 287 Extracellular (Potential). FT TRANSMEM 288 308 7 (Potential). FT TOPO_DOM 309 339 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT DISULFID 96 182 By similarity. SQ SEQUENCE 339 AA; 39092 MW; 5E72FA61CEFAC0E0 CRC64; MMPFCHNIIN ISCVKNNWSN DVRASLYSLM VLIILTTLVG NLIVIVSISH FKQLHTPTNW LIHSMATVDF LLGCLVMPYS MVRSAEHCWY FGEVFCKIHT STDIMLSSAS IFHLSFISID RYYAVCDPLR YKAKMNILVI CVMIFISWSV PAVFAFGMIF LELNFKGAEE IYYKHVHCRG GCSVFFSKIS GVLTFMTSFY IPGSIMLCVY YRIYLIAKEQ ARLISDANQK LQIGLEMKNG ISQSKERKAV KTLGIVMGVF LICWCPFFIC TVMDPFLHYI IPPTLNDVLI WFGYLNSTFN PMVYAFFYPW FRKALKMMLF GKIFQKDSSR CKLFLELSS // ID ADA1A_ORYLA STANDARD; PRT; 470 AA. AC Q91175; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 21-MAR-2006, entry version 37. DE Alpha-1A adrenergic receptor (Alpha 1A-adrenoceptor) (Alpha 1A- DE adrenoreceptor) (MAR1). OS Oryzias latipes (Medaka fish) (Japanese ricefish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Atherinomorpha; OC Beloniformes; Adrianichthyidae; Oryziinae; Oryzias. OX NCBI_TaxID=8090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96184522; PubMed=8654394; RA Yasuoka A., Abe K., Arai S., Emori Y.; RT "Molecular cloning and functional expression of the alpha1A- RT adrenoceptor of Medaka fish, Oryzias latipes."; RL Eur. J. Biochem. 235:501-507(1996). CC -!- FUNCTION: This alpha-adrenergic receptor mediates its action by CC association with G proteins that activate a phosphatidylinositol- CC calcium second messenger system (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D63859; BAA09921.1; -; Genomic_DNA. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001991; Na/diCO_symport. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00173; EDTRNSPORT. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 470 Alpha-1A adrenergic receptor. FT /FTId=PRO_0000069067. FT TOPO_DOM 1 27 Extracellular (Potential). FT TRANSMEM 28 51 1 (Potential). FT TOPO_DOM 52 64 Cytoplasmic (Potential). FT TRANSMEM 65 88 2 (Potential). FT TOPO_DOM 89 99 Extracellular (Potential). FT TRANSMEM 100 122 3 (Potential). FT TOPO_DOM 123 143 Cytoplasmic (Potential). FT TRANSMEM 144 167 4 (Potential). FT TOPO_DOM 168 181 Extracellular (Potential). FT TRANSMEM 182 205 5 (Potential). FT TOPO_DOM 206 271 Cytoplasmic (Potential). FT TRANSMEM 272 295 6 (Potential). FT TOPO_DOM 296 303 Extracellular (Potential). FT TRANSMEM 304 327 7 (Potential). FT TOPO_DOM 328 470 Cytoplasmic (Potential). FT COMPBIAS 351 354 Poly-His. FT LIPID 343 343 S-palmitoyl cysteine (Potential). FT CARBOHYD 9 9 N-linked (GlcNAc...) (Potential). FT CARBOHYD 12 12 N-linked (GlcNAc...) (Potential). FT DISULFID 99 176 By similarity. SQ SEQUENCE 470 AA; 51925 MW; D4F7A83033061D4E CRC64; MTPSSVTLNC SNCSHVLAPE LNTVKAVVLG MVLGIFILFG VIGNILVILS VVCHRHLQTV TYYFIVNLAV ADLLLSSTVL PFSAIFEILD RWVFGRVFCN IWAAVDVLCC TASIMSLCVI SVDRYIGVSY PLRYPAIMTK RRALLAVMLL WVLSVIISIG PLFGWKEPAP EDETVCKITE EPGYAIFSAV GSFYLPLAII LAMYCRVYVV AQKESRGLKE GQKIEKSDSE QVILRMHRGN TTVSEDEALR SRTHFALRLL KFSREKKAAK TLGIVVGCFV LCWLPFFLVL PIGSIFPAYR PSDTVFKITF WLGYFNSCIN PIIYLCSNQE FKKAFQSLLG VHCLRMTPRA HHHHLSVGQS QTQGHSLTIS LDSKGAPCRL SPSSSVALSR TPSSRDSREW RVFSGGPINS GPGPTEAGRA KVAKLCNKSL HRTCCCILRA RTPTQDPAPL GDLPTIKIHQ LSLSEKGESV // ID ADA1D_HUMAN STANDARD; PRT; 572 AA. AC P25100; Q9NPY0; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 18-APR-2006, entry version 52. DE Alpha-1D adrenergic receptor (Alpha 1D-adrenoceptor) (Alpha 1D- DE adrenoreceptor) (Alpha-1A adrenergic receptor) (Alpha adrenergic DE receptor 1a). GN Name=ADRA1D; Synonyms=ADRA1A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Hippocampus; RX MEDLINE=92028892; PubMed=1656955; RA Bruno J.F., Whittaker J., Song J., Berelowitz M.; RT "Molecular cloning and sequencing of a cDNA encoding a human alpha 1A RT adrenergic receptor."; RL Biochem. Biophys. Res. Commun. 179:1485-1490(1991). RN [2] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Hippocampus; RX MEDLINE=94239386; PubMed=8183249; RA Forray C., Bard J.A., Wetzel J.M., Chiu G., Shapiro E., Tang R., RA Lepor H., Hartig P.R., Weinshank R.L., Branchek T.A., Gluchowski C.; RT "The alpha 1-adrenergic receptor that mediates smooth muscle RT contraction in human prostate has the pharmacological properties of RT the cloned human alpha 1c subtype."; RL Mol. Pharmacol. 45:703-708(1994). RN [3] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=95114877; PubMed=7815325; RA Schwinn D.A., Johnston G.I., Page S.O., Mosley M.J., Wilson K.H., RA Worman N.P., Campbell S., Fidock M.D., Furness L.M., Parry-Smith D.J., RA Peter B., Bailey D.S.; RT "Cloning and pharmacological characterization of human alpha-1 RT adrenergic receptors: sequence corrections and direct comparison with RT other species homologues."; RL J. Pharmacol. Exp. Ther. 272:134-142(1995). RN [4] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=94296402; PubMed=8024574; RA Weinberg D.H., Trivedi P., Tan C.P., Mitra S., Perkins-Barrow A., RA Borkowski D., Strader C.D., Bayne M.; RT "Cloning, expression and characterization of human alpha adrenergic RT receptors alpha 1a, alpha 1b and alpha 1c."; RL Biochem. Biophys. Res. Commun. 201:1296-1304(1994). RN [5] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Placenta, and Prostate; RX MEDLINE=95265059; PubMed=7746284; RA Esbenshade T.A., Hirasawa A., Tsujimoto G., Tanaka T., Yano J., RA Minneman K.P., Murphy T.J.; RT "Cloning of the human alpha 1d-adrenergic receptor and inducible RT expression of three human subtypes in SK-N-MC cells."; RL Mol. Pharmacol. 47:977-985(1995). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). CC -!- FUNCTION: This alpha-adrenergic receptor mediates its effect CC through the influx of extracellular calcium. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M76446; AAA35496.1; -; mRNA. DR EMBL; U03864; AAB60351.1; -; mRNA. DR EMBL; L31772; AAB59487.1; -; mRNA. DR EMBL; S70782; AAB31163.2; -; mRNA. DR EMBL; D29952; BAA06222.1; -; Genomic_DNA. DR EMBL; AL121675; CAC00601.2; -; Genomic_DNA. DR EMBL; AL357040; CAC00601.2; JOINED; Genomic_DNA. DR PIR; I39369; I39369. DR PIR; JH0447; JH0447. DR UniGene; Hs.557; -. DR Ensembl; ENSG00000171873; Homo sapiens. DR HGNC; HGNC:280; ADRA1D. DR MIM; 104219; gene. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0004937; F:alpha1-adrenergic receptor activity; TAS. DR GO; GO:0008283; P:cell proliferation; TAS. DR GO; GO:0007267; P:cell-cell signaling; TAS. DR GO; GO:0007275; P:development; TAS. DR GO; GO:0006259; P:DNA metabolism; TAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS. DR GO; GO:0007188; P:G-protein signaling, coupled to cAMP nucleo...; TAS. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS. DR InterPro; IPR000363; Adren_rcpt_A1A. DR InterPro; IPR002233; Adrnrgc_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01103; ADRENERGICR. DR PRINTS; PR00240; ADRENRGCA1DR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 572 Alpha-1D adrenergic receptor. FT /FTId=PRO_0000069073. FT TOPO_DOM 1 95 Extracellular (Potential). FT TRANSMEM 96 121 1 (Potential). FT TOPO_DOM 122 133 Cytoplasmic (Potential). FT TRANSMEM 134 159 2 (Potential). FT TOPO_DOM 160 169 Extracellular (Potential). FT TRANSMEM 170 192 3 (Potential). FT TOPO_DOM 193 213 Cytoplasmic (Potential). FT TRANSMEM 214 238 4 (Potential). FT TOPO_DOM 239 251 Extracellular (Potential). FT TRANSMEM 252 275 5 (Potential). FT TOPO_DOM 276 348 Cytoplasmic (Potential). FT TRANSMEM 349 373 6 (Potential). FT TOPO_DOM 374 380 Extracellular (Potential). FT TRANSMEM 381 405 7 (Potential). FT TOPO_DOM 406 572 Cytoplasmic (Potential). FT COMPBIAS 422 428 Poly-Arg. FT LIPID 419 419 S-palmitoyl cysteine (Potential). FT CARBOHYD 65 65 N-linked (GlcNAc...) (Potential). FT CARBOHYD 82 82 N-linked (GlcNAc...) (Potential). FT CONFLICT 1 83 MTFRDLLSVSFEGPRPDSSAGGSSAGGGGGSAGGAAPSEGP FT AVGGVPGGAGGGGGVVGAGSGEDNRSSAGEPGSAGAGGDVN FT G -> MAAALRSVMMAGYLSEWRTPTYRSTEMVQRLRMEAV FT QHSTS (in Ref. 1). FT CONFLICT 31 31 S -> G (in Ref. 4). FT CONFLICT 489 572 KPPSAFREWRLLGPFRRPTTQLRAKVSSLSHKIRAGGAQRA FT EAACAQRSEVEAVSLGVPHEVAEGATCQAYELADYSNLRET FT DI -> SHPAPSASGGCWGRSGDPRPSCAPKSPACRTRSPP FT GARSAQRQRAPSAQRWRLCP (in Ref. 1). FT CONFLICT 522 522 R -> P (in Ref. 4). SQ SEQUENCE 572 AA; 60463 MW; EBEB134CF20A4988 CRC64; MTFRDLLSVS FEGPRPDSSA GGSSAGGGGG SAGGAAPSEG PAVGGVPGGA GGGGGVVGAG SGEDNRSSAG EPGSAGAGGD VNGTAAVGGL VVSAQGVGVG VFLAAFILMA VAGNLLVILS VACNRHLQTV TNYFIVNLAV ADLLLSATVL PFSATMEVLG FWAFGRAFCD VWAAVDVLCC TASILSLCTI SVDRYVGVRH SLKYPAIMTE RKAAAILALL WVVALVVSVG PLLGWKEPVP PDERFCGITE EAGYAVFSSV CSFYLPMAVI VVMYCRVYVV ARSTTRSLEA GVKRERGKAS EVVLRIHCRG AATGADGAHG MRSAKGHTFR SSLSVRLLKF SREKKAAKTL AIVVGVFVLC WFPFFFVLPL GSLFPQLKPS EGVFKVIFWL GYFNSCVNPL IYPCSSREFK RAFLRLLRCQ CRRRRRRRPL WRVYGHHWRA STSGLRQDCA PSSGDAPPGA PLALTALPDP DPEPPGTPEM QAPVASRRKP PSAFREWRLL GPFRRPTTQL RAKVSSLSHK IRAGGAQRAE AACAQRSEVE AVSLGVPHEV AEGATCQAYE LADYSNLRET DI // ID 5HT2C_HUMAN STANDARD; PRT; 458 AA. AC P28335; Q9NP28; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 18-APR-2006, entry version 66. DE 5-hydroxytryptamine 2C receptor (5-HT-2C) (Serotonin receptor 2C) (5- DE HT2C) (5-HTR2C) (5HT-1C). GN Name=HTR2C; Synonyms=HTR1C; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain; RX MEDLINE=92109767; PubMed=1722404; RA Saltzman A.G., Morse B., Whitman M.M., Ivanshchenko Y., Jaye M., RA Felder S.; RT "Cloning of the human serotonin 5-HT2 and 5-HT1C receptor subtypes."; RL Biochem. Biophys. Res. Commun. 181:1469-1478(1991). RN [2] RP NUCLEOTIDE SEQUENCE, AND FUNCTION. RC TISSUE=Hippocampus, and Placenta; RX MEDLINE=95203331; PubMed=7895773; DOI=10.1016/0922-4106(94)90042-6; RA Stam N.J., Vanderheyden P., Van Alebeek C., Klomp J., De Boer T., RA Van Delft A.M.L., Olijve W.; RT "Genomic organisation and functional expression of the gene encoding RT the human serotonin 5-HT2C receptor."; RL Eur. J. Pharmacol. 269:339-348(1994). RN [3] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain; RX MEDLINE=97001158; PubMed=8812491; DOI=10.1006/geno.1996.0397; RA Xie E., Zhao L., Levine A.J., Shenk T., Chang L.-S.; RT "The human serotonin 5-HT2C receptor: complete cDNA, genomic RT structure, and alternatively spliced variant."; RL Genomics 35:551-561(1996). RN [4] RP NUCLEOTIDE SEQUENCE, AND RNA EDITING OF POSITIONS 156; 158 AND 160. RC TISSUE=Brain; RX MEDLINE=99127198; PubMed=9928237; RA Niswender C.M., Sanders-Bush E., Emeson R.B.; RT "Identification and characterization of RNA editing events within the RT 5-HT2C receptor."; RL Ann. N. Y. Acad. Sci. 861:38-48(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE OF 1-116. RA Kalicki J., Mead K.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP INTERACTION WITH MPDZ, DOMAIN, MUTAGENESIS OF SER-456; SER-457 AND RP VAL-458, AND N-GLYCOSYLATION. RX MEDLINE=21201137; PubMed=11150294; DOI=10.1074/jbc.M008089200; RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., RA Luebbert H., Ullmer C.; RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with RT PDZ10 of the multi-PDZ domain protein MUPP1."; RL J. Biol. Chem. 276:12974-12982(2001). RN [8] RP VARIANT SER-23. RX MEDLINE=96044432; PubMed=7557992; RA Lappalainen J., Zhang L., Dean M., Oz M., Ozaki N., Yu D., RA Virkkunen M., Weight F., Linnoila M., Goldman D.; RT "Identification, expression, and pharmacology of a Cys23-Ser23 RT substitution in the human 5-HT2c receptor gene (HTR2C)."; RL Genomics 27:274-279(1995). RN [9] RP VARIANT SER-23. RX MEDLINE=99221071; PubMed=10206230; RX DOI=10.1002/(SICI)1096-8628(19990416)88:2<126::AID-AJMG6>3.3.CO;2-D; RA Samochowiec J., Smolka M., Winterer G., Rommelspacher H., RA Schmidt L.G., Sander T.; RT "Association analysis between a Cys23Ser substitution polymorphism of RT the human 5-HT2c receptor gene and neuronal hyperexcitability."; RL Am. J. Med. Genet. 88:126-130(1999). RN [10] RP VARIANT SER-23. RX MEDLINE=20049881; PubMed=10581480; RX DOI=10.1002/(SICI)1096-8628(19991215)88:6<621::AID-AJMG9>3.0.CO;2-H; RA Marshall S.E., Bird T.G., Hart K., Welsh K.I.; RT "Unified approach to the analysis of genetic variation in serotonergic RT pathways."; RL Am. J. Med. Genet. 88:621-627(1999). RN [11] RP VARIANT SER-23. RX MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [12] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor CC mediates its action by association with G proteins that activate a CC phosphatidylinositol-calcium second messenger system. CC -!- SUBUNIT: Interacts with MPDZ. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with MPDZ. CC -!- PTM: N-glycosylated. CC -!- RNA EDITING: Modified_positions=156, 158, 160; Note=Partially CC edited. RNA editing generates receptor isoforms that differ in CC their ability to interact with the phospholipase C signaling CC cascade in a transfected cell line, suggesting that this RNA CC processing event may contribute to the modulation of serotonergic CC neurotransmission in the central nervous system. CC -!- POLYMORPHISM: Position 23 is polymorphic; the frequencies in CC unrelated Caucasians are 0.87 for Cys and 0.13 for Ser. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M81778; AAA60317.1; -; mRNA. DR EMBL; X80763; CAB59978.1; -; Genomic_DNA. DR EMBL; U49516; AAB40898.1; -; mRNA. DR EMBL; AF208053; AAF35842.1; -; mRNA. DR EMBL; AF498983; AAM21130.1; -; mRNA. DR EMBL; AC004822; AAC71658.1; -; Genomic_DNA. DR PIR; JS0616; JS0616. DR UniGene; Hs.149037; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000147246; Homo sapiens. DR HGNC; HGNC:5295; HTR2C. DR MIM; 312861; gene. DR GO; GO:0007631; P:feeding behavior; TAS. DR GO; GO:0007268; P:synaptic transmission; TAS. DR InterPro; IPR000377; 5HT2C_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00517; 5HT2CRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; KW Receptor; RNA editing; Transducer; Transmembrane. FT CHAIN 1 458 5-hydroxytryptamine 2C receptor. FT /FTId=PRO_0000068958. FT TOPO_DOM 1 52 Extracellular (Potential). FT TRANSMEM 53 78 1 (Potential). FT TOPO_DOM 79 89 Cytoplasmic (Potential). FT TRANSMEM 90 110 2 (Potential). FT TOPO_DOM 111 127 Extracellular (Potential). FT TRANSMEM 128 150 3 (Potential). FT TOPO_DOM 151 170 Cytoplasmic (Potential). FT TRANSMEM 171 193 4 (Potential). FT TOPO_DOM 194 213 Extracellular (Potential). FT TRANSMEM 214 235 5 (Potential). FT TOPO_DOM 236 311 Cytoplasmic (Potential). FT TRANSMEM 312 333 6 (Potential). FT TOPO_DOM 334 348 Extracellular (Potential). FT TRANSMEM 349 371 7 (Potential). FT TOPO_DOM 372 458 Cytoplasmic (Potential). FT MOTIF 456 458 PDZ-binding. FT CARBOHYD 39 39 N-linked (GlcNAc...) (Probable). FT DISULFID 127 207 By similarity. FT VARIANT 23 23 C -> S (in dbSNP:6318). FT /FTId=VAR_003450. FT VARIANT 156 156 I -> V (in RNA edited version). FT /FTId=VAR_010166. FT VARIANT 158 158 N -> S (in RNA edited version). FT /FTId=VAR_010167. FT VARIANT 160 160 I -> V (in RNA edited version). FT /FTId=VAR_010168. FT MUTAGEN 456 456 S->A: Loss of interaction with MPDZ. FT MUTAGEN 456 456 S->T: No effect on interaction with MPDZ. FT MUTAGEN 457 457 S->A: No effect on interaction with MPDZ. FT MUTAGEN 458 458 V->A: Loss of interaction with MPDZ. SQ SEQUENCE 458 AA; 51821 MW; 9E76B3FFD3E09C93 CRC64; MVNLRNAVHS FLVHLIGLLV WQCDISVSPV AAIVTDIFNT SDGGRFKFPD GVQNWPALSI VIIIIMTIGG NILVIMAVSM EKKLHNATNY FLMSLAIADM LVGLLVMPLS LLAILYDYVW PLPRYLCPVW ISLDVLFSTA SIMHLCAISL DRYVAIRNPI EHSRFNSRTK AIMKIAIVWA ISIGVSVPIP VIGLRDEEKV FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIYV LRRQALMLLH GHTEEPPGLS LDFLKCCKRN TAEEENSANP NQDQNARRRK KKERRPRGTM QAINNERKAS KVLGIVFFVF LIMWCPFFIT NILSVLCEKS CNQKLMEKLL NVFVWIGYVC SGINPLVYTL FNKIYRRAFS NYLRCNYKVE KKPPVRQIPR VAATALSGRE LNVNIYRHTN EPVIEKASDN EPGIEMQVEN LELPVNPSSV VSERISSV // ID HRH1_GORGO STANDARD; PRT; 487 AA. AC Q9N2B1; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 18-APR-2006, entry version 24. DE Histamine H1 receptor. GN Name=HRH1; OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kitano T., Kobayakawa H., Saitou N.; RT "Silver project."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: In peripheral tissues, the H1 subclass of histamine CC receptors mediates the contraction of smooth muscles, increase in CC capillary permeability due to contraction of terminal venules, and CC catecholamine release from adrenal medulla, as well as mediating CC neurotransmission in the central nervous system (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Potential sites of phosphorylation in the third cytoplasmic CC loop may play an important role in regulating signal transduction CC through the receptor molecule (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041382; BAA94467.1; -; Genomic_DNA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000921; H1_rcpt. DR PANTHER; PTHR19266:SF77; H1_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00530; HISTAMINEH1R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Receptor; Transducer; Transmembrane. FT CHAIN 1 487 Histamine H1 receptor. FT /FTId=PRO_0000069675. FT TOPO_DOM 1 29 Extracellular (Potential). FT TRANSMEM 30 49 1 (Potential). FT TOPO_DOM 50 63 Cytoplasmic (Potential). FT TRANSMEM 64 83 2 (Potential). FT TOPO_DOM 84 101 Extracellular (Potential). FT TRANSMEM 102 123 3 (Potential). FT TOPO_DOM 124 145 Cytoplasmic (Potential). FT TRANSMEM 146 165 4 (Potential). FT TOPO_DOM 166 189 Extracellular (Potential). FT TRANSMEM 190 210 5 (Potential). FT TOPO_DOM 211 418 Cytoplasmic (Potential). FT TRANSMEM 419 438 6 (Potential). FT TOPO_DOM 439 450 Extracellular (Potential). FT TRANSMEM 451 470 7 (Potential). FT TOPO_DOM 471 487 Cytoplasmic (Potential). FT LIPID 445 445 S-palmitoyl cysteine (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 18 18 N-linked (GlcNAc...) (Potential). FT DISULFID 100 180 By similarity. SQ SEQUENCE 487 AA; 55623 MW; 1112546AEFA51521 CRC64; MSLPNSSCLL EDKMCESNKT TMASPQLMPL VVVLSTICLV TVGLNLLVLY AVRSERKLHT VGNLYIVSLS VADLIVGAVV MPMNILYLLM SKWSLGRPLC LFWLSMDYVA STASIFSVFI LCIDRYRSVQ QPLRYLKYRT KTRASATILG AWFLSFLWVI PILGWNHFMQ QTSVRREDKC ETDFYDVTWF KVMTAIINFY LPTLLMLWFY AKIYKAVRQH CQHRELINGS LPSFSEIKLR PENPKGDAKK PGKESPWEVL KRKPKDAGGG SVLKSPSQTP KEMKSPVVFS QEDDREVDKL HCFPLDIVHM QTAAEGSSRD YVAVNQSHGQ LKTDEQGLNT HGASEISEDQ MLGDSQSFSR TDSDTTTETA SGKGKLRSGS NTGLGYIKFT WKRLRSHSRQ YVSGLHMNRE RKAAKQLGFI MAAFILCWIP YFIFFMVIAF CKNCCNEHLH MFTIWLGYIN STLNPLIYPL CNENFKKTFK RILHIRS // ID ACM1_HUMAN STANDARD; PRT; 460 AA. AC P11229; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 2. DT 18-APR-2006, entry version 73. DE Muscarinic acetylcholine receptor M1. GN Name=CHRM1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=88096607; PubMed=3697105; RA Allard W.J., Sigal I.S., Dixon R.A.F.; RT "Sequence of the gene encoding the human M1 muscarinic acetylcholine RT receptor."; RL Nucleic Acids Res. 15:10604-10604(1987). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=90245684; PubMed=2336407; RA Chapman C.G., Browne M.J.; RT "Isolation of the human ml (Hml) muscarinic acetylcholine receptor RT gene by PCR amplification."; RL Nucleic Acids Res. 18:2191-2191(1990). RN [3] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=88166632; PubMed=3443095; RA Peralta E.G., Ashkenazi A., Winslow J.W., Smith D.H., Ramachandran J., RA Capon D.J.; RT "Distinct primary structures, ligand-binding properties and tissue- RT specific expression of four human muscarinic acetylcholine RT receptors."; RL EMBO J. 6:3923-3929(1987). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP MUTAGENESIS. RX MEDLINE=93075202; PubMed=1445347; RA Arden J.R., Nagata O., Shockley M.S., Philip M., Lameh J., Sadee W.; RT "Mutational analysis of third cytoplasmic loop domains in G-protein RT coupling of the HM1 muscarinic receptor."; RL Biochem. Biophys. Res. Commun. 188:1111-1115(1992). CC -!- FUNCTION: The muscarinic acetylcholine receptor mediates various CC cellular responses, including inhibition of adenylate cyclase, CC breakdown of phosphoinositides and modulation of potassium CC channels through the action of G proteins. Primary transducing CC effect is Pi turnover. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X52068; CAA36291.1; -; Genomic_DNA. DR EMBL; X15263; CAA33334.1; -; Genomic_DNA. DR EMBL; Y00508; CAA68560.1; -; Genomic_DNA. DR EMBL; AF498915; AAM18938.1; -; mRNA. DR EMBL; BC007740; AAH07740.1; -; mRNA. DR EMBL; BC022984; AAH22984.1; -; mRNA. DR PIR; S09508; S09508. DR UniGene; Hs.247917; -. DR HSSP; P08913; 1HLL. DR Ensembl; ENSG00000168539; Homo sapiens. DR H-InvDB; HIX0009731; -. DR HGNC; HGNC:1950; CHRM1. DR MIM; 118510; gene. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0005624; C:membrane fraction; TAS. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0004981; F:muscarinic acetylcholine receptor activity; TAS. DR GO; GO:0004435; F:phosphoinositide phospholipase C activity; TAS. DR GO; GO:0007213; P:acetylcholine receptor signaling, muscarini...; TAS. DR GO; GO:0008283; P:cell proliferation; TAS. DR GO; GO:0007207; P:muscarinic acetylcholine receptor, phosphol...; TAS. DR GO; GO:0007399; P:nervous system development; TAS. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS. DR GO; GO:0007205; P:protein kinase C activation; TAS. DR GO; GO:0006464; P:protein modification; TAS. DR GO; GO:0007165; P:signal transduction; TAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR002228; Musac_M1_rcpt. DR InterPro; IPR000995; Musac_rcpt. DR PANTHER; PTHR19266:SF86; MusacM1_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00243; MUSCARINICR. DR PRINTS; PR00538; MUSCRINICM1R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphorylation; KW Postsynaptic membrane; Receptor; Transducer; Transmembrane. FT CHAIN 1 460 Muscarinic acetylcholine receptor M1. FT /FTId=PRO_0000069015. FT TOPO_DOM 1 24 Extracellular (Potential). FT TRANSMEM 25 47 1 (Potential). FT TOPO_DOM 48 61 Cytoplasmic (Potential). FT TRANSMEM 62 82 2 (Potential). FT TOPO_DOM 83 99 Extracellular (Potential). FT TRANSMEM 100 121 3 (Potential). FT TOPO_DOM 122 141 Cytoplasmic (Potential). FT TRANSMEM 142 164 4 (Potential). FT TOPO_DOM 165 186 Extracellular (Potential). FT TRANSMEM 187 209 5 (Potential). FT TOPO_DOM 210 366 Cytoplasmic (Potential). FT TRANSMEM 367 387 6 (Potential). FT TOPO_DOM 388 401 Extracellular (Potential). FT TRANSMEM 402 421 7 (Potential). FT TOPO_DOM 422 460 Cytoplasmic (Potential). FT MOD_RES 428 428 Phosphothreonine (Potential). FT MOD_RES 451 451 Phosphoserine (Potential). FT MOD_RES 455 455 Phosphothreonine (Potential). FT MOD_RES 457 457 Phosphoserine (Potential). FT CARBOHYD 2 2 N-linked (GlcNAc...) (Probable). FT CARBOHYD 12 12 N-linked (GlcNAc...) (Probable). FT DISULFID 98 178 By similarity. FT CONFLICT 173 173 V -> M (in Ref. 3). SQ SEQUENCE 460 AA; 51421 MW; 567C20F63541C8D0 CRC64; MNTSAPPAVS PNITVLAPGK GPWQVAFIGI TTGLLSLATV TGNLLVLISF KVNTELKTVN NYFLLSLACA DLIIGTFSMN LYTTYLLMGH WALGTLACDL WLALDYVASN ASVMNLLLIS FDRYFSVTRP LSYRAKRTPR RAALMIGLAW LVSFVLWAPA ILFWQYLVGE RTVLAGQCYI QFLSQPIITF GTAMAAFYLP VTVMCTLYWR IYRETENRAR ELAALQGSET PGKGGGSSSS SERSQPGAEG SPETPPGRCC RCCRAPRLLQ AYSWKEEEEE DEGSMESLTS SEGEEPGSEV VIKMPMVDPE AQAPTKQPPR SSPNTVKRPT KKGRDRAGKG QKPRGKEQLA KRKTFSLVKE KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW ELGYWLCYVN STINPMCYAL CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC // ID ACM3_BOVIN STANDARD; PRT; 590 AA. AC P41984; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 04-APR-2006, entry version 39. DE Muscarinic acetylcholine receptor M3. GN Name=CHRM3; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=94339178; PubMed=8061048; DOI=10.1016/0167-4889(94)90085-X; RA Lee P.H., Hodges P.K., Glickman F., Chang K.J.; RT "Cloning and expression of a cDNA encoding bovine muscarinic RT acetylcholine m3 receptor."; RL Biochim. Biophys. Acta 1223:151-154(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 327-467. RC TISSUE=Adrenal gland; RA Sui A.-L., Chou W.-Y., Kao L.-S.; RT "Presence of multiple muscarinic receptor subtypes in bovine RT chromaffin cells - analysis by polymerase chain reaction."; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The muscarinic acetylcholine receptor mediates various CC cellular responses, including inhibition of adenylate cyclase, CC breakdown of phosphoinositides and modulation of potassium CC channels through the action of G proteins. Primary transducing CC effect is Pi turnover. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U08286; AAA51866.1; -; mRNA. DR EMBL; L27103; AAA30653.1; -; mRNA. DR PIR; S47572; S47572. DR UniGene; Bt.501; -. DR HSSP; P08913; 1HLL. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001183; Musac_M3_rcpt. DR InterPro; IPR000995; Musac_rcpt. DR PANTHER; PTHR19266:SF87; MusacM3_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00243; MUSCARINICR. DR PRINTS; PR00540; MUSCRINICM3R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphorylation; KW Postsynaptic membrane; Receptor; Transducer; Transmembrane. FT CHAIN 1 590 Muscarinic acetylcholine receptor M3. FT /FTId=PRO_0000069027. FT TOPO_DOM 1 67 Extracellular (Potential). FT TRANSMEM 68 91 1 (Potential). FT TOPO_DOM 92 104 Cytoplasmic (Potential). FT TRANSMEM 105 125 2 (Potential). FT TOPO_DOM 126 142 Extracellular (Potential). FT TRANSMEM 143 164 3 (Potential). FT TOPO_DOM 165 184 Cytoplasmic (Potential). FT TRANSMEM 185 207 4 (Potential). FT TOPO_DOM 208 229 Extracellular (Potential). FT TRANSMEM 230 252 5 (Potential). FT TOPO_DOM 253 492 Cytoplasmic (Potential). FT TRANSMEM 493 513 6 (Potential). FT TOPO_DOM 514 527 Extracellular (Potential). FT TRANSMEM 528 547 7 (Potential). FT TOPO_DOM 548 590 Cytoplasmic (Potential). FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). FT CARBOHYD 7 7 N-linked (GlcNAc...) (Potential). FT CARBOHYD 15 15 N-linked (GlcNAc...) (Potential). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT CARBOHYD 53 53 N-linked (GlcNAc...) (Potential). FT DISULFID 141 221 By similarity. FT CONFLICT 424 424 F -> S (in Ref. 2). FT CONFLICT 438 438 A -> G (in Ref. 2). FT CONFLICT 440 440 A -> G (in Ref. 2). FT CONFLICT 452 452 A -> G (in Ref. 2). FT CONFLICT 461 461 A -> G (in Ref. 2). FT CONFLICT 467 467 F -> L (in Ref. 2). SQ SEQUENCE 590 AA; 66103 MW; 4DE04EDE33CCA8D6 CRC64; MTLHNNNTTS PLFPNISSSW IHGPSDTGLP PGTVTHFGSY NISRAAGNLS SPNGTTSDPL GGHTIWQVVF IAFLTGVLAL VTIIGNILVI VAFKVNKQLK TVNNYFLLSL ACADLIIGVI SMNLFTTYII MNRWALGNLA CDLWLSIDYV ASNASVMNLL VISFDRYFSI TRPLTYRAKR TTKRAGVMIG LAWVISFILW APAILFWQYF VGKRTVPPGE CFIQFLSEPT ITFGTAIAAF YMPVTIMTIL YWRIYKETEK RTKELAGLQA SGTEAEAENF VHPTGSSRSC SSYELQQQSM KRSARRKYGR CHFWFTTKSW KPSAEQMDQD HSSSDSWNNN DAAASLENSA SSDEEDIGSE TRAIYSIVLK LPGHSTILNS TKLPSSDNLQ VPEEELGSVG LERKPSKLQT QQSMDDGGSF QKSFSKLPIQ LESAVDTAKA SDVNSSVGKT TATLPLSFKE ATLAKRFALK TRSQITKRKR MSLIKEKKAA QTLSAILLAF IITWTPYNIM VLVNTFCDSC IPKTYWNLGY WLCYINSTVN PVCYALCNKT FRNTFKMLLL CQCDKRKRRK QQYQQRQSVI FHKRVPEQAL // ID ACM4_XENLA STANDARD; PRT; 484 AA. AC P30544; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 07-MAR-2006, entry version 42. DE Muscarinic acetylcholine receptor M4. GN Name=chrm4; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Ovary; RX MEDLINE=95010703; PubMed=7925970; DOI=10.1016/0014-5793(94)00957-0; RA Herrera L., Carvallo P., Antonelli M., Olate J.; RT "Cloning of a Xenopus laevis muscarinic receptor encoded by an RT intronless gene."; RL FEBS Lett. 352:175-179(1994). CC -!- FUNCTION: The muscarinic acetylcholine receptor mediates various CC cellular responses, including inhibition of adenylate cyclase, CC breakdown of phosphoinositides and modulation of potassium CC channels through the action of G proteins. Primary transducing CC effect is inhibition of adenylate cyclase. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X65865; CAA46694.1; -; Genomic_DNA. DR PIR; S48657; S48657. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001432; Musac_M4_rcpt. DR InterPro; IPR000995; Musac_rcpt. DR PANTHER; PTHR19266:SF85; M4_receptor; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00243; MUSCARINICR. DR PRINTS; PR00541; MUSCRINICM4R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphorylation; KW Postsynaptic membrane; Receptor; Transducer; Transmembrane. FT CHAIN 1 484 Muscarinic acetylcholine receptor M4. FT /FTId=PRO_0000069041. FT TOPO_DOM 1 32 Extracellular (Potential). FT TRANSMEM 33 55 1 (Potential). FT TOPO_DOM 56 69 Cytoplasmic (Potential). FT TRANSMEM 70 90 2 (Potential). FT TOPO_DOM 91 107 Extracellular (Potential). FT TRANSMEM 108 129 3 (Potential). FT TOPO_DOM 130 149 Cytoplasmic (Potential). FT TRANSMEM 150 172 4 (Potential). FT TOPO_DOM 173 194 Extracellular (Potential). FT TRANSMEM 195 217 5 (Potential). FT TOPO_DOM 218 406 Cytoplasmic (Potential). FT TRANSMEM 407 427 6 (Potential). FT TOPO_DOM 428 441 Extracellular (Potential). FT TRANSMEM 442 461 7 (Potential). FT TOPO_DOM 462 484 Cytoplasmic (Potential). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). FT DISULFID 106 186 By similarity. SQ SEQUENCE 484 AA; 54137 MW; D83BD856DE302BE8 CRC64; MENDTWENES SASNHSIDET IVEIPGKYQT MEMIFIATVT GSLSLVTVVG NILVMLSIKV NRQLQTVNNY FLFSLACADL IIGVFSMNLY SLYIIKGYWP LGPIVCDLWL ALDYVVSNAS VMNLLIISLE RXFCVTKPLT YPARRTTKMA GLMIAAAWLL SFELWAPAIL FWQFIVGQRT VPSGECYIQF LSNPAVTFGT AIAAFYLPVV IMTILYIHIS LASRSRVRRH CPETRQEKKK PISSMKSLLI KQTKNIPKQD AGDKVVEKKN GVSNGKIEKS MTNLQTAEEK ETSNESSSAS LSHNPPEKQP LSEASSGVVL APTQSMPPLP AKANTASKWS KIKIVTKQTG NECVTAIEIV PECAIPLPEQ ANNRPVNVAR KFASIARNQV RKKRQMAARE KKVTRTIFAI LLAFIITWTP YNVMVLINTF CQTCIPETIW YIGYWLCYVN STINPACYAL CNATFKKTFK HLLMCQYKSI GTAR // ID ACM1_DROME STANDARD; PRT; 805 AA. AC P16395; Q8MLP2; Q9W180; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 04-APR-2006, entry version 57. DE Muscarinic acetylcholine receptor DM1. GN Name=mAcR-60C; Synonyms=AcrC; ORFNames=CG4356; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM A). RX MEDLINE=90005981; PubMed=2507354; DOI=10.1016/0014-5793(89)81095-6; RA Onai T., Fitzgerald M.G., Arakawa S., Gocayne J.D., Urquhart D.A., RA Hall L.M., Fraser C.M., McCombie W.R., Venter J.C.; RT "Cloning, sequence analysis and chromosome localization of a RT Drosophila muscarinic acetylcholine receptor."; RL FEBS Lett. 255:219-225(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE OF 45-805 (ISOFORM B), AND FUNCTION. RC STRAIN=Oregon-R; RX MEDLINE=90046926; PubMed=2510174; RA Shapiro R.A., Wakimoto B.T., Subers E.M., Nathanson N.M.; RT "Characterization and functional expression in mammalian cells of RT genomic and cDNA clones encoding a Drosophila muscarinic acetylcholine RT receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9039-9043(1989). RN [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX MEDLINE=96047550; PubMed=7550280; RA Harrison J.B., Chen H.H., Blake A.D., Huskisson N.S., Barker P., RA Sattelle D.B.; RT "Localization in the nervous system of Drosophila melanogaster of a C- RT terminus anti-peptide antibody to a cloned Drosophila muscarinic RT acetylcholine receptor."; RL J. Neuroendocrinol. 7:347-352(1995). CC -!- FUNCTION: The muscarinic acetylcholine receptor mediates various CC cellular responses, including inhibition of adenylate cyclase, CC breakdown of phosphoinositides and modulation of potassium CC channels through the action of G proteins. Primary transducing CC effect is Pi turnover. May have a role in the processing of CC olfactory and mechanosensory signals; regulation of CC neurosecretion. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=P16395-1; Sequence=Displayed; CC Name=A; CC IsoId=P16395-2; Sequence=VSP_012002; CC -!- TISSUE SPECIFICITY: Intense staining in the glomeruli of the CC antennal lobes, the region of the nervous system containing CC terminals of antennal olfactory sensory neurons and mechanosensory CC neurons. Also a discrete group of neurosecretory cells in the pars CC intercerebralis of the brain. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- CAUTION: Ref.4 sequence differs from that shown due to a CC frameshift in position 57. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M23412; AAA28676.1; -; mRNA. DR EMBL; AE003464; AAF47197.1; -; Genomic_DNA. DR EMBL; AE003464; AAM68310.1; -; Genomic_DNA. DR EMBL; M27495; AAA85449.1; ALT_FRAME; mRNA. DR PIR; S05661; S05661. DR UniGene; Dm.2775; -. DR Ensembl; CG4356; Drosophila melanogaster. DR FlyBase; FBgn0000037; mAcR-60C. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0004981; F:muscarinic acetylcholine receptor activity; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000995; Musac_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00243; MUSCARINICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; Complete proteome; G-protein coupled receptor; KW Glycoprotein; Membrane; Phosphorylation; Postsynaptic membrane; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 805 Muscarinic acetylcholine receptor DM1. FT /FTId=PRO_0000069051. FT TOPO_DOM 1 100 Extracellular (Potential). FT TRANSMEM 101 121 1 (Potential). FT TOPO_DOM 122 141 Cytoplasmic (Potential). FT TRANSMEM 142 162 2 (Potential). FT TOPO_DOM 163 177 Extracellular (Potential). FT TRANSMEM 178 198 3 (Potential). FT TOPO_DOM 199 220 Cytoplasmic (Potential). FT TRANSMEM 221 241 4 (Potential). FT TOPO_DOM 242 266 Extracellular (Potential). FT TRANSMEM 267 287 5 (Potential). FT TOPO_DOM 288 718 Cytoplasmic (Potential). FT TRANSMEM 719 739 6 (Potential). FT TOPO_DOM 740 752 Extracellular (Potential). FT TRANSMEM 753 773 7 (Potential). FT TOPO_DOM 774 805 Cytoplasmic (Potential). FT COMPBIAS 24 69 Thr-rich. FT COMPBIAS 502 534 Asn-rich. FT CARBOHYD 65 65 N-linked (GlcNAc...) (Potential). FT CARBOHYD 84 84 N-linked (GlcNAc...) (Potential). FT CARBOHYD 87 87 N-linked (GlcNAc...) (Potential). FT VARSPLIC 427 443 Missing (in isoform A). FT /FTId=VSP_012002. FT CONFLICT 23 23 K -> R (in Ref. 1). FT CONFLICT 155 155 A -> T (in Ref. 4). FT CONFLICT 199 199 S -> N (in Ref. 4). FT CONFLICT 216 216 R -> G (in Ref. 4). FT CONFLICT 227 227 Missing (in Ref. 4). FT CONFLICT 331 331 G -> P (in Ref. 4). FT CONFLICT 355 355 P -> A (in Ref. 1 and 4). FT CONFLICT 462 462 G -> A (in Ref. 1). FT CONFLICT 532 532 A -> T (in Ref. 4). FT CONFLICT 687 688 VG -> C (in Ref. 4). FT CONFLICT 696 697 AR -> P (in Ref. 4). FT CONFLICT 737 739 VLI -> CLS (in Ref. 4). FT CONFLICT 771 771 C -> S (in Ref. 4). FT CONFLICT 797 805 EGMVRGVYN -> DFMYAASTIR (in Ref. 4). SQ SEQUENCE 805 AA; 86623 MW; 97A9229CAA5BBED8 CRC64; MEPVMSLALA AHGPPSILEP LFKTVTTSTT TTTTTTTSTT TTTASPAGYS PGYPGTTLLT ALFENLTSTA ASGLYDPYSG MYGNQTNGTI GFETKGPRYS LASMVVMGFV AAILSTVTVA GNVMVMISFK IDKQLQTISN YFLFSLAIAD FAIGAISMPL FAVTTILGYW PLGPIVCDTW LALDYLASNA SVLNLLIISF DRYFSVTRPL TYRAKRTTNR AAVMIGAAWG ISLLLWPPWI YSWPYIEGKR TVPKDECYIQ FIETNQYITF GTALAAFYFP VTIMCFLYWR IWRETKKRQK DLPNLQAGKK DSSKRSNSSD ENTVVNHASG GLLAFAQVGG NDHDTWRRPR SESSPDAESV YMTNMVIDSG YHGMHSRKSS IKSTNTIKKS YTCFGSIKEW CIAWWHSGRE DSDDFAYEQE EPSDLGYATP VTIETPLQSS VSRCTSMNVM RDNYSMGGSV SGVRPPSILL SDVSPTPLPR PPLASISQLQ EMSAVTASTT ANVNTSGNGN GAINNNNNAS HNGNGAVNGN GAGNGSGIGL GTTGNATHRD SRTLPVINRI NSRSVSQDSV YTILIRLPSD GASSNAANGG GGGPGAGAAA SASLSMQGDC APSIKMIHED GPTTTAAAAP LASAAATRRP LPSRDSEFSL PLGRRMSHAQ HDARLLNAKV IPKQLGKAGG GAAGGGVGGA HALMNARNAA KKKKKSQEKR QESKAAKTLS AILLSFIITW TPYNILVLIK PLTTCSDCIP TELWDFFYAL CYINSTINPM CYALCNATFR RTYVRILTCK WHTRNREGMV RGVYN // ID HRH3_MOUSE STANDARD; PRT; 445 AA. AC P58406; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2001, sequence version 1. DT 18-APR-2006, entry version 33. DE Histamine H3 receptor (HH3R). GN Name=Hrh3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; RA Coge F., Rique H., Levacher B., Leopold O., Guenin S.-P., Boutin J.A., RA Galizzi J.-P.; RT "Cloning of mouse histamine H3 receptor."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The H3 subclass of histamine receptors could mediate the CC histamine signals in CNS and peripheral nervous system. Signals CC through the inhibition of adenylate cyclase and displays high CC constitutive activity (spontaneous activity in the absence of CC agonist) (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY044153; AAK72406.1; -; mRNA. DR UniGene; Mm.285360; -. DR Ensembl; ENSMUSG00000039059; Mus musculus. DR MGI; MGI:2139279; Hrh3. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR003980; H3_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01471; HISTAMINEH3R. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 445 Histamine H3 receptor. FT /FTId=PRO_0000069691. FT TOPO_DOM 1 39 Extracellular (Potential). FT TRANSMEM 40 60 Potential. FT TOPO_DOM 61 70 Cytoplasmic (Potential). FT TRANSMEM 71 91 Potential. FT TOPO_DOM 92 108 Extracellular (Potential). FT TRANSMEM 109 129 Potential. FT TOPO_DOM 130 156 Cytoplasmic (Potential). FT TRANSMEM 157 177 Potential. FT TOPO_DOM 178 196 Extracellular (Potential). FT TRANSMEM 197 217 Potential. FT TOPO_DOM 218 359 Cytoplasmic (Potential). FT TRANSMEM 360 380 Potential. FT TOPO_DOM 381 396 Extracellular (Potential). FT TRANSMEM 397 417 Potential. FT TOPO_DOM 418 445 Cytoplasmic (Potential). FT COMPBIAS 20 23 Poly-Ala. FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 445 AA; 48541 MW; B8D406E29E1F3C5F CRC64; MERAPPDGLM NASGALAGEA AAAGGARGFS AAWTAVLAAL MALLIVATVL GNALVMLAFV ADSSLRTQNN FFLLNLAISD FLVGAFCIPL YVPYVLTGRW TFGRGLCKLW LVVDYLLCAS SVFNIVLISY DRFLSVTRAV SYRAQQGDTR RAVRKMALVW VLAFLLYGPA ILSWEYLSGG SSIPEGHCYA EFFYNWYFLI TASTLEFFTP FLSVTFFNLS IYLNIQRRTR LRLDGGREAG PEPPPDAQPS PPPAPPSCWG CWPKGHGEAM PLHRYGVGEA GPGVETGEAG LGGGSGGGAA ASPTSSSGSS SRGTERPRSL KRGSKPSASS ASLEKRMKMV SQSITQRFRL SRDKKVAKSL AIIVSIFGLC WAPYTLLMII RAACHGHCVP DYWYETSFWL LWANSAVNPV LYPLCHYSFR RAFTKLLCPQ KLKVQPHGSL EQCWK // ID 5HTB1_APLCA STANDARD; PRT; 453 AA. AC Q16950; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 07-FEB-2006, entry version 28. DE 5-hydroxytryptamine 1 receptor (5-HTB1) (Serotonin receptor 1). GN Name=5HTB1; OS Aplysia californica (California sea hare). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Orthogastropoda; OC Apogastropoda; Heterobranchia; Euthyneura; Opisthobranchia; Anaspidea; OC Aplysioidea; Aplysiidae; Aplysia. OX NCBI_TaxID=6500; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96066780; PubMed=7472509; RA Li X.C., Giot J.F., Kuhl D., Hen R., Kandel E.R.; RT "Cloning and characterization of two related serotonergic receptors RT from the brain and the reproductive system of Aplysia that activate RT phospholipase C."; RL J. Neurosci. 15:7585-7591(1995). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin). 5-HT plays important roles in CC various behavioral and physiological processes in aplysia. These CC include feeding, locomotion, circadian rhythm, learning and CC memory, synaptic plasticity, and synaptic growth. This receptor is CC mediated by G proteins that stimulate phospholipase C. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Reproductive system. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43557; AAA93101.1; -; Genomic_DNA. DR HSSP; P29274; 1MMH. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Membrane; Receptor; Transducer; KW Transmembrane. FT CHAIN 1 453 5-hydroxytryptamine 1 receptor. FT /FTId=PRO_0000068983. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 57 1 (Potential). FT TOPO_DOM 58 74 Cytoplasmic (Potential). FT TRANSMEM 75 94 2 (Potential). FT TOPO_DOM 95 110 Extracellular (Potential). FT TRANSMEM 111 133 3 (Potential). FT TOPO_DOM 134 153 Cytoplasmic (Potential). FT TRANSMEM 154 175 4 (Potential). FT TOPO_DOM 176 223 Extracellular (Potential). FT TRANSMEM 224 244 5 (Potential). FT TOPO_DOM 245 301 Cytoplasmic (Potential). FT TRANSMEM 302 322 6 (Potential). FT TOPO_DOM 323 331 Extracellular (Potential). FT TRANSMEM 332 352 7 (Potential). FT TOPO_DOM 353 453 Cytoplasmic (Potential). FT DISULFID 110 225 By similarity. SQ SEQUENCE 453 AA; 50622 MW; 227B997840C0C820 CRC64; MKSLKSSTHD VPHPEHVVWA PPAYDEQHHL FFSHGTVLIG IVGSLIITVA VVGNVLVCLA IFTEPILSHS KSNFFIVSLA VADLLLALLV MTFALVNDMY GYWLFGETFC FIWMSADVMC ETASIFSICV ISYDRLKQVQ KPLHYEEFMT TTRALLIIAC LWICSFVLSF VPIFLEWHEL SVEEIKAIFK DNKTEKEKAL EAHNFSSALN QTLGDNQKSN AKHVCLFDVH FTYSVIYSFI CFYVPCTLML TNYLRLFLIA QTHQVRIRSL QMTNPPQLRG QGASSYRNQG TQGSKAARTL TIITGTFLAC WLPFFIINPI AAADEHLIPL ECFMVTIWLG YFNSSVNPII YGTSNSKFRA AFKRLLRCRS VKSVVGSISP VSPAYRAFSW IRPSRLDLSS SEHPSDACDT GRGKNSKGGD CATADPTKPD VSVSEEIIYA GTKVFDSDTA FSS // ID ACM2_CAEEL STANDARD; PRT; 627 AA. AC Q09388; Q09561; Q95WX7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 3. DT 04-APR-2006, entry version 49. DE Probable muscarinic acetylcholine receptor gar-2 (G-protein linked DE acetylcholine receptor 2). GN Name=gar-2; ORFNames=F47D12.1/F47D12.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND TISSUE SPECIFICITY. RC STRAIN=Bristol N2; RX MEDLINE=20490918; PubMed=11032868; RA Lee Y.-S., Park Y.-S., Nam S., Suh S.J., Lee J., Kaang B.-K., RA Cho N.J.; RT "Characterization of GAR-2, a novel G protein-linked acetylcholine RT receptor from Caenorhabditis elegans."; RL J. Neurochem. 75:1800-1809(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RX MEDLINE=21556942; PubMed=11700045; DOI=10.1006/bbrc.2001.5909; RA Suh S.J., Park Y.-S., Lee Y.-S., Cho T.J., Kaang B.-K., Cho N.J.; RT "Three functional isoforms of GAR-2, a Caenorhabditis elegans G- RT protein-linked acetylcholine receptor, are produced by alternative RT splicing."; RL Biochem. Biophys. Res. Commun. 288:1238-1243(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [4] RP SEQUENCE REVISION. RG WormBase consortium; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The muscarinic acetylcholine receptor mediates various CC cellular responses, including inhibition of adenylate cyclase, CC breakdown of phosphoinositides and modulation of potassium CC channels through the action of G proteins. Primary transducing CC effect is Pi turnover. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; CC IsoId=Q09388-1; Sequence=Displayed; CC Name=b; Synonyms=c; CC IsoId=Q09388-2; Sequence=VSP_001862; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in head region of the larva. In CC adults, expression is seen in putative sensory neurons, many cells CC of the ventral cord and in the hermaphrodite-specific neuron (HSN) CC motor neurons. CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from CC embryonic to adult stage. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF272738; AAK94896.1; -; mRNA. DR EMBL; AY053365; AAL15153.1; -; mRNA. DR EMBL; U22831; AAL65783.1; -; Genomic_DNA. DR EMBL; U22831; AAL65784.1; -; Genomic_DNA. DR UniGene; Cel.8076; -. DR Ensembl; F47D12.1; Caenorhabditis elegans. DR WormBase; WBGene00001518; gar-2. DR WormPep; F47D12.1a; CE30134. DR WormPep; F47D12.1b; CE30135. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000995; Musac_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00243; MUSCARINICR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW Alternative splicing; Complete proteome; G-protein coupled receptor; KW Membrane; Receptor; Transducer; Transmembrane. FT CHAIN 1 627 Probable muscarinic acetylcholine FT receptor gar-2. FT /FTId=PRO_0000069049. FT TOPO_DOM 1 9 Extracellular (Potential). FT TRANSMEM 10 30 1 (Potential). FT TOPO_DOM 31 41 Cytoplasmic (Potential). FT TRANSMEM 42 62 2 (Potential). FT TOPO_DOM 63 81 Extracellular (Potential). FT TRANSMEM 82 102 3 (Potential). FT TOPO_DOM 103 122 Cytoplasmic (Potential). FT TRANSMEM 123 143 4 (Potential). FT TOPO_DOM 144 172 Extracellular (Potential). FT TRANSMEM 173 193 5 (Potential). FT TOPO_DOM 194 549 Cytoplasmic (Potential). FT TRANSMEM 550 570 6 (Potential). FT TOPO_DOM 571 586 Extracellular (Potential). FT TRANSMEM 587 609 7 (Potential). FT TOPO_DOM 610 627 Cytoplasmic (Potential). FT DISULFID 79 160 By similarity. FT VARSPLIC 520 532 Missing (in isoform b). FT /FTId=VSP_001862. SQ SEQUENCE 627 AA; 71483 MW; CB319E3BA8230AE5 CRC64; MAVASVLLAL FMLFLSIVTV IGNLAVLLSY YLDKNIRQPT NYFIFSLAIS DLLIGLEGIP VYTAFYLNNN EWIWGDVLCD LWLSIDYIVC LASIYTVLGI TVDRYYSVKK PATYRNWRTP GRVVLIIIFI WLVPSILFSV SIFGYGTFTG TGRILKETEC YVQFMTNPYL NMGMYISYYW TTLFVMLYLY WGIYRAAKKL ALKSDQKTKR LALLTEMRRP EVSVRTSDAG NSSSDSPNDT SNSSKCFRTA PPTTTVQTTQ TNVGTPPPVF RNHMTLHNNN MDFTKDNEIV RPPTPPDDNT YSNPNFSMIS EQLTNGFSRQ EPSSVIERES TAPCVSPEPS HASLENEFNE NHHAHFKPEL SLPFIDADSV SSMVGHDDLR RAMSIRISRS VSMQGTARAT PVIEIVENLE EALKICENLE ELREDENKNE EEKQKNGLEN GGMNHVIIAN DEQQPSTSKE SEQKEEMTPE NHDPNEVKVP LIAVSRVESV KSTAGGKVRR LITQMRSHSI RSKRKANKNK SVLSALNFFQ RKKEYKSRSE NRARKALRTI TFILGSFIIL WTPFYVLATI YGFCETCKAS PSFNTLYTIS YYLCYMNSPL NPFCYAMANQ QFKKTLTRIF KGDFRRV // ID OAR2_LYMST STANDARD; PRT; 578 AA. AC O01670; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 07-FEB-2006, entry version 28. DE Octopamine receptor 2 (OA2). OS Lymnaea stagnalis (Great pond snail). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Pulmonata; Basommatophora; OC Lymnaeoidea; Lymnaeidae; Lymnaea. OX NCBI_TaxID=6523; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RC TISSUE=CNS; RX MEDLINE=97197784; PubMed=9045634; DOI=10.1074/jbc.272.10.6201; RA Gerhardt C.C., Lodder H.C., Vincent M., Bakker R.A., Planta R.J., RA Vreugdenhil E., Kits K.S., van Heerikhuizen H.; RT "Cloning and expression of a complementary DNA encoding a molluscan RT octopamine receptor that couples to chloride channels in HEK293 RT cells."; RL J. Biol. Chem. 272:6201-6207(1997). CC -!- FUNCTION: Receptor for octopamine. Octopamine (OA) is a CC neurotransmitter, neurohormone, and neuromodulator in CC invertebrates. This receptor induces a long lasting opening of CC voltage- independent chloride channels, a process which seems to CC involve protein phosphorylation but does not require either cAPK CC or PKC. The rank order of potency for agonists is p-synephrine > CC p-octopamine > xylometazoline > B-HT920 > norepinephrine = CC clonidine > epinephrine > p-tyramine > phenylephrine = CC oxymetazoline = mehoxamine = dopamine > serotonin > histamine. For CC antagonists, the rank order is rauwolscine = mianserin > CC phentolamine > chlorpromazine > spiperone > yohimbine > propanolol CC > alprenolol > prazosine > pindolol. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U62770; AAB53033.1; -; mRNA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 578 Octopamine receptor 2. FT /FTId=PRO_0000069957. FT TOPO_DOM 1 84 Extracellular (Potential). FT TRANSMEM 85 107 1 (Potential). FT TOPO_DOM 108 117 Cytoplasmic (Potential). FT TRANSMEM 118 139 2 (Potential). FT TOPO_DOM 140 156 Extracellular (Potential). FT TRANSMEM 157 177 3 (Potential). FT TOPO_DOM 178 197 Cytoplasmic (Potential). FT TRANSMEM 198 220 4 (Potential). FT TOPO_DOM 221 251 Extracellular (Potential). FT TRANSMEM 252 272 5 (Potential). FT TOPO_DOM 273 495 Cytoplasmic (Potential). FT TRANSMEM 496 517 6 (Potential). FT TOPO_DOM 518 531 Extracellular (Potential). FT TRANSMEM 532 553 7 (Potential). FT TOPO_DOM 554 578 Cytoplasmic (Potential). FT CARBOHYD 13 13 N-linked (GlcNAc...) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 46 46 N-linked (GlcNAc...) (Potential). FT CARBOHYD 59 59 N-linked (GlcNAc...) (Potential). FT CARBOHYD 231 231 N-linked (GlcNAc...) (Potential). FT DISULFID 154 239 By similarity. SQ SEQUENCE 578 AA; 65131 MW; 05AF2E2447B3B09C CRC64; MMSFPIALFA DVNQSFRANL VVSSYHHAIT FPTVRGANFS TFFPRNFSVS ADVWLCGANF SQEWQLMQPV CSTKYDSITI FITVAVVLTL ITLWTILGNF FVLMALYRYG TLRTMSNCLI GNLAISDLLL AVTVLPISTV HDLLGYWVFG EFTCTLWLCM DVLYCTASIW GLCTVAFDRY LATVYPVWYH DQRSVRKAVG CIVFVWIFSI VISFAPFIGW QHMIPSFFSF NASIQRYQCI LFTSSSYVLY SSMGSFVIPA ILMAFMYVRI FVVLHNQSRG VKFKSGLKIS SSKYNGCPVI NEPSREGING LGRDVTNTTL LSDAVGSSAD LTSNGKDDPR VLATAPIELT EDVPPLNGHH HRTVHETPYV SGLHTKRSNS FALPTELEKK CKPLTNNILH MMDFDRRNSH NAVIQRSASE MVNLDVSKHE LLISNVCHRS KSATALTSET GDPLGSLAGP RRSLQCNVGG LVRNKHMTLS MKRRFELREQ RATKRMLLIM ACFCVCWMPF LFMYILRSVC DTCHMNQHFV AAIIWLGYVN SSLNPVLYTL FNDDFKVAFK RLIGARSPSA YRSPGPRR // ID OPSV_ORYLA STANDARD; PRT; 334 AA. AC P87368; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 07-FEB-2006, entry version 38. DE Putative violet-sensitive opsin (Violet cone photoreceptor pigment) DE (KFH-V). OS Oryzias latipes (Medaka fish) (Japanese ricefish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Atherinomorpha; OC Beloniformes; Adrianichthyidae; Oryziinae; Oryzias. OX NCBI_TaxID=8090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RA Hisatomi O., Satoh T., Tokunaga F.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: The three color pigments are found in the cone CC photoreceptor cells. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB001605; BAA19422.1; -; mRNA. DR HSSP; P02699; 1FDF. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001521; Opsin_blue. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00574; OPSINBLUE. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 334 Putative violet-sensitive opsin. FT /FTId=PRO_0000197771. FT TOPO_DOM 1 29 Extracellular (Potential). FT TRANSMEM 30 54 1 (Potential). FT TOPO_DOM 55 66 Cytoplasmic (Potential). FT TRANSMEM 67 88 2 (Potential). FT TOPO_DOM 89 106 Extracellular (Potential). FT TRANSMEM 107 126 3 (Potential). FT TOPO_DOM 127 145 Cytoplasmic (Potential). FT TRANSMEM 146 168 4 (Potential). FT TOPO_DOM 169 194 Extracellular (Potential). FT TRANSMEM 195 222 5 (Potential). FT TOPO_DOM 223 244 Cytoplasmic (Potential). FT TRANSMEM 245 272 6 (Potential). FT TOPO_DOM 273 279 Extracellular (Potential). FT TRANSMEM 280 301 7 (Potential). FT TOPO_DOM 302 334 Cytoplasmic (Potential). FT BINDING 288 288 Retinal chromophore (covalent). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT DISULFID 103 179 Potential. SQ SEQUENCE 334 AA; 37394 MW; 557422B64F75580F CRC64; MGKYFYLYEN ISKVGPYDGP QYYLAPTWAF YLQAAFMGFV FFVGTPLNFV VLLATAKYKK LRVPLNYILV NITFAGFIFV TFSVSQVFLA SVRGYYFFGQ TLCALEAAVG AVAGLVTSWS LAVLSFERYL VICKPFGAFK FGSNHALAAV IFTWFMGVVR CPPFFGWSRY IPEGLGCSCG PDWYTNCEEF SCASYSKFLL VTCFICPITI IIFSYSQLLG ALRAVAAQQA ESASTQKAEK EVSRMIIVMV ASFVTCYGPY ALTAQYYAYS QDENKDYRLV TIPAFFSKSS CVYNPLIYAF MNKQFNGCIM EMVFGKKMEE ASEVSSKTEV STDS // ID OP1S2_BRARE STANDARD; PRT; 354 AA. AC Q9W6A8; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 04-APR-2006, entry version 36. DE Opsin-1, short-wave-sensitive 2 (Blue-sensitive opsin) (Blue cone DE photoreceptor pigment) (Opsin SWS-2). GN Name=opn1sw2; Synonyms=bluops, opn1sw1, sws2; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Eye; RX MEDLINE=99277479; PubMed=10349976; RA Vihtelic T.S., Doro C.J., Hyde D.R.; RT "Cloning and characterization of six zebrafish photoreceptor opsin RT cDNAs and immunolocalization of their corresponding proteins."; RL Vis. Neurosci. 16:571-585(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=AB; TISSUE=Eye; RX MEDLINE=22505400; PubMed=12618404; RA Chinen A., Hamaoka T., Yamada Y., Kawamura S.; RT "Gene duplication and spectral diversification of cone visual pigments RT of zebrafish."; RL Genetics 163:663-675(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen; RG The Danio rerio sequencing project at the Sanger Institute; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=416 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Retinal long single cone outer segments. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF109372; AAD24755.1; -; mRNA. DR EMBL; AB087809; BAC24133.1; -; Genomic_DNA. DR EMBL; AL844847; CAE30415.1; -; Genomic_DNA. DR EMBL; BC059418; AAH59418.1; -; mRNA. DR EMBL; BC062277; AAH62277.1; -; mRNA. DR UniGene; Dr.8097; -. DR HSSP; P02699; 1EDV. DR Ensembl; ENSDARG00000017274; Danio rerio. DR ZFIN; ZDB-GENE-990604-40; opn1sw2. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0009882; F:blue light photoreceptor activity; NAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001521; Opsin_blue. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00574; OPSINBLUE. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 354 Opsin-1, short-wave-sensitive 2. FT /FTId=PRO_0000197755. FT TOPO_DOM 1 43 Extracellular (Potential). FT TRANSMEM 44 68 1 (Potential). FT TOPO_DOM 69 80 Cytoplasmic (Potential). FT TRANSMEM 81 106 2 (Potential). FT TOPO_DOM 107 120 Extracellular (Potential). FT TRANSMEM 121 140 3 (Potential). FT TOPO_DOM 141 159 Cytoplasmic (Potential). FT TRANSMEM 160 183 4 (Potential). FT TOPO_DOM 184 209 Extracellular (Potential). FT TRANSMEM 210 237 5 (Potential). FT TOPO_DOM 238 259 Cytoplasmic (Potential). FT TRANSMEM 260 283 6 (Potential). FT TOPO_DOM 284 291 Extracellular (Potential). FT TRANSMEM 292 316 7 (Potential). FT TOPO_DOM 317 354 Cytoplasmic (Potential). FT BINDING 303 303 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 207 207 N-linked (GlcNAc...) (Potential). FT DISULFID 117 194 Potential. SQ SEQUENCE 354 AA; 39484 MW; A434A07E864A30EC CRC64; MKQQQQTPEL FEDFHMPITL DVSNISAYSP FLVPQDHLGH SGVFMGMSAF MLFLFIAGTA INVLTIVCTI QYKKLRSHLN YILVNLAISN LWVSVFGSSV AFYAFYKKYF VFGPIGCKIE GFTSTIGGMV SLWSLAVVAL ERWLVICKPL GNFTFKTPHA IAGCILPWCM ALAAGLPPLL GWSRYIPEGL QCSCGPDWYT TNNKFNNESY VMFLFCFCFA VPFSTIVFCY GQLLITLKLA AKAQADSAST QKAEREVTKM VVVMVFGFLI CWGPYAIFAI WVVSNRGAPF DLRLATIPSC LCKASTVYNP VIYVLMNKQF RSCMMKMVFN KNIEEDEASS SSQVTQVSSV APEK // ID OPSB_CHICK STANDARD; PRT; 361 AA. AC P28682; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 04-APR-2006, entry version 47. DE Blue-sensitive opsin (Blue cone photoreceptor pigment). OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 304-318. RC TISSUE=Retina; RX MEDLINE=92335211; PubMed=1385866; RA Okano T., Kojima D., Fukada Y., Shichida Y., Yoshizawa T.; RT "Primary structures of chicken cone visual pigments: vertebrate RT rhodopsins have evolved out of cone visual pigments."; RL Proc. Natl. Acad. Sci. U.S.A. 89:5932-5936(1992). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=455 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: The color pigments are found in the cone CC photoreceptor cells. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M92037; AAA48633.1; -; mRNA. DR PIR; B46137; B46137. DR UniGene; Gga.874; -. DR HSSP; P02699; 1FDF. DR Ensembl; ENSGALG00000002848; Gallus gallus. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001521; Opsin_blue. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00574; OPSINBLUE. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; Direct protein sequencing; G-protein coupled receptor; KW Glycoprotein; Membrane; Phosphorylation; Photoreceptor protein; KW Receptor; Retinal protein; Sensory transduction; Transducer; KW Transmembrane; Vision. FT CHAIN 1 361 Blue-sensitive opsin. FT /FTId=PRO_0000197759. FT TOPO_DOM 1 43 Extracellular. FT TRANSMEM 44 68 1 (Potential). FT TOPO_DOM 69 80 Cytoplasmic. FT TRANSMEM 81 106 2 (Potential). FT TOPO_DOM 107 120 Extracellular. FT TRANSMEM 121 140 3 (Potential). FT TOPO_DOM 141 159 Cytoplasmic. FT TRANSMEM 160 183 4 (Potential). FT TOPO_DOM 184 209 Extracellular. FT TRANSMEM 210 237 5 (Potential). FT TOPO_DOM 238 259 Cytoplasmic. FT TRANSMEM 260 283 6 (Potential). FT TOPO_DOM 284 291 Extracellular. FT TRANSMEM 292 316 7 (Potential). FT TOPO_DOM 317 361 Cytoplasmic. FT BINDING 303 303 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Probable). FT DISULFID 117 194 Potential. SQ SEQUENCE 361 AA; 39657 MW; B9F262EA617D2888 CRC64; MHPPRPTTDL PEDFYIPMAL DAPNITALSP FLVPQTHLGS PGLFRAMAAF MFLLIALGVP INTLTIFCTA RFRKLRSHLN YILVNLALAN LLVILVGSTT ACYSFSQMYF ALGPTACKIE GFAATLGGMV SLWSLAVVAF ERFLVICKPL GNFTFRGSHA VLGCVATWVL GFVASAPPLF GWSRYIPEGL QCSCGPDWYT TDNKWHNESY VLFLFTFCFG VPLAIIVFSY GRLLITLRAV ARQQEQSATT QKADREVTKM VVVMVLGFLV CWAPYTAFAL WVVTHRGRSF EVGLASIPSV FSKSSTVYNP VIYVLMNKQF RSCMLKLLFC GRSPFGDDED VSGSSQATQV SSVSSSHVAP A // ID OPSG1_BRARE STANDARD; PRT; 349 AA. AC Q9W6A5; Q8AYM9; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 2. DT 04-APR-2006, entry version 38. DE Green-sensitive opsin-1 (Green cone photoreceptor pigment 1) (Opsin-1, DE medium-wave-sensitive 1) (Opsin RH2-1). GN Name=opn1mw1; Synonyms=grops1, rh21; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Eye; RX MEDLINE=99277479; PubMed=10349976; RA Vihtelic T.S., Doro C.J., Hyde D.R.; RT "Cloning and characterization of six zebrafish photoreceptor opsin RT cDNAs and immunolocalization of their corresponding proteins."; RL Vis. Neurosci. 16:571-585(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=AB; TISSUE=Eye; RX MEDLINE=22505400; PubMed=12618404; RA Chinen A., Hamaoka T., Yamada Y., Kawamura S.; RT "Gene duplication and spectral diversification of cone visual pigments RT of zebrafish."; RL Genetics 163:663-675(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen; RG The Danio rerio sequencing project at the Sanger Institute; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=467 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Retinal double cone accessory photoreceptor CC cell outer segments. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF109369; AAD24752.1; -; mRNA. DR EMBL; AB087805; BAC24129.1; -; Genomic_DNA. DR EMBL; AL732567; CAD87812.1; -; Genomic_DNA. DR EMBL; BC060896; AAH60896.1; -; mRNA. DR UniGene; Dr.8102; -. DR HSSP; P02699; 1F88. DR Ensembl; ENSDARG00000028424; Danio rerio. DR ZFIN; ZDB-GENE-990604-42; opn1mw1. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0009881; F:photoreceptor activity; NAS. DR GO; GO:0007602; P:phototransduction; IC. DR GO; GO:0007601; P:visual perception; NAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR000732; Rhodopsin. DR PANTHER; PTHR19264:SF16; Rhodopsin; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00579; RHODOPSIN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 349 Green-sensitive opsin-1. FT /FTId=PRO_0000197775. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 61 1 (Potential). FT TOPO_DOM 62 73 Cytoplasmic (Potential). FT TRANSMEM 74 99 2 (Potential). FT TOPO_DOM 100 113 Extracellular (Potential). FT TRANSMEM 114 133 3 (Potential). FT TOPO_DOM 134 152 Cytoplasmic (Potential). FT TRANSMEM 153 176 4 (Potential). FT TOPO_DOM 177 202 Extracellular (Potential). FT TRANSMEM 203 230 5 (Potential). FT TOPO_DOM 231 252 Cytoplasmic (Potential). FT TRANSMEM 253 276 6 (Potential). FT TOPO_DOM 277 284 Extracellular (Potential). FT TRANSMEM 285 309 7 (Potential). FT TOPO_DOM 310 349 Cytoplasmic (Potential). FT BINDING 296 296 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 2 2 N-linked (GlcNAc...) (Potential). FT CARBOHYD 15 15 N-linked (GlcNAc...) (Potential). FT CARBOHYD 200 200 N-linked (GlcNAc...) (Potential). FT DISULFID 110 187 Potential. FT CONFLICT 288 288 M -> I (in Ref. 1). SQ SEQUENCE 349 AA; 38844 MW; 0620B718F5C3F04B CRC64; MNGTEGSNFY IPMSNRTGLV RSPYDYTQYY LAEPWKFKAL AFYMFLLIIF GFPINVLTLV VTAQHKKLRQ PLNYILVNLA FAGTIMVIFG FTVSFYCSLV GYMALGPLGC VMEGFFATLG GQVALWSLVV LAIERYIVVC KPMGSFKFSA NHAMAGIAFT WFMACSCAVP PLFGWSRYLP EGMQTSCGPD YYTLNPEYNN ESYVMYMFSC HFCIPVTTIF FTYGSLVCTV KAAAAQQQES ESTQKAEREV TRMVILMVLG FLFAWVPYAS FAAWIFFNRG AAFSAQAMAV PAFFSKTSAV FNPIIYVLLN KQFRSCMLNT LFCGKSPLGD DESSSVSTSK TEVSSVSPA // ID OPSG1_ASTFA STANDARD; PRT; 355 AA. AC P22330; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 07-FEB-2006, entry version 49. DE Green-sensitive opsin-1 (Green cone photoreceptor pigment 1). GN Name=G103; Synonyms=GF; OS Astyanax fasciatus (Blind cave fish) (Astyanax mexicanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes; OC Characidae; Astyanax. OX NCBI_TaxID=7994; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Pineal gland; RX MEDLINE=90350274; PubMed=2385921; DOI=10.1016/0042-6989(90)90049-Q; RA Yokoyama R., Yokoyama S.; RT "Isolation, DNA sequence and evolution of a color visual pigment gene RT of the blind cave fish Astyanax fasciatus."; RL Vision Res. 30:807-816(1990). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: The color pigments are found in the cone CC photoreceptor cells. CC -!- MISCELLANEOUS: This fish possesses three genes for green opsin. CC Two (G103 and G101) that belong to the LWS/MWS group and one CC (RH11) that belongs to the RH2 group. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M60945; AAA48545.1; -; Genomic_DNA. DR EMBL; M60938; AAA48545.1; JOINED; Genomic_DNA. DR EMBL; M60939; AAA48545.1; JOINED; Genomic_DNA. DR EMBL; M60940; AAA48545.1; JOINED; Genomic_DNA. DR EMBL; M60943; AAA48545.1; JOINED; Genomic_DNA. DR EMBL; M60944; AAA48545.1; JOINED; Genomic_DNA. DR EMBL; U12025; AAA67216.1; -; Genomic_DNA. DR PIR; I50091; I50091. DR HSSP; P02699; 1FDF. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000378; Opsin_red/grn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00575; OPSINREDGRN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 355 Green-sensitive opsin-1. FT /FTId=PRO_0000197772. FT TOPO_DOM 1 49 Extracellular (Potential). FT TRANSMEM 50 74 1 (Potential). FT TOPO_DOM 75 86 Cytoplasmic (Potential). FT TRANSMEM 87 112 2 (Potential). FT TOPO_DOM 113 126 Extracellular (Potential). FT TRANSMEM 127 146 3 (Potential). FT TOPO_DOM 147 165 Cytoplasmic (Potential). FT TRANSMEM 166 189 4 (Potential). FT TOPO_DOM 190 215 Extracellular (Potential). FT TRANSMEM 216 243 5 (Potential). FT TOPO_DOM 244 265 Cytoplasmic (Potential). FT TRANSMEM 266 289 6 (Potential). FT TOPO_DOM 290 297 Extracellular (Potential). FT TRANSMEM 298 322 7 (Potential). FT TOPO_DOM 323 355 Cytoplasmic (Potential). FT BINDING 309 309 Retinal chromophore (covalent). FT CARBOHYD 31 31 N-linked (GlcNAc...) (Potential). FT DISULFID 123 200 Potential. SQ SEQUENCE 355 AA; 39696 MW; 9B7B6B8F361BCDA2 CRC64; MAAHADEPVF AARRYNEETT RESAFVYTNA NNTRDPFEGP NYHIAPRWVY NLASLWMIIV VIASIFTNSL VIVATAKFKK LRHPLNWILV NLAIADLGET VLASTISVFN QVFGYFVLGH PMCIFEGWTV SVCGITALWS LTIISWERWV VVCKPFGNVK FDGKWAAGGI IFAWTWAIIW CTPPIFGWSR YWPHGLKTSC GPDVFSGSED PGVASYMVTL LLTCCILPLS VIIICYIFVW NAIHQVAQQQ KDSESTQKAE KEVSRMVVVM ILAFILCWGP YASFATFSAL NPGYAWHPLA AALPAYFAKS ATIYNPIIYV FMNRQFRSCI MQLFGKKVED ASEVSGSTTE VSTAS // ID OPSO_SALSA STANDARD; PRT; 323 AA. AC O13018; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 07-FEB-2006, entry version 39. DE Vertebrate ancient opsin. OS Salmo salar (Atlantic salmon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Salmo. OX NCBI_TaxID=8030; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eye; RX MEDLINE=97282593; PubMed=9136902; DOI=10.1016/S0014-5793(97)00287-1; RA Soni B.G., Foster R.G.; RT "A novel and ancient vertebrate opsin."; RL FEBS Lett. 406:279-283(1997). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF001499; AAC60124.1; -; mRNA. DR HSSP; P02699; 1FDF. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR002206; Opsin_pineal. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00666; PINOPSIN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 2. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane. FT CHAIN 1 323 Vertebrate ancient opsin. FT /FTId=PRO_0000197811. FT TOPO_DOM 1 38 Extracellular. FT TRANSMEM 39 63 1 (Potential). FT TOPO_DOM 64 75 Cytoplasmic. FT TRANSMEM 76 100 2 (Potential). FT TOPO_DOM 101 115 Extracellular. FT TRANSMEM 116 135 3 (Potential). FT TOPO_DOM 136 154 Cytoplasmic. FT TRANSMEM 155 178 4 (Potential). FT TOPO_DOM 179 202 Extracellular. FT TRANSMEM 203 230 5 (Potential). FT TOPO_DOM 231 250 Cytoplasmic. FT TRANSMEM 251 274 6 (Potential). FT TOPO_DOM 275 282 Extracellular. FT TRANSMEM 283 307 7 (Potential). FT TOPO_DOM 308 323 Cytoplasmic. FT BINDING 294 294 Retinal chromophore (covalent). FT CARBOHYD 200 200 N-linked (GlcNAc...) (Potential). FT DISULFID 112 189 By similarity. SQ SEQUENCE 323 AA; 36668 MW; D1FD813EC599D0C3 CRC64; MDTLRIAVNG VSYNEASEIY KPHADPFTGP ITNLAPWNFA VLATLMFVIT SLSLFENFTV MLATYKFKQL RQPLNYIIVN LSLADFLVSL TGGTISFLTN ARGYFFLGNW ACVLEGFAVT YFGIVAMWSL AVLSFERYFV ICRPLGNVRL RGKHAALGLL FVWTFSFIWT IPPVFGWCSY TVSKIGTTCE PNWYSNNIWN HTYIITFFVT CFIMPLGMII YCYGKLLQKL RKVSHDRLGN AKKPERQVSR MVVVMIVAYL VGWTPYAAFS IIVTACPTIY LDPRLAAAPA FFSKTAAVYN PVIYVFMNKQ VSTQLNWGFW SRA // ID OPSP_ICTPU STANDARD; PRT; 346 AA. AC O42266; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 07-FEB-2006, entry version 36. DE Parapinopsin. OS Ictalurus punctatus (Channel catfish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes; OC Ictaluridae; Ictalurus. OX NCBI_TaxID=7998; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97477428; PubMed=9334384; RA Blackshaw S., Snyder S.H.; RT "Parapinopsin, a novel catfish opsin localized to the parapineal RT organ, defines a new gene family."; RL J. Neurosci. 17:8083-8092(1997). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Parapineal organ. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF028014; AAB84050.1; -; mRNA. DR HSSP; P02699; 1FDF. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Lipoprotein; KW Membrane; Palmitate; Phosphorylation; Photoreceptor protein; Receptor; KW Retinal protein; Sensory transduction; Transducer; Transmembrane. FT CHAIN 1 346 Parapinopsin. FT /FTId=PRO_0000197809. FT TOPO_DOM 1 29 Extracellular (Potential). FT TRANSMEM 30 54 1 (Potential). FT TOPO_DOM 55 66 Cytoplasmic (Potential). FT TRANSMEM 67 91 2 (Potential). FT TOPO_DOM 92 106 Extracellular (Potential). FT TRANSMEM 107 126 3 (Potential). FT TOPO_DOM 127 145 Cytoplasmic (Potential). FT TRANSMEM 146 169 4 (Potential). FT TOPO_DOM 170 193 Extracellular (Potential). FT TRANSMEM 194 221 5 (Potential). FT TOPO_DOM 222 244 Cytoplasmic (Potential). FT TRANSMEM 245 268 6 (Potential). FT TOPO_DOM 269 276 Extracellular (Potential). FT TRANSMEM 277 301 7 (Potential). FT TOPO_DOM 302 346 Cytoplasmic (Potential). FT BINDING 288 288 Retinal chromophore (covalent) (By FT similarity). FT LIPID 315 315 S-palmitoyl cysteine (By similarity). FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 191 191 N-linked (GlcNAc...) (Potential). FT DISULFID 103 180 By similarity. SQ SEQUENCE 346 AA; 38203 MW; A70871684F8FC7FD CRC64; MASIILINFS ETDTLHLGSV NDHIMPRIGY TILSIIMALS STFGIILNMV VIIVTVRYKQ LRQPLNYALV NLAVADLGCP VFGGLLTAVT NAMGYFSLGR VGCVLEGFAV AFFGIAGLCS VAVIAVDRYM VVCRPLGAVM FQTKHALAGV VFSWVWSFIW NTPPLFGWGS YQLEGVMTSC APNWYRRDPV NVSYILCYFM LCFALPFATI IFSYMHLLHT LWQVAKLQVA DSGSTAKVEV QVARMVVIMV MAFLLTWLPY AAFALTVIID SNIYINPVIG TIPAYLAKSS TVFNPIIYIF MNRQFRDYAL PCLLCGKNPW AAKEGRDSDT NTLTTTVSKN TSVSPL // ID OPS2_DROME STANDARD; PRT; 381 AA. AC P08099; Q9VE29; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 02-MAY-2006, entry version 68. DE Opsin Rh2 (Ocellar opsin). GN Name=Rh2; ORFNames=CG16740; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86133563; PubMed=2936466; DOI=10.1016/0092-8674(86)90836-6; RA Cowman A.F., Zuker C.S., Rubin G.M.; RT "An opsin gene expressed in only one photoreceptor cell type of the RT Drosophila eye."; RL Cell 44:705-710(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP LOCALIZATION OF OPSIN RH2, AND BIOPHYSICOCHEMICAL PROPERTIES. RX MEDLINE=88261498; PubMed=2455230; DOI=10.1038/333737a0; RA Feiler R., Harris W.A., Kirschfeld K., Wehrhahn C., Zuker C.S.; RT "Targeted misexpression of a Drosophila opsin gene leads to altered RT visual function."; RL Nature 333:737-741(1988). RN [5] RP LOCALIZATION OF OPSIN RH2. RX MEDLINE=88261503; PubMed=2968518; DOI=10.1038/333779a0; RA Pollock J.A., Benzer S.; RT "Transcript localization of four opsin genes in the three visual RT organs of Drosophila; RH2 is ocellus specific."; RL Nature 333:779-782(1988). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=420 nm; CC -!- INTERACTION: CC Q9VL06:CG5604; NbExp=1; IntAct=EBI-162315, EBI-173559; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Predominant opsin expressed in the dorsal CC ocelli. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M12896; AAA28734.1; -; Genomic_DNA. DR EMBL; AE003724; AAF55601.1; -; Genomic_DNA. DR PIR; A24058; OOFF2. DR UniGene; Dm.2404; -. DR HSSP; P02699; 1EDV. DR IntAct; P08099; -. DR Ensembl; CG16740; Drosophila melanogaster. DR FlyBase; FBgn0003248; Rh2. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-012289-MONOMER; -. DR GO; GO:0008020; F:G-protein coupled photoreceptor activity; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0007602; P:phototransduction; IGI. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001735; Opsin_RH1/RH2. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00576; OPSINRH1RH2. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; Complete proteome; G-protein coupled receptor; KW Glycoprotein; Membrane; Phosphorylation; Photoreceptor protein; KW Receptor; Retinal protein; Sensory transduction; Transducer; KW Transmembrane; Vision. FT CHAIN 1 381 Opsin Rh2. FT /FTId=PRO_0000197625. FT TOPO_DOM 1 56 Extracellular. FT TRANSMEM 57 81 1 (Potential). FT TOPO_DOM 82 93 Cytoplasmic. FT TRANSMEM 94 119 2 (Potential). FT TOPO_DOM 120 133 Extracellular. FT TRANSMEM 134 153 3 (Potential). FT TOPO_DOM 154 172 Cytoplasmic. FT TRANSMEM 173 196 4 (Potential). FT TOPO_DOM 197 220 Extracellular. FT TRANSMEM 221 248 5 (Potential). FT TOPO_DOM 249 283 Cytoplasmic. FT TRANSMEM 284 307 6 (Potential). FT TOPO_DOM 308 314 Extracellular. FT TRANSMEM 315 339 7 (Potential). FT TOPO_DOM 340 381 Cytoplasmic. FT BINDING 326 326 Retinal chromophore (covalent). FT CARBOHYD 27 27 N-linked (GlcNAc...) (Probable). FT DISULFID 130 207 Potential. SQ SEQUENCE 381 AA; 42722 MW; 628322D228396F9D CRC64; MERSHLPETP FDLAHSGPRF QAQSSGNGSV LDNVLPDMAH LVNPYWSRFA PMDPMMSKIL GLFTLAIMII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY ETWVLGPLWC DIYAGCGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKILFI WMMAVFWTVM PLIGWSAYVP EGNLTACSID YMTRMWNPRS YLITYSLFVY YTPLFLICYS YWFIIAAVAA HEKAMREQAK KMNVKSLRSS EDCDKSAEGK LAKVALTTIS LWFMAWTPYL VICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRIVLKEK CPMCVFGNTD EPKPDAPASD TETTSEADSK A // ID OPS6_DROME STANDARD; PRT; 369 AA. AC O01668; Q8SXF4; Q9VF58; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 04-APR-2006, entry version 49. DE Opsin Rh6 (Rhodopsin Rh6, long-wavelength). GN Name=Rh6; ORFNames=CG5192; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM B). RC STRAIN=Oregon-R; TISSUE=Retina; RX MEDLINE=97263460; PubMed=9109375; DOI=10.1016/S0014-5793(97)00210-X; RA Huber A., Schulz S., Bentrop J., Groell C., Wolfrum U., Paulsen R.; RT "Molecular cloning of Drosophila Rh6 rhodopsin: the visual pigment of RT a subset of R8 photoreceptor cells."; RL FEBS Lett. 406:6-10(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=O01668-1; Sequence=Displayed; CC Name=A; CC IsoId=O01668-2; Sequence=VSP_009271; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Each Drosophila eye is composed of 800 facets CC or ommatidia. Each ommatidium contains 8 photoreceptor cells (R1- CC R8), the R1 to R6 cells are outer cells, while R7 and R8 are inner CC cells. Rh6 is expressed in a subset of R8 cells, most likely CC expressed in the subset of R8 cells paired with Rh4-expressing R7 CC cells (R7y). CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z86118; CAB06821.1; -; mRNA. DR EMBL; AE003709; AAN13666.2; -; Genomic_DNA. DR EMBL; AY089666; AAL90404.1; -; mRNA. DR UniGene; Dm.1656; -. DR HSSP; P02699; 1EDV. DR Ensembl; CG4550; Drosophila melanogaster. DR FlyBase; FBgn0019940; Rh6. DR GO; GO:0016028; C:rhabdomere; IDA. DR GO; GO:0008020; F:G-protein coupled photoreceptor activity; IGI. DR GO; GO:0007602; P:phototransduction; IGI. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001735; Opsin_RH1/RH2. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00576; OPSINRH1RH2. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Alternative splicing; Chromophore; Complete proteome; KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphorylation; KW Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 369 Opsin Rh6. FT /FTId=PRO_0000197634. FT TOPO_DOM 1 46 Extracellular. FT TRANSMEM 47 71 1 (Potential). FT TOPO_DOM 72 83 Cytoplasmic. FT TRANSMEM 84 109 2 (Potential). FT TOPO_DOM 110 123 Extracellular. FT TRANSMEM 124 143 3 (Potential). FT TOPO_DOM 144 162 Cytoplasmic. FT TRANSMEM 163 186 4 (Potential). FT TOPO_DOM 187 210 Extracellular. FT TRANSMEM 211 238 5 (Potential). FT TOPO_DOM 239 274 Cytoplasmic. FT TRANSMEM 275 298 6 (Potential). FT TOPO_DOM 299 305 Extracellular. FT TRANSMEM 306 330 7 (Potential). FT TOPO_DOM 331 369 Cytoplasmic. FT BINDING 317 317 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 193 193 N-linked (GlcNAc...) (Potential). FT CARBOHYD 208 208 N-linked (GlcNAc...) (Potential). FT DISULFID 120 197 Potential. FT VARSPLIC 230 369 Missing (in isoform A). FT /FTId=VSP_009271. SQ SEQUENCE 369 AA; 41691 MW; 5670A7435AD5F244 CRC64; MASLHPPSFA YMRDGRNLSL AESVPAEIMH MVDPYWYQWP PLEPMWFGII GFVIAILGTM SLAGNFIVMY IFTSSKGLRT PSNMFVVNLA FSDFMMMFTM FPPVVLNGFY GTWIMGPFLC ELYGMFGSLF GCVSIWSMTL IAYDRYCVIV KGMARKPLTA TAAVLRLMVV WTICGAWALM PLFGWNRYVP EGNMTACGTD YFAKDWWNRS YIIVYSLWVY LTPLLTIIFS YWHIMKAVAA HEKAMREQAK KMNVASLRNS EADKSKAIEI KLAKVALTTI SLWFFAWTPY TIINYAGIFE SMHLSPLSTI CGSVFAKANA VCNPIVYGLS HPKYKQVLRE KMPCLACGKD DLTSDSRTQA TAEISESQA // ID OPSL_LIMPO STANDARD; PRT; 376 AA. AC P35360; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 07-FEB-2006, entry version 42. DE Lateral eye opsin. OS Limulus polyphemus (Atlantic horseshoe crab). OC Eukaryota; Metazoa; Arthropoda; Chelicerata; Merostomata; Xiphosura; OC Limulidae; Limulus. OX NCBI_TaxID=6850; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lateral eye; RX MEDLINE=93317641; PubMed=8327495; RA Smith W.C., Price D.A., Greenberg R.M., Battelle B.-A.; RT "Opsins from the lateral eyes and ocelli of the horseshoe crab, RT Limulus polyphemus."; RL Proc. Natl. Acad. Sci. U.S.A. 90:6150-6154(1993). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=520 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Lateral eye. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L03791; AAA28273.1; -; mRNA. DR EMBL; L03781; AAA02498.1; -; mRNA. DR PIR; B48197; B48197. DR HSSP; P02699; 1EDV. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001391; Opsin_lateye. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00578; OPSINLTRLEYE. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 376 Lateral eye opsin. FT /FTId=PRO_0000197751. FT TOPO_DOM 1 46 Extracellular. FT TRANSMEM 47 71 1 (Potential). FT TOPO_DOM 72 83 Cytoplasmic. FT TRANSMEM 84 108 2 (Potential). FT TOPO_DOM 109 123 Extracellular. FT TRANSMEM 124 143 3 (Potential). FT TOPO_DOM 144 162 Cytoplasmic. FT TRANSMEM 163 186 4 (Potential). FT TOPO_DOM 187 210 Extracellular. FT TRANSMEM 211 238 5 (Potential). FT TOPO_DOM 239 274 Cytoplasmic. FT TRANSMEM 275 298 6 (Potential). FT TOPO_DOM 299 306 Extracellular. FT TRANSMEM 307 331 7 (Potential). FT TOPO_DOM 332 376 Cytoplasmic. FT BINDING 318 318 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 193 193 N-linked (GlcNAc...) (Potential). FT DISULFID 120 197 By similarity. SQ SEQUENCE 376 AA; 42140 MW; CCE401766AB06F26 CRC64; MANQLSYSSL GWPYQPNASV VDTMPKEMLY MIHEHWYAFP PMNPLWYSIL GVAMIILGII CVLGNGMVIY LMMTTKSLRT PTNLLVVNLA FSDFCMMAFM MPTMTSNCFA ETWILGPFMC EVYGMAGSLF GCASIWSMVM ITLDRYNVIV RGMAAAPLTH KKATLLLLFV WIWSGGWTIL PFFGWSRYVP EGNLTSCTVD YLTKDWSSAS YVVIYGLAVY FLPLITMIYC YFFIVHAVAE HEKQLREQAK KMNVASLRAN ADQQKQSAEC RLAKVAMMTV GLWFMAWTPY LIISWAGVFS SGTRLTPLAT IWGSVFAKAN SCYNPIVYGI SHPRYKAALY QRFPSLACGS GESGSDVKSE ASATTTMEEK PKIPEA // ID OPSC2_HEMSA STANDARD; PRT; 377 AA. AC Q25158; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 07-FEB-2006, entry version 39. DE Compound eye opsin BCRH2. OS Hemigrapsus sanguineus (Crab). OC Eukaryota; Metazoa; Arthropoda; Crustacea; Malacostraca; OC Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura; OC Eubrachyura; Grapsoidea; Varunidae; Hemigrapsus. OX NCBI_TaxID=40176; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eye; RX PubMed=9318091; RA Sakamoto K., Hisatomi O., Tokunaga F., Eguchi E.; RT "Two opsins from the compound eye of the crab Hemigrapsus RT sanguineus."; RL J. Exp. Biol. 199:441-450(1996). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. This opsin produces visual pigments with CC maximal absorption in the blue-green region of the spectrum. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in all of the seven retinular cells CC (R1-R7) forming the main rhabdom in each ommatidium. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D50584; BAA09133.1; -; mRNA. DR HSSP; P02699; 1L9H. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000856; Opsin_RH3/RH4. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00577; OPSINRH3RH4. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 377 Compound eye opsin BCRH2. FT /FTId=PRO_0000197750. FT TOPO_DOM 1 53 Extracellular. FT TRANSMEM 54 78 1 (Potential). FT TOPO_DOM 79 90 Cytoplasmic. FT TRANSMEM 91 115 2 (Potential). FT TOPO_DOM 116 131 Extracellular. FT TRANSMEM 132 151 3 (Potential). FT TOPO_DOM 152 170 Cytoplasmic. FT TRANSMEM 171 194 4 (Potential). FT TOPO_DOM 195 218 Extracellular. FT TRANSMEM 219 246 5 (Potential). FT TOPO_DOM 247 281 Cytoplasmic. FT TRANSMEM 282 305 6 (Potential). FT TOPO_DOM 306 313 Extracellular. FT TRANSMEM 314 338 7 (Potential). FT TOPO_DOM 339 377 Cytoplasmic. FT BINDING 325 325 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT DISULFID 128 205 By similarity. SQ SEQUENCE 377 AA; 42114 MW; FD6CC2E0E199A256 CRC64; MTNATGPQMA YYGAASMDFG YPEGVSIVDF VRPEIKPYVH QHWYNYPPVN PMWHYLLGVI YLFLGTVSIF GNGLVIYLFN KSAALRTPAN ILVVNLALSD LIMLTTNVPF FTYNCFSGGV WMFSPQYCEI YACLGAITGV CSIWLLCMIS FDRYNIICNG FNGPKLTTGK AVVFALISWV IAIGCALPPF FGWGNYILEG ILDSCSYDYL TQDFNTFSYN IFIFVFDYFL PAAIIVFSYV FIVKAIFAHE AAMRAQAKKM NVSTLRSNEA DAQRAEIRIA KTALVNVSLW FICWTPYALI SLKGVMGDTS GITPLVSTLP ALLAKSCSCY NPFVYAISHP KYRLAITQHL PWFCVHETET KSNDDSQSNS TVAQDKA // ID OPSB_APIME STANDARD; PRT; 377 AA. AC P90680; O61302; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 04-APR-2006, entry version 43. DE Opsin, blue-sensitive (AMBLOP). GN Name=BLOP; OS Apis mellifera (Honeybee). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; OC Apidae; Apis. OX NCBI_TaxID=7460; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Head; RX MEDLINE=97210781; PubMed=9057845; RA Bellingham J., Wilkie S.E., Morris A.G., Bowmaker J.K., Hunt D.M.; RT "Characterisation of the ultraviolet-sensitive opsin gene in the honey RT bee, Apis mellifera."; RL Eur. J. Biochem. 243:775-781(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Head; RX MEDLINE=98171548; PubMed=9502802; RA Townson S.M., Chang B.S., Salcedo E., Chadwell L.V., Pierce N.E., RA Britt S.G.; RT "Honeybee blue- and ultraviolet-sensitive opsins: cloning, RT heterologous expression in Drosophila, and physiological RT characterization."; RL J. Neurosci. 18:2412-2422(1998). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to 11-cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=439 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC -!- CAUTION: Was originally (Ref.1) thought to be the ultraviolet CC sensitive opsin. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U70841; AAC47455.1; -; mRNA. DR EMBL; AF004168; AAC13417.1; -; mRNA. DR UniGene; Ame.1207; -. DR HSSP; P02699; 1F88. DR Ensembl; ENSAPMG00000014724; Apis mellifera. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000856; Opsin_RH3/RH4. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00577; OPSINRH3RH4. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 377 Opsin, blue-sensitive. FT /FTId=PRO_0000197638. FT TOPO_DOM 1 56 Extracellular. FT TRANSMEM 57 81 1 (Potential). FT TOPO_DOM 82 93 Cytoplasmic. FT TRANSMEM 94 119 2 (Potential). FT TOPO_DOM 120 132 Extracellular. FT TRANSMEM 133 152 3 (Potential). FT TOPO_DOM 153 170 Cytoplasmic. FT TRANSMEM 171 195 4 (Potential). FT TOPO_DOM 196 219 Extracellular. FT TRANSMEM 220 247 5 (Potential). FT TOPO_DOM 248 282 Cytoplasmic. FT TRANSMEM 283 306 6 (Potential). FT TOPO_DOM 307 314 Extracellular. FT TRANSMEM 315 339 7 (Potential). FT TOPO_DOM 340 377 Cytoplasmic. FT BINDING 326 326 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT DISULFID 129 206 Potential. FT CONFLICT 43 43 R -> H (in Ref. 2). SQ SEQUENCE 377 AA; 43016 MW; 7C066A675605E513 CRC64; MLLHNKTLAG KALAFIAEEG YVPSMREKFL GWNVPPEYSD LVRPHWRAFP APGKHFHIGL AIIYSMLLIM SLVGNCCVIW IFSTSKSLRT PSNMFIVSLA IFDIIMAFEM PMLVISSFME RMIGWEIGCD VYSVFGSISG MGQAMTNAAI AFDRYRTISC PIDGRLNSKQ AAVIIAFTWF WVTPFTVLPL LKVWGRYTTE GFLTTCSFDF LTDDEDTKVF VTCIFIWAYV IPLIFIILFY SRLLSSIRNH EKMLREQAKK MNVKSLVSNQ DKERSAEVRI AKVAFTIFFL FLLAWTPYAT VALIGVYGNR ELLTPVSTML PAVFAKTVSC IDPWIYAINH PRYRQELQKR CKWMGIHEPE TTSDATSAQT EKIKTDE // ID OPS3_DROME STANDARD; PRT; 383 AA. AC P04950; Q9TX53; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 04-APR-2006, entry version 74. DE Opsin Rh3 (Inner R7 photoreceptor cells opsin). GN Name=Rh3; Synonyms=RH92CD; ORFNames=CG10888; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Canton-S; RX MEDLINE=87218500; PubMed=2953598; RA Fryxell K.J., Meyerowitz E.M.; RT "An opsin gene that is expressed only in the R7 photoreceptor cell of RT Drosophila."; RL EMBO J. 6:443-451(1987). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=87197540; PubMed=2437266; RA Zuker C.S., Montell C., Jones K., Laverty T., Rubin G.M.; RT "A rhodopsin gene expressed in photoreceptor cell R7 of the Drosophila RT eye: homologies with other signal-transducing molecules."; RL J. Neurosci. 7:1550-1557(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=20196012; PubMed=10731138; DOI=10.1126/science.287.5461.2222; RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., RA Stapleton M., Harvey D.A.; RT "A Drosophila complementary DNA resource."; RL Science 287:2222-2224(2000). RN [6] RP NUCLEOTIDE SEQUENCE OF 34-355. RX MEDLINE=94275868; PubMed=8006992; DOI=10.1007/BF00176087; RA Carulli J.P., Chen D.M., Stark W.S., Hartl D.L.; RT "Phylogeny and physiology of Drosophila opsins."; RL J. Mol. Evol. 38:250-262(1994). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region. CC -!- MISCELLANEOUS: Each Drosophila eye is composed of 800 facets or CC ommatidia. Each ommatidium contains 8 photoreceptor cells (R1-R8), CC the R1 to R6 cells are outer cells, while R7 and R8 are inner CC cells. CC -!- MISCELLANEOUS: Opsin Rh3 is sensitive to UV light. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00043; CAA68259.1; -; Genomic_DNA. DR EMBL; M17718; AAA28854.1; -; Genomic_DNA. DR EMBL; AE003729; AAG22157.1; -; Genomic_DNA. DR EMBL; AF184224; AAD55735.1; -; mRNA. DR PIR; A26768; A26768. DR UniGene; Dm.2396; -. DR HSSP; P02699; 1F88. DR Ensembl; CG10888; Drosophila melanogaster. DR FlyBase; FBgn0003249; Rh3. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-012450-MONOMER; -. DR GO; GO:0008020; F:G-protein coupled photoreceptor activity; IDA. DR GO; GO:0016039; P:absorption of UV light; IMP. DR GO; GO:0007604; P:phototransduction, UV; IDA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000856; Opsin_RH3/RH4. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00577; OPSINRH3RH4. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; Complete proteome; G-protein coupled receptor; KW Glycoprotein; Membrane; Phosphorylation; Photoreceptor protein; KW Receptor; Retinal protein; Sensory transduction; Transducer; KW Transmembrane; Vision. FT CHAIN 1 383 Opsin Rh3. FT /FTId=PRO_0000197627. FT TOPO_DOM 1 57 Extracellular. FT TRANSMEM 58 82 1 (Potential). FT TOPO_DOM 83 94 Cytoplasmic. FT TRANSMEM 95 119 2 (Potential). FT TOPO_DOM 120 133 Extracellular. FT TRANSMEM 134 153 3 (Potential). FT TOPO_DOM 154 171 Cytoplasmic. FT TRANSMEM 172 196 4 (Potential). FT TOPO_DOM 197 220 Extracellular. FT TRANSMEM 221 248 5 (Potential). FT TOPO_DOM 249 284 Cytoplasmic. FT TRANSMEM 285 308 6 (Potential). FT TOPO_DOM 309 316 Extracellular. FT TRANSMEM 317 341 7 (Potential). FT TOPO_DOM 342 383 Cytoplasmic. FT BINDING 328 328 Retinal chromophore (covalent). FT CARBOHYD 13 13 N-linked (GlcNAc...) (Probable). FT DISULFID 130 207 Potential. SQ SEQUENCE 383 AA; 42940 MW; BF9D009A25CA6343 CRC64; MESGNVSSSL FGNVSTALRP EARLSAETRL LGWNVPPEEL RHIPEHWLTY PEPPESMNYL LGTLYIFFTL MSMLGNGLVI WVFSAAKSLR TPSNILVINL AFCDFMMMVK TPIFIYNSFH QGYALGHLGC QIFGIIGSYT GIAAGATNAF IAYDRFNVIT RPMEGKMTHG KAIAMIIFIY MYATPWVVAC YTETWGRFVP EGYLTSCTFD YLTDNFDTRL FVACIFFFSF VCPTTMITYY YSQIVGHVFS HEKALRDQAK KMNVESLRSN VDKNKETAEI RIAKAAITIC FLFFCSWTPY GVMSLIGAFG DKTLLTPGAT MIPACACKMV ACIDPFVYAI SHPRYRMELQ KRCPWLALNE KAPESSAVAS TSTTQEPQQT TAA // ID OPSUV_APIME STANDARD; PRT; 371 AA. AC O61303; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 04-APR-2006, entry version 41. DE Opsin, ultraviolet-sensitive (AMUVOP) (BUVOPS). GN Name=UVOP; OS Apis mellifera (Honeybee). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; OC Apidae; Apis. OX NCBI_TaxID=7460; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Head; RX MEDLINE=98171548; PubMed=9502802; RA Townson S.M., Chang B.S., Salcedo E., Chadwell L.V., Pierce N.E., RA Britt S.G.; RT "Honeybee blue- and ultraviolet-sensitive opsins: cloning, RT heterologous expression in Drosophila, and physiological RT characterization."; RL J. Neurosci. 18:2412-2422(1998). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to 11-cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=353 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF004169; AAC13418.1; -; mRNA. DR UniGene; Ame.1210; -. DR HSSP; P02699; 1F88. DR Ensembl; ENSAPMG00000007831; Apis mellifera. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000856; Opsin_RH3/RH4. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00577; OPSINRH3RH4. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 371 Opsin, ultraviolet-sensitive. FT /FTId=PRO_0000197639. FT TOPO_DOM 1 52 Extracellular (Potential). FT TRANSMEM 53 73 Potential. FT TOPO_DOM 74 84 Cytoplasmic (Potential). FT TRANSMEM 85 105 Potential. FT TOPO_DOM 106 121 Extracellular (Potential). FT TRANSMEM 122 142 Potential. FT TOPO_DOM 143 161 Cytoplasmic (Potential). FT TRANSMEM 162 182 Potential. FT TOPO_DOM 183 209 Extracellular (Potential). FT TRANSMEM 210 230 Potential. FT TOPO_DOM 231 278 Cytoplasmic (Potential). FT TRANSMEM 279 299 Potential. FT TOPO_DOM 300 302 Extracellular (Potential). FT TRANSMEM 303 323 Potential. FT TOPO_DOM 324 371 Cytoplasmic (Potential). FT BINDING 318 318 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT DISULFID 120 197 Potential. SQ SEQUENCE 371 AA; 41458 MW; 9B2BB1FF92762956 CRC64; MSNDSIHWEA RYLPAGPPRL LGWNVPAEEL IHIPEHWLVY PEPNPSLHYL LALLYILFTF LALLGNGLVI WIFCAAKSLR TPSNMFVVNL AICDFFMMIK TPIFIYNSFN TGFALGNLGC QIFAVIGSLT GIGAAITNAA IAYDRYSTIA RPLDGKLSRG QVILFIVLIW TYTIPWALMP VMGVWGRFVP EGFLTSCSFD YLTDTNEIRI FVATIFTFSY CIPMILIIYY YSQIVSHVVN HEKALREQAK KMNVDSLRSN ANTSSQSAEI RIAKAAITIC FLYVLSWTPY GVMSMIGAFG NKALLTPGVT MIPACTCKAV ACLDPYVYAI SHPKYRLELQ KRLPWLELQE KPISDSTSTT TETVNTPPAS S // ID OPSD1_PATYE STANDARD; PRT; 499 AA. AC O15973; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 07-FEB-2006, entry version 37. DE Rhodopsin, GQ-coupled (GQ-rhodopsin). GN Name=SCOP1; OS Patinopecten yessoensis (Ezo giant scallop) (Yesso scallop). OC Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Pectinoida; OC Pectinoidea; Pectinidae; Mizuhopecten. OX NCBI_TaxID=6573; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eye; RX MEDLINE=97435252; PubMed=9287291; DOI=10.1074/jbc.272.37.22979; RA Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A., RA Shichida Y.; RT "A novel Go-mediated phototransduction cascade in scallop visual RT cells."; RL J. Biol. Chem. 272:22979-22989(1997). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Retina. Expressed in the depolarizing cell CC layer of the photoreceptor cells distant from the lens. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB006454; BAA22217.1; -; mRNA. DR HSSP; P02699; 1F88. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000856; Opsin_RH3/RH4. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00577; OPSINRH3RH4. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Lipoprotein; KW Membrane; Palmitate; Phosphorylation; Photoreceptor protein; Receptor; KW Retinal protein; Sensory transduction; Transducer; Transmembrane; KW Vision. FT CHAIN 1 499 Rhodopsin, GQ-coupled. FT /FTId=PRO_0000197735. FT TOPO_DOM 1 50 Extracellular. FT TRANSMEM 51 75 1 (Potential). FT TOPO_DOM 76 87 Cytoplasmic. FT TRANSMEM 88 114 2 (Potential). FT TOPO_DOM 115 128 Extracellular. FT TRANSMEM 129 148 3 (Potential). FT TOPO_DOM 149 168 Cytoplasmic. FT TRANSMEM 169 192 4 (Potential). FT TOPO_DOM 193 216 Extracellular. FT TRANSMEM 217 244 5 (Potential). FT TOPO_DOM 245 278 Cytoplasmic. FT TRANSMEM 279 302 6 (Potential). FT TOPO_DOM 303 310 Extracellular. FT TRANSMEM 311 335 7 (Potential). FT TOPO_DOM 336 499 Cytoplasmic. FT BINDING 322 322 Retinal chromophore (covalent). FT LIPID 353 353 S-palmitoyl cysteine (By similarity). FT LIPID 354 354 S-palmitoyl cysteine (By similarity). FT CARBOHYD 4 4 N-linked (GlcNAc...) (Potential). FT CARBOHYD 15 15 N-linked (GlcNAc...) (Potential). FT CARBOHYD 19 19 N-linked (GlcNAc...) (Potential). FT DISULFID 125 203 By similarity. SQ SEQUENCE 499 AA; 55946 MW; 853D1B7E35E09EEA CRC64; MADNKSTLPG LPDINGTLNR SMTPNTGWEG PYDMSVHLHW TQFPPVTEEW HYIIGVYITI VGLLGIMGNT TVVYIFSNTK SLRSPSNLFV VNLAVSDLIF SAVNGFPLLT VSSFHQKWIF GSLFCQLYGF VGGVFGLMSI NTLTAISIDR YVVITKPLQA SQTMTRRKVH LMIVIVWVLS ILLSIPPFFG WGAYIPEGFQ TSCTFDYLTK TARTRTYIVV LYLFGFLIPL IIIGVCYVLI IRGVRRHDQK MLTITRSMKT EDARANNKRA RSELRISKIA MTVTCLFIIS WSPYAIIALI AQFGPAHWIT PLVSELPMML AKSSSMHNPV VYALSHPKFR KALYQRVPWL FCCCKPKEKA DFRTSVCSKR SVTRTESVNS DVSSVISNLS DSTTTLGLTS EGATRANRET SFRRSVSIIK GDEDPCTHPD TFLLAYKEVE VGNLFDMTDD QNRRDSNLHS LYIPTRVQHR PTTQSLGTTP GGVYIVDNGQ RVNGLTFNS // ID OPSX_HUMAN STANDARD; PRT; 337 AA. AC O14718; Q7RTS4; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 18-APR-2006, entry version 44. DE Visual pigment-like receptor peropsin. GN Name=RRH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Retina; RX MEDLINE=97420780; PubMed=9275222; DOI=10.1073/pnas.94.18.9893; RA Sun H., Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.; RT "Peropsin, a novel visual pigment-like protein located in the apical RT microvilli of the retinal pigment epithelium."; RL Proc. Natl. Acad. Sci. U.S.A. 94:9893-9898(1997). RN [2] RP GENE STRUCTURE. RX MEDLINE=22730755; PubMed=12542842; DOI=10.1186/1471-2164-4-3; RA Bellingham J., Wells D.J., Foster R.G.; RT "In silico characterisation and chromosomal localisation of human RRH RT (peropsin) -- implications for opsin evolution."; RL BMC Genomics 4:3-3(2003). CC -!- FUNCTION: May play a role in rpe physiology either by detecting CC light directly or by monitoring the concentration of retinoids or CC other photoreceptor-derived compounds. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein (By CC similarity). CC -!- TISSUE SPECIFICITY: Found only in the eye, where it is localized CC to the retinal pigment epithelium (RPE). In the RPE, it is CC localized to the microvilli that surround the photoreceptor outer CC segments. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF012270; AAC51757.1; -; mRNA. DR EMBL; BK000958; DAA00976.1; -; Genomic_DNA. DR UniGene; Hs.352262; -. DR HSSP; P02699; 1FDF. DR Ensembl; ENSG00000180245; Homo sapiens. DR HGNC; HGNC:10450; RRH. DR MIM; 605224; gene. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS. DR GO; GO:0007601; P:visual perception; TAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR002962; Peropsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR01244; PEROPSIN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Receptor; Transducer; Transmembrane. FT CHAIN 1 337 Visual pigment-like receptor peropsin. FT /FTId=PRO_0000197819. FT TOPO_DOM 1 26 Extracellular. FT TRANSMEM 27 49 1 (Potential). FT TOPO_DOM 50 61 Cytoplasmic. FT TRANSMEM 62 87 2 (Potential). FT TOPO_DOM 88 101 Extracellular. FT TRANSMEM 102 121 3 (Potential). FT TOPO_DOM 122 140 Cytoplasmic. FT TRANSMEM 141 164 4 (Potential). FT TOPO_DOM 165 188 Extracellular. FT TRANSMEM 189 212 5 (Potential). FT TOPO_DOM 213 240 Cytoplasmic. FT TRANSMEM 241 264 6 (Potential). FT TOPO_DOM 265 272 Extracellular. FT TRANSMEM 273 297 7 (Potential). FT TOPO_DOM 298 337 Cytoplasmic. FT BINDING 284 284 Retinal chromophore (covalent). FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT DISULFID 98 175 Potential. SQ SEQUENCE 337 AA; 37423 MW; 9DFD8847F07A28EA CRC64; MLRNNLGNSS DSKNEDGSVF SQTEHNIVAT YLIMAGMISI ISNIIVLGIF IKYKELRTPT NAIIINLAVT DIGVSSIGYP MSAASDLYGS WKFGYAGCQV YAGLNIFFGM ASIGLLTVVA VDRYLTICLP DVGRRMTTNT YIGLILGAWI NGLFWALMPI IGWASYAPDP TGATCTINWR KNDRSFVSYT MTVIAINFIV PLTVMFYCYY HVTLSIKHHT TSDCTESLNR DWSDQIDVTK MSVIMICMFL VAWSPYSIVC LWASFGDPKK IPPPMAIIAP LFAKSSTFYN PCIYVVANKK FRRAMLAMFK CQTHQTMPVT SILPMDVSQN PLASGRI // ID OPN3_HUMAN STANDARD; PRT; 402 AA. AC Q9H1Y3; Q8IX08; Q9Y344; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 18-APR-2006, entry version 40. DE Opsin-3 (Encephalopsin) (Panopsin). GN Name=OPN3; Synonyms=ECPN; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RX MEDLINE=99252448; PubMed=10234000; RA Blackshaw S., Snyder S.H.; RT "Encephalopsin: a novel mammalian extraretinal opsin discretely RT localized in the brain."; RL J. Neurosci. 19:3681-3690(1999). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RX MEDLINE=21295039; PubMed=11401433; DOI=10.1006/geno.2001.6469; RA Halford S., Freedman M.S., Bellingham J., Inglis S.L., RA Poopalasundaram S., Soni B.G., Foster R.G., Hunt D.M.; RT "Characterization of a novel human opsin gene with wide tissue RT expression and identification of embedded and flanking genes on RT chromosome 1q43."; RL Genomics 72:203-208(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RX PubMed=12242008; DOI=10.1016/S0378-1119(02)00799-0; RA Kasper G., Taudien S., Staub E., Mennerich D., Rieder M., Hinzmann B., RA Dahl E., Schwidetzky U., Rosenthal A., Rump A.; RT "Different structural organization of the encephalopsin gene in man RT and mouse."; RL Gene 295:27-32(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Human chromosome 1 international sequencing consortium; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ovary; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May play a role in encephalic photoreception. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=1-4b-5-6; CC IsoId=Q9H1Y3-1; Sequence=Displayed; CC Name=2; Synonyms=1-2-5-6; CC IsoId=Q9H1Y3-2; Sequence=VSP_010209; CC -!- TISSUE SPECIFICITY: Strongly expressed in brain. Highly expressed CC in the preoptic area and paraventricular nucleus of the CC hypothalamus. Shows highly patterned expression in other regions CC of the brain, being enriched in selected regions of the cerebral CC cortex, cerebellar Purkinje cells, a subset of striatal neurons, CC selected thalamic nuclei, and a subset of interneurons in the CC ventral horn of the spinal cord. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF140242; AAD32671.1; -; mRNA. DR EMBL; AF303588; AAK37447.1; -; mRNA. DR EMBL; AF482426; AAO15715.1; -; Genomic_DNA. DR EMBL; AF482426; AAO15717.1; -; Genomic_DNA. DR EMBL; AL133390; CAC19785.1; -; Genomic_DNA. DR EMBL; BC036773; AAH36773.1; -; mRNA. DR UniGene; Hs.409081; -. DR UniGene; Hs.534399; -. DR HSSP; P02699; 1FDF. DR Ensembl; ENSG00000054277; Homo sapiens. DR HGNC; HGNC:14007; OPN3. DR MIM; 606695; gene. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0008020; F:G-protein coupled photoreceptor activity; NAS. DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS. DR GO; GO:0007602; P:phototransduction; NAS. DR GO; GO:0042752; P:regulation of circadian rhythm; NAS. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Alternative splicing; Chromophore; G-protein coupled receptor; KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Photoreceptor protein; KW Receptor; Retinal protein; Sensory transduction; Transducer; KW Transmembrane. FT CHAIN 1 402 Opsin-3. FT /FTId=PRO_0000197813. FT TOPO_DOM 1 40 Extracellular (Potential). FT TRANSMEM 41 65 1 (Potential). FT TOPO_DOM 66 77 Cytoplasmic (Potential). FT TRANSMEM 78 102 2 (Potential). FT TOPO_DOM 103 117 Extracellular (Potential). FT TRANSMEM 118 137 3 (Potential). FT TOPO_DOM 138 153 Cytoplasmic (Potential). FT TRANSMEM 154 177 4 (Potential). FT TOPO_DOM 178 201 Extracellular (Potential). FT TRANSMEM 202 229 5 (Potential). FT TOPO_DOM 230 255 Cytoplasmic (Potential). FT TRANSMEM 256 279 6 (Potential). FT TOPO_DOM 280 287 Extracellular (Potential). FT TRANSMEM 288 312 7 (Potential). FT TOPO_DOM 313 402 Cytoplasmic (Potential). FT BINDING 299 299 Retinal chromophore (covalent). FT LIPID 325 325 S-palmitoyl cysteine (By similarity). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 198 198 N-linked (GlcNAc...) (Potential). FT DISULFID 114 188 By similarity. FT VARSPLIC 126 231 IVSIATLTVLAYERYIRVVHARVINFSWAWRAITYIWLYSL FT AWAGAPLLGWNRYILDVHGLGCTVDWKSKDANDSSFVLFLF FT LGCLVVPLGVIAHCYGHILYSIRM -> WISQLQAATREAR FT ASMGPVQQGTICMQ (in isoform 2). FT /FTId=VSP_010209. FT CONFLICT 390 396 NGSKVDV -> IGVQSLML (in Ref. 1). SQ SEQUENCE 402 AA; 44873 MW; 370F64C19F834A71 CRC64; MYSGNRSGGH GYWDGGGAAG AEGPAPAGTL SPAPLFSPGT YERLALLLGS IGLLGVGNNL LVLVLYYKFQ RLRTPTHLLL VNISLSDLLV SLFGVTFTFV SCLRNGWVWD TVGCVWDGFS GSLFGIVSIA TLTVLAYERY IRVVHARVIN FSWAWRAITY IWLYSLAWAG APLLGWNRYI LDVHGLGCTV DWKSKDANDS SFVLFLFLGC LVVPLGVIAH CYGHILYSIR MLRCVEDLQT IQVIKILKYE KKLAKMCFLM IFTFLVCWMP YIVICFLVVN GHGHLVTPTI SIVSYLFAKS NTVYNPVIYV FMIRKFRRSL LQLLCLRLLR CQRPAKDLPA AGSEMQIRPI VMSQKDGDRP KKKVTFNSSS IIFIITSDES LSVDDSDKTN GSKVDVIQVR PL // ID RGR_BOVIN STANDARD; PRT; 291 AA. AC P47803; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 04-APR-2006, entry version 38. DE RPE-retinal G protein-coupled receptor. GN Name=RGR; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RX MEDLINE=94081108; PubMed=8258527; RA Jiang M., Pandey S., Fong H.K.W.; RT "An opsin homologue in the retina and pigment epithelium."; RL Invest. Ophthalmol. Vis. Sci. 34:3669-3678(1993). CC -!- FUNCTION: Receptor for all-trans- and 11-cis-retinal. Binds CC preferentially to the former and may catalyze the isomerization of CC the chromophore by a retinochrome-like mechanism. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Preferentially expressed at high levels in the CC retinal pigment epithelium (RPE) and Mueller cells of the neural CC retina. CC -!- PTM: Covalently binds all-trans- and 11-cis-retinal. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S67535; AAB29270.1; -; mRNA. DR PIR; I46965; I46965. DR UniGene; Bt.567; -. DR HSSP; P02699; 1F88. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001793; RPE_GPCR. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00667; RPERETINALR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 291 RPE-retinal G protein-coupled receptor. FT /FTId=PRO_0000197821. FT TOPO_DOM 1 15 Extracellular (Potential). FT TRANSMEM 16 36 1 (Potential). FT TOPO_DOM 37 52 Cytoplasmic (Potential). FT TRANSMEM 53 73 2 (Potential). FT TOPO_DOM 74 91 Extracellular (Potential). FT TRANSMEM 92 112 3 (Potential). FT TOPO_DOM 113 130 Cytoplasmic (Potential). FT TRANSMEM 131 151 4 (Potential). FT TOPO_DOM 152 175 Extracellular (Potential). FT TRANSMEM 176 196 5 (Potential). FT TOPO_DOM 197 219 Cytoplasmic (Potential). FT TRANSMEM 220 240 6 (Potential). FT TOPO_DOM 241 247 Extracellular (Potential). FT TRANSMEM 248 268 7 (Potential). FT TOPO_DOM 269 291 Cytoplasmic (Potential). FT BINDING 255 255 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 172 172 N-linked (GlcNAc...) (Potential). FT DISULFID 88 162 Potential. SQ SEQUENCE 291 AA; 31961 MW; A25964BBDCA25E98 CRC64; MAESGTLPTG FGELEVLAVG TVLLVEALSG LSLNILTILS FCKTPELRTP SHLLVLSLAL ADSGISLNAL VAATSSLLRR WPYGSEGCQA HGFQGFVTAL ASICSSAAVA WGRYHHFCTR SRLDWNTAVS LVFFVWLSSA FWAALPLLGW GHYDYEPLGT CCTLDYSRGD RNFTSFLFTM AFFNFLLPLF ITVVSYRLME QKLGKTSRPP VNTVLPARTL LLGWGPYALL YLYATIADAT SISPKLQMVP ALIAKAVPTV NAMNYALGSE MVHRGIWQCL SPQRREHSRE Q //