ID D2K4B4_9TELE Unreviewed; 273 AA. AC D2K4B4; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 03-MAY-2023, entry version 43. DE RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951}; DE Flags: Fragment; GN Name=RH {ECO:0000313|EMBL:ACZ64913.1}; OS Poecilia picta (swamp guppy). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae; OC Poecilia. OX NCBI_TaxID=69234 {ECO:0000313|EMBL:ACZ64913.1}; RN [1] {ECO:0000313|EMBL:ACZ64913.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19922806; DOI=10.1016/j.ympev.2009.11.006; RA Meredith R.W., Pires M.N., Reznick D.N., Springer M.S.; RT "Molecular phylogenetic relationships and the evolution of the placenta in RT Poecilia (Micropoecilia) (Poeciliidae: Cyprinodontiformes)."; RL Mol. Phylogenet. Evol. 55:631-639(2010). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141, CC ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}. CC -!- PTM: Contains one covalently linked retinal chromophore. CC {ECO:0000256|PIRSR:PIRSR600732-50}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin CC subfamily. {ECO:0000256|RuleBase:RU004951}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|RuleBase:RU004951}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GU179279; ACZ64913.1; -; Genomic_DNA. DR EMBL; GU179280; ACZ64914.1; -; Genomic_DNA. DR AlphaFoldDB; D2K4B4; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000732; Rhodopsin. DR PANTHER; PTHR24240; OPSIN; 1. DR PANTHER; PTHR24240:SF15; RHODOPSIN; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00579; RHODOPSIN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 3: Inferred from homology; KW Chromophore {ECO:0000256|PIRSR:PIRSR600732-50, KW ECO:0000256|RuleBase:RU004951}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR600732-3}; KW G-protein coupled receptor {ECO:0000256|RuleBase:RU004951}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004951}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR600732-1}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Photoreceptor protein {ECO:0000256|RuleBase:RU004951}; KW Receptor {ECO:0000256|RuleBase:RU004951}; KW Retinal protein {ECO:0000256|PIRSR:PIRSR600732-50, KW ECO:0000256|RuleBase:RU004951}; KW Sensory transduction {ECO:0000256|RuleBase:RU004951}; KW Transducer {ECO:0000256|RuleBase:RU004951}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU004951}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU004951}; Vision {ECO:0000256|ARBA:ARBA00023305}; KW Zinc {ECO:0000256|PIRSR:PIRSR600732-1}. FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 44..64 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 84..102 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 123..142 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 172..192 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 223..245 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT DOMAIN 23..273 FT /note="G-protein coupled receptors family 1 profile" FT /evidence="ECO:0000259|PROSITE:PS50262" FT BINDING 170 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1" FT BINDING 248 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1" FT SITE 82 FT /note="Plays an important role in the conformation switch FT to the active conformation" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-2" FT MOD_RES 265 FT /note="N6-(retinylidene)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-50" FT DISULFID 79..156 FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACZ64913.1" FT NON_TER 273 FT /evidence="ECO:0000313|EMBL:ACZ64913.1" SQ SEQUENCE 273 AA; 30747 MW; ACF72B31BA7E4F68 CRC64; VSPAAYACLG AYMFFLILVG FPINFLTLYV TIEHKKLRTP LNYILLNLAV ADLFMVFGGF TTTIYTSMHG YFVLGRLGCN LEGYFATLGG EIGLWSLVVL AVERWLVVCK PISNFRFSEN HAIMGLVFTW IMANTCAAPP LLGWSRYIPE GMQCSCGVDY YTRAEGFNNE SFVVYMFICH FCIPLVVVFF CYGRLLCAVK EAAAAQQESE TTQRAEREVT RMVVIMVIGF LVCWIPYASV AWYIFTHQGS EFGPLFMTIP AFFAKTASIY NPM //