ID OPSD_GAMAF Reviewed; 354 AA. AC P79756; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 22-FEB-2023, entry version 92. DE RecName: Full=Rhodopsin; GN Name=rho; OS Gambusia affinis (Western mosquitofish) (Heterandria affinis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae; OC Gambusia. OX NCBI_TaxID=33528; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Holbrooki; TISSUE=Retina; RX PubMed=9236103; DOI=10.1111/j.1095-8649.1997.tb02528.x; RA Archer S.N., Hirano J.; RT "Opsin sequences of the rod visual pigments in two species of Poeciliid RT fish."; RL J. Fish Biol. 51:215-219(1997). RN [2] RP RETINAL-BINDING, AND FUNCTION. RX PubMed=18422881; DOI=10.1111/j.1751-1097.2008.00344.x; RA Toyama M., Hironaka M., Yamahama Y., Horiguchi H., Tsukada O., Uto N., RA Ueno Y., Tokunaga F., Seno K., Hariyama T.; RT "Presence of rhodopsin and porphyropsin in the eyes of 164 fishes, RT representing marine, diadromous, coastal and freshwater species--a RT qualitative and comparative study."; RL Photochem. Photobiol. 84:996-1002(2008). CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light CC intensity. While most salt water fish species use retinal as CC chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of CC retinal and 3-dehydroretinal (PubMed:18422881). Light-induced CC isomerization of 11-cis to all-trans retinal triggers a conformational CC change that activates signaling via G-proteins. Subsequent receptor CC phosphorylation mediates displacement of the bound G-protein alpha CC subunit by arrestin and terminates signaling (By similarity). CC {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100, CC ECO:0000250|UniProtKB:P32309, ECO:0000269|PubMed:18422881}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08100}; Multi- CC pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell projection, CC cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P35359}. CC Note=Synthesized in the inner segment (IS) of rod photoreceptor cells CC before vectorial transport to disk membranes in the rod outer segment CC (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}. CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues CC present in the C-terminal region. {ECO:0000250|UniProtKB:P02699}. CC -!- PTM: Contains one covalently linked retinal chromophore. CC {ECO:0000250|UniProtKB:P02699}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}. 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; Y11146; CAA72033.1; -; mRNA. DR AlphaFoldDB; P79756; -. DR SMR; P79756; -. DR STRING; 33528.ENSGAFP00000031268; -. DR GlyCosmos; P79756; 2 sites, No reported glycans. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB. DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB. DR GO; GO:0016038; P:absorption of visible light; ISS:UniProtKB. DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd15080; 7tmA_MWS_opsin; 1. 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; IPR027430; Retinal_BS. DR InterPro; IPR000732; Rhodopsin. DR InterPro; IPR019477; Rhodopsin_N. DR PANTHER; PTHR24240; OPSIN; 1. DR PANTHER; PTHR24240:SF15; RHODOPSIN; 1. DR Pfam; PF00001; 7tm_1; 1. DR Pfam; PF10413; Rhodopsin_N; 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. DR PROSITE; PS00238; OPSIN; 1. PE 1: Evidence at protein level; KW Cell projection; Chromophore; Disulfide bond; G-protein coupled receptor; KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Photoreceptor protein; Receptor; Retinal protein; Sensory transduction; KW Transducer; Transmembrane; Transmembrane helix; Vision. FT CHAIN 1..354 FT /note="Rhodopsin" FT /id="PRO_0000197674" FT TOPO_DOM 1..36 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 37..61 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P02699" FT TOPO_DOM 62..73 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 74..96 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P02699" FT TOPO_DOM 97..110 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 111..133 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P02699" FT TOPO_DOM 134..152 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 153..173 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P02699" FT TOPO_DOM 174..202 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 203..224 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P02699" FT TOPO_DOM 225..252 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 253..274 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P02699" FT TOPO_DOM 275..286 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 287..308 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P02699" FT TOPO_DOM 309..354 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 333..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 134..136 FT /note="'Ionic lock' involved in activated form FT stabilization" FT /evidence="ECO:0000250|UniProtKB:P02699" FT SITE 113 FT /note="Plays an important role in the conformation switch FT to the active conformation" FT /evidence="ECO:0000250|UniProtKB:P02699" FT MOD_RES 296 FT /note="N6-(retinylidene)lysine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT LIPID 322 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT LIPID 323 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT CARBOHYD 2 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 15 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 110..187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 354 AA; 39644 MW; 1CE46D74A03D406B CRC64; MNGTEGPYFY VPMVNTTGIV RSPYEYPQYY LVSPAAYACL GAYMFFLILV GFPVNFLTLY VTIEHKKLRT PLNYILLNLA VADLFMVFGG FTTTIYTSMH GYFVLGRLGC NLEGYFATLG GEIGLWSLVV LAVERWLVVC KPISNFRFTE NHAIMGLVFT WIMANACAAP PLLGWSRYIP EGMQCSCGVD YYTRAEGFNN ESFVIYMFIC HFCIPLVVVF FCYGRLLCAV KEAAAAQQES ETTQRAEREV TRMVVILVIG FLVCWTPYAS VAWYIFSNQG SEFGPLFMTI PAFFAKSSSI YNPMIYICMN KQFRHCMITT LCCGKNPFEE EEGASTTASK TEASSVSSSS VSPA //