ID OPSD_SPAAU Reviewed; 353 AA. AC Q9YH02; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 11-DEC-2019, entry version 80. DE RecName: Full=Rhodopsin; GN Name=rho; OS Sparus aurata (Gilthead sea bream). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Spariformes; Sparidae; Sparus. OX NCBI_TaxID=8175; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RA Archer S.N., Hirano J.; RT "Comparative analysis of opsins in Mediterranian coastal fish."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). 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}. 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; Y18665; CAA77247.1; -; mRNA. DR SMR; Q9YH02; -. DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB. DR GO; GO:0097381; C:photoreceptor disc 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:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. 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 Pfam; PF00001; 7tm_1; 1. DR Pfam; PF10413; Rhodopsin_N; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. 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. PE 2: Evidence at transcript 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..353 FT /note="Rhodopsin" FT /id="PRO_0000197722" 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..353 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" 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 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 CARBOHYD 200 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 110..187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 353 AA; 39523 MW; DC56FEF259355873 CRC64; MNGTEGPFFY VPMVNTSGIV RSPYEYPQYY LVNPAAYAAL GAYMFLLILV GFPINFLTLY VTIEHKKLRT PLNYILLNLA VADLFMVFGG FTTTMYTSMH GYFVLGRLGC NIEGFFATLG GEIALWSLVV LAIERWVVVC KPISNFRFGE NHAIMGLAFT WIMAMACAAP PLVGWSRYIP EGMQCSCGID YYTRAEGFNN ESFVIYMFIC HFSIPLTIVF FCYGRLLCAV KEAAAAQQES ETTQRAEREV TRMVIMMVIA FLVCWLPYAG VAWWIFTHQG SEFGPVFMTI PAFFAKSSSI YNPMIYICLN KQFRHCMITT LCCGKNPFEE EEGASTASKT EASSVSSSSV SPA //