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 25-OCT-2017, entry version 75. 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: Visual pigments such as rhodopsin and porphyropsin are CC light-absorbing molecules that mediate vision. Rhodopsin consists CC of an apoprotein, opsin, covalently linked to 11-cis-retinal. This CC receptor is coupled to the activation of phospholipase C. CC Porphyropsin consists of opsin covalently linked to 11-cis 3,4- CC didehydroretinal. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates CC vision in dim light. 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. {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 ProteinModelPortal; Q9YH02; -. DR SMR; Q9YH02; -. DR HOVERGEN; HBG107442; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004930; F:G-protein coupled receptor activity; 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:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 4.10.840.10; -; 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 InterPro; IPR037114; Rhodopsin_N_sf. 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 Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix; KW Vision. FT CHAIN 1 353 Rhodopsin. FT /FTId=PRO_0000197722. FT TOPO_DOM 1 36 Extracellular. FT TRANSMEM 37 61 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 62 73 Cytoplasmic. FT TRANSMEM 74 98 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 99 113 Extracellular. FT TRANSMEM 114 133 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 134 152 Cytoplasmic. FT TRANSMEM 153 176 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 177 202 Extracellular. FT TRANSMEM 203 230 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 231 252 Cytoplasmic. FT TRANSMEM 253 276 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 277 284 Extracellular. FT TRANSMEM 285 309 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 310 353 Cytoplasmic. FT MOD_RES 296 296 N6-(retinylidene)lysine. {ECO:0000250}. FT LIPID 322 322 S-palmitoyl cysteine. {ECO:0000250}. FT CARBOHYD 2 2 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 15 15 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 200 200 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 110 187 {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 //