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 31-JAN-2018, entry version 76. 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 CC light intensity. While most salt water fish species use retinal as CC chromophore, most freshwater fish use 3-dehydroretinal, or a CC mixture of retinal and 3-dehydroretinal (By similarity). Light- CC induced isomerization of 11-cis to all-trans retinal triggers a CC conformational change that activates signaling via G-proteins. CC Subsequent receptor phosphorylation mediates displacement of the CC bound G-protein alpha subunit by arrestin and terminates signaling CC (By similarity). {ECO:0000250|UniProtKB:P02699, CC ECO:0000250|UniProtKB:P08100, ECO:0000250|UniProtKB:P32309}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08100}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell CC projection, cilium, photoreceptor outer segment CC {ECO:0000250|UniProtKB:P35359}. Note=Synthesized in the inner CC segment (IS) of rod photoreceptor cells before vectorial transport CC to disk membranes in the rod outer segment (OS) photosensory CC cilia. {ECO:0000250|UniProtKB:P08100}. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region. CC {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. 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 Cell projection; Chromophore; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphoprotein; Photoreceptor protein; Receptor; KW Retinal protein; Sensory transduction; Transducer; Transmembrane; KW Transmembrane helix; Vision. FT CHAIN 1 353 Rhodopsin. FT /FTId=PRO_0000197722. FT TOPO_DOM 1 36 Extracellular. {ECO:0000305}. FT TRANSMEM 37 61 Helical; Name=1. FT {ECO:0000250|UniProtKB:P02699}. FT TOPO_DOM 62 73 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 74 96 Helical; Name=2. FT {ECO:0000250|UniProtKB:P02699}. FT TOPO_DOM 97 110 Extracellular. {ECO:0000305}. FT TRANSMEM 111 133 Helical; Name=3. FT {ECO:0000250|UniProtKB:P02699}. FT TOPO_DOM 134 152 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 153 173 Helical; Name=4. FT {ECO:0000250|UniProtKB:P02699}. FT TOPO_DOM 174 202 Extracellular. {ECO:0000305}. FT TRANSMEM 203 224 Helical; Name=5. FT {ECO:0000250|UniProtKB:P02699}. FT TOPO_DOM 225 252 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 253 274 Helical; Name=6. FT {ECO:0000250|UniProtKB:P02699}. FT TOPO_DOM 275 286 Extracellular. {ECO:0000305}. FT TRANSMEM 287 308 Helical; Name=7. FT {ECO:0000250|UniProtKB:P02699}. FT TOPO_DOM 309 353 Cytoplasmic. {ECO:0000305}. FT MOTIF 134 136 'Ionic lock' involved in activated form FT stabilization. FT {ECO:0000250|UniProtKB:P02699}. FT SITE 113 113 Plays an important role in the FT conformation switch to the active FT conformation. FT {ECO:0000250|UniProtKB:P02699}. FT MOD_RES 296 296 N6-(retinylidene)lysine. FT {ECO:0000250|UniProtKB:P02699}. 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 //