ID A0A481Y5B9_9CICH Unreviewed; 352 AA. AC A0A481Y5B9; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 27-NOV-2024, entry version 20. DE RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951}; OS Cichla monoculus. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids; OC Cichlinae; Cichlini; Cichla. OX NCBI_TaxID=81334 {ECO:0000313|EMBL:QBK51058.1}; RN [1] {ECO:0000313|EMBL:QBK51058.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30787138; RA Escobar-Camacho D., Pierotti M.E.R., Ferenc V., Sharpe D.M.T., Ramos E., RA Martins C., Carleton K.L.; RT "Variable vision in variable environments: the visual system of an invasive RT cichlid (Cichla monoculus, Agassiz, 1831) in Lake Gatun, Panama."; RL J. Exp. Biol. 0:0-0(2019). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently linked CC to cis-retinal. {ECO:0000256|ARBA:ARBA00002881}. 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 --------------------------------------------------------------------------- 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; MK568305; QBK51058.1; -; mRNA. DR AlphaFoldDB; A0A481Y5B9; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001750; C:photoreceptor outer segment; IEA:TreeGrafter. DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0071482; P:cellular response to light stimulus; IEA:TreeGrafter. DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR FunFam; 1.20.1070.10:FF:000018; Rhodopsin; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR050125; GPCR_opsins. 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:SF153; GREEN-SENSITIVE OPSIN; 1. DR PANTHER; PTHR24240; OPSIN; 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 2: Evidence at transcript level; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|PIRSR:PIRSR600732- KW 50}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR600732-3}; KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040, KW ECO:0000256|RuleBase:RU004951}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR600732- KW 4}; 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|ARBA:ARBA00022543, KW ECO:0000256|RuleBase:RU004951}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004951}; KW Retinal protein {ECO:0000256|ARBA:ARBA00022925, KW ECO:0000256|PIRSR:PIRSR600732-50}; KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606, KW ECO:0000256|RuleBase:RU004951}; KW Transducer {ECO:0000256|ARBA:ARBA00023224, 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 48..71 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 83..107 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 119..141 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 161..181 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 211..231 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 262..285 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 291..316 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT DOMAIN 62..314 FT /note="G-protein coupled receptors family 1 profile" FT /evidence="ECO:0000259|PROSITE:PS50262" FT BINDING 209 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1" FT SITE 121 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 304 FT /note="N6-(retinylidene)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-50" FT CARBOHYD 10 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-4" FT CARBOHYD 23 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-4" FT DISULFID 118..195 FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3" SQ SEQUENCE 352 AA; 38695 MW; B42EEFC64EA03184 CRC64; MVWDGGIEPN GTEGKNFYIP MSNRTGIVRS PFEYPQYYMV DPMIYKVLAF YMFFLICTGT PINGLTLFVT AQNKKLRQPL NYILVNLAVA GLIMCCFGFT ITITSALNGY FILGPTFCAI EGFMATLGGE VALWSLVVLA VERYIVVCKP MGSFKFSGTH AGAGVLFTWI MAMACAAPPL VGWSRYLPEG MQCSCGPDYY TLAPGFNNES YVIYMFVVHF FVPVFVIFFT YGSLVMTVKA AAAQQQDSAS TQKAEKEVTR MCVLMVLGFL VAWTPYATFA GWIFLNKGAS FTALTAALPA FFAKSSALYN PVIYVLMNKQ FRNCMLTTIG MGGMVEDETS VSTSKTEVSS VS //