ID A0A897TIV4_NANAN Unreviewed; 352 AA. AC A0A897TIV4; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 27-NOV-2024, entry version 14. DE RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951}; GN Name=rh2a-beta {ECO:0000313|EMBL:QSG73667.1}; OS Nannacara anomala (Goldeneye cichlid). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids; OC Cichlasomatinae; Cichlasomatini; Nannacara. OX NCBI_TaxID=168802 {ECO:0000313|EMBL:QSG73667.1}; RN [1] {ECO:0000313|EMBL:QSG73667.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=33619757; RA Torres-Dowdall J., Karagic N., Harer A., Meyer A.; RT "Diversity in visual sensitivity across Neotropical cichlid fishes via RT differential expression and intraretinal variation of opsin genes."; RL Mol. Ecol. 0:0-0(2021). 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; MW588232; QSG73667.1; -; mRNA. 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 49..71 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 83..103 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 123..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..317 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; 38459 MW; 5554DFD35D2A6627 CRC64; MGWDGGIEPN GTEGKNFYIP MSNRTGIVRS PFEYPXXXXX XXXXXXXXAF YMFFLICTGT PINGLTLFVT AQNKKLRQPL NYILVNLAVA GLIMCCFGFT ITLTSALNGY FILGPTFCAI EGFMATLGGE VALWSLVVLA IERYVVVCKP MGSFKFSGTH AGAGVLFTWI MAMACAGPPL FGWSRYIPEG MQCSCGPDYY TLAPGFNNES YVIYMFVVHF FIPVFVIFFT YGSLVMTVKA AAAQQQDSAS TQKAEKEVTR MCILMVLGFL VAWTPYASFA GWIFLNKGAS FSALTAALPA FFAKSSALYN PIIYVLMNKQ FRNCMLSTIG MGGMVEDETS VSASKTEVSS VS //