ID OPSD_RAT Reviewed; 348 AA. AC P51489; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 154. DE RecName: Full=Rhodopsin; GN Name=Rho; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Sprague-Dawley; TISSUE=Retinal rod cell; RX PubMed=7654522; DOI=10.1007/bf02736734; RA Barnstable C.J., Morabito M.A.; RT "Isolation and coding sequence of the rat rod opsin gene."; RL J. Mol. Neurosci. 5:207-209(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Retina; RA Huber A., Baker B.B., Sander P., Gerdon G., Paulsen R., Williams T.P.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light CC intensity. Required for photoreceptor cell viability after birth (By CC similarity). Light-induced isomerization of 11-cis to all-trans retinal CC triggers a conformational change that activates signaling via G- CC proteins. Subsequent receptor phosphorylation mediates displacement of CC the bound G-protein alpha subunit by the arrestin SAG and terminates CC signaling (By similarity). {ECO:0000250|UniProtKB:P02699, CC ECO:0000250|UniProtKB:P08100}. CC -!- SUBUNIT: Homodimer. May form a complex composed of RHO, GRK1 and RCVRN CC in a Ca(2+)-dependent manner; RCVRN prevents the interaction between CC GRK1 and RHO (By similarity). Interacts with GRK1 (By similarity). CC Interacts (phosphorylated form) with SAG (By similarity). Interacts CC with GNAT1 (By similarity). Interacts with GNAT3. SAG and G-proteins CC compete for a common binding site (By similarity). Interacts with PRCD; CC the interaction promotes PRCD stability (By similarity). Forms a CC complex with ASAP1 and ARF4. Forms a complex with ASAP1, RAB11A, CC Rabin8/RAB3IP, ARF4 and RAB11FIP3; the complex regulates Golgi-to-cilia CC rhodopsin/RHO transport in photoreceptors (By similarity). CC {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100, CC ECO:0000250|UniProtKB:P15409}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02699}; Multi- CC pass membrane protein {ECO:0000250|UniProtKB:P02699}. Cell projection, CC cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P02699}. 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. Upon light CC absorption, the covalently bound 11-cis-retinal is converted to all- CC trans-retinal. After hydrolysis of the Schiff base and release of the CC covalently bound all-trans-retinal, active rhodopsin is regenerated by CC binding of a fresh molecule of 11-cis-retinal. 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; U22180; AAA84439.1; -; Genomic_DNA. DR EMBL; Z46957; CAA87081.1; -; mRNA. DR PIR; S51677; S51677. DR RefSeq; NP_254276.1; NM_033441.1. DR AlphaFoldDB; P51489; -. DR SMR; P51489; -. DR STRING; 10116.ENSRNOP00000061473; -. DR GlyCosmos; P51489; 2 sites, No reported glycans. DR GlyGen; P51489; 2 sites. DR iPTMnet; P51489; -. DR PhosphoSitePlus; P51489; -. DR PaxDb; 10116-ENSRNOP00000061473; -. DR GeneID; 24717; -. DR KEGG; rno:24717; -. DR UCSC; RGD:3573; rat. DR AGR; RGD:3573; -. DR CTD; 6010; -. DR RGD; 3573; Rho. DR eggNOG; KOG3656; Eukaryota. DR InParanoid; P51489; -. DR OrthoDB; 5350930at2759; -. DR PhylomeDB; P51489; -. DR TreeFam; TF324998; -. DR Reactome; R-RNO-2453902; The canonical retinoid cycle in rods (twilight vision). DR Reactome; R-RNO-2485179; Activation of the phototransduction cascade. DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR Reactome; R-RNO-418594; G alpha (i) signalling events. DR Reactome; R-RNO-419771; Opsins. DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium. DR PRO; PR:P51489; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005911; C:cell-cell junction; ISO:RGD. DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB. DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD. DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:RGD. DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0120200; C:rod photoreceptor outer segment; ISO:RGD. DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IDA:RGD. DR GO; GO:1990913; C:sperm head plasma membrane; ISO:RGD. DR GO; GO:0097225; C:sperm midpiece; ISO:RGD. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016918; F:retinal binding; IDA:RGD. DR GO; GO:0030507; F:spectrin binding; IDA:MGI. DR GO; GO:0016038; P:absorption of visible light; ISS:AgBase. DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; ISO:RGD. DR GO; GO:0071482; P:cellular response to light stimulus; ISO:RGD. DR GO; GO:0009583; P:detection of light stimulus; ISO:RGD. DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; ISO:RGD. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD. DR GO; GO:0010467; P:gene expression; ISO:RGD. DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:RGD. DR GO; GO:0007602; P:phototransduction; ISO:RGD. DR GO; GO:0071800; P:podosome assembly; ISO:RGD. DR GO; GO:0009585; P:red, far-red light phototransduction; IDA:RGD. DR GO; GO:0009642; P:response to light intensity; ISO:RGD. DR GO; GO:0009416; P:response to light stimulus; ISO:RGD. DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD. DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IDA:RGD. DR GO; GO:1904389; P:rod bipolar cell differentiation; ISO:RGD. DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:RGD. DR GO; GO:0043052; P:thermotaxis; ISO:RGD. DR GO; GO:0007601; P:visual perception; ISO:RGD. DR CDD; cd15080; 7tmA_MWS_opsin; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 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 PANTHER; PTHR24240; OPSIN; 1. DR PANTHER; PTHR24240:SF15; RHODOPSIN; 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 Acetylation; Cell projection; Chromophore; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Metal-binding; Palmitate; Phosphoprotein; Photoreceptor protein; Receptor; KW Reference proteome; Retinal protein; Sensory transduction; Transducer; KW Transmembrane; Transmembrane helix; Vision; Zinc. FT CHAIN 1..348 FT /note="Rhodopsin" FT /id="PRO_0000197708" 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..348 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 330..348 FT /note="Interaction with SAG" FT /evidence="ECO:0000250|UniProtKB:P02699" FT MOTIF 134..136 FT /note="'Ionic lock' involved in activated form FT stabilization" FT /evidence="ECO:0000250|UniProtKB:P02699" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P02699" FT BINDING 279 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" 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 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT MOD_RES 296 FT /note="N6-(retinylidene)lysine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT MOD_RES 334 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02700" FT MOD_RES 336 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P02700" FT MOD_RES 338 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02700" FT MOD_RES 340 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT MOD_RES 342 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT MOD_RES 343 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT LIPID 322 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P02699" FT LIPID 323 FT /note="S-palmitoyl cysteine" 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 DISULFID 110..187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 320 FT /note="S -> T (in Ref. 2; CAA87081)" FT /evidence="ECO:0000305" SQ SEQUENCE 348 AA; 39042 MW; DA0F3F90C30984BC CRC64; MNGTEGPNFY VPFSNITGVV RSPFEQPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG GEIGLWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLVGWSRYIP EGMQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIVIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV TRMVIIMVIF FLICWLPYAS VAMYIFTHQG SNFGPIFMTL PAFFAKTASI YNPIIYIMMN KQFRNCMLTS LCCGKNPLGD DEASATASKT ETSQVAPA //