OPSD_PIG
ID OPSD_PIG Reviewed; 348 AA.
AC O18766;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Rhodopsin;
GN Name=RHO; Synonyms=RHO1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF PRO-347.
RX PubMed=9335046; DOI=10.1038/nbt1097-965;
RA Petters R.M., Alexander C.A., Wells K.D., Collins E.B., Sommer J.R.,
RA Blanton M.R., Rojas G., Hao Y., Flowers W.L., Banin E., Cideciyan A.V.,
RA Jacobson S.G., Wong F.;
RT "Genetically engineered large animal model for studying cone photoreceptor
RT survival and degeneration in retinitis pigmentosa.";
RL Nat. Biotechnol. 15:965-970(1997).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. Required for photoreceptor cell viability after birth
CC (PubMed:9335046). Light-induced isomerization of 11-cis to all-trans
CC retinal triggers a conformational change that activates signaling via
CC G-proteins. Subsequent receptor phosphorylation mediates displacement
CC of 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, ECO:0000269|PubMed:9335046}.
CC -!- SUBUNIT: Homodimer (By similarity). May form a complex composed of RHO,
CC GRK1 and RCVRN in a Ca(2+)-dependent manner; RCVRN prevents the
CC interaction between GRK1 and RHO (By similarity). Interacts with GRK1
CC (By similarity). Interacts (phosphorylated form) with SAG. Interacts
CC with GNAT1. Interacts with GNAT3. SAG and G-proteins compete for a
CC common binding site (By similarity). Interacts with PRCD; the
CC interaction promotes PRCD stability. {ECO:0000250|UniProtKB:P02699,
CC ECO:0000250|UniProtKB:P08100}.
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}.
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DR EMBL; AF008947; AAB86808.1; -; mRNA.
DR RefSeq; NP_999386.1; NM_214221.1.
DR AlphaFoldDB; O18766; -.
DR BMRB; O18766; -.
DR SMR; O18766; -.
DR IntAct; O18766; 2.
DR STRING; 9823.ENSSSCP00000012353; -.
DR PaxDb; O18766; -.
DR PeptideAtlas; O18766; -.
DR PRIDE; O18766; -.
DR Ensembl; ENSSSCT00000012686; ENSSSCP00000012353; ENSSSCG00000011590.
DR Ensembl; ENSSSCT00005048157; ENSSSCP00005029658; ENSSSCG00005030296.
DR Ensembl; ENSSSCT00015074764; ENSSSCP00015029990; ENSSSCG00015056060.
DR Ensembl; ENSSSCT00025037995; ENSSSCP00025015998; ENSSSCG00025027966.
DR Ensembl; ENSSSCT00030059461; ENSSSCP00030027215; ENSSSCG00030042653.
DR Ensembl; ENSSSCT00035102385; ENSSSCP00035043667; ENSSSCG00035075320.
DR Ensembl; ENSSSCT00040071930; ENSSSCP00040030713; ENSSSCG00040053115.
DR Ensembl; ENSSSCT00045008896; ENSSSCP00045006043; ENSSSCG00045005359.
DR Ensembl; ENSSSCT00050001985; ENSSSCP00050000602; ENSSSCG00050001576.
DR Ensembl; ENSSSCT00055022503; ENSSSCP00055017796; ENSSSCG00055011447.
DR Ensembl; ENSSSCT00060021418; ENSSSCP00060008807; ENSSSCG00060016077.
DR Ensembl; ENSSSCT00065013494; ENSSSCP00065005502; ENSSSCG00065010157.
DR GeneID; 397437; -.
DR KEGG; ssc:397437; -.
DR CTD; 6010; -.
DR VGNC; VGNC:92283; RHO.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; O18766; -.
DR OMA; VICGFTT; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR Reactome; R-SSC-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-SSC-2485179; Activation of the phototransduction cascade.
DR Reactome; R-SSC-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-SSC-418594; G alpha (i) signalling events.
DR Reactome; R-SSC-419771; Opsins.
DR Reactome; R-SSC-5620916; VxPx cargo-targeting to cilium.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000011590; Expressed in heart.
DR Genevisible; O18766; SS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0120200; C:rod photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:1990913; C:sperm head plasma membrane; IEA:Ensembl.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
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:0016038; P:absorption of visible light; ISS:AgBase.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0043052; P:thermotaxis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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 Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF10413; Rhodopsin_N; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00579; RHODOPSIN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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 1: Evidence at protein 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_0000197699"
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 335
FT /note="Phosphothreonine"
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 MUTAGEN 347
FT /note="P->L: Causes photoreceptor degeneration beginning
FT during the first weeks after birth."
FT /evidence="ECO:0000269|PubMed:9335046"
SQ SEQUENCE 348 AA; 39027 MW; 272E6B0BEE3DA51B CRC64;
MNGTEGPNFY VPFSNKTGVV RSPFEYPQYY LAEPWQFSML AAYMFMLIVL GFPINFLTLY
VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGLALT WVMALACAAP PLVGWSRYIP
EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFSIPLVIIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVVA FLICWLPYAS VAFYIFTHQG SDFGPIFMTI PAFFAKSASI
YNPVIYIMMN KQFRNCMLTT LCCGKNPLGD DEASTTTSKT ETSQVAPA
