OPSD_SHEEP
ID OPSD_SHEEP Reviewed; 348 AA.
AC P02700;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Rhodopsin;
GN Name=RHO;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE.
RX DOI=10.1016/0141-8130(84)90066-7;
RA Pappin D.J.C., Elipoulos E., Brett M., Findlay J.B.C.;
RT "A structural model for ovine rhodopsin.";
RL Int. J. Biol. Macromol. 6:73-76(1984).
RN [2]
RP PROTEIN SEQUENCE OF 1-111 AND 144-239.
RX PubMed=6224479; DOI=10.1042/bj2110661;
RA Brett M., Findlay J.B.C.;
RT "Isolation and characterization of the CNBr peptides from the
RT proteolytically derived N-terminal fragment of ovine opsin.";
RL Biochem. J. 211:661-670(1983).
RN [3]
RP PROTEIN SEQUENCE OF 240-348, SUBCELLULAR LOCATION, AND RETINAL-BINDING
RP SITE.
RX PubMed=7278988; DOI=10.1038/293314a0;
RA Findlay J.B.C., Brett M., Pappin D.J.C.;
RT "Primary structure of C-terminal functional sites in ovine rhodopsin.";
RL Nature 293:314-316(1981).
RN [4]
RP RETINAL-BINDING SITE AT LYS-296.
RX PubMed=6370231; DOI=10.1042/bj2170605;
RA Pappin D.J.C., Findlay J.B.C.;
RT "Sequence variability in the retinal-attachment domain of mammalian
RT rhodopsins.";
RL Biochem. J. 217:605-613(1984).
RN [5]
RP PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338 AND SER-343, AND
RP SUBCELLULAR LOCATION.
RX PubMed=6466303; DOI=10.1042/bj2200773;
RA Thompson P., Findlay J.B.C.;
RT "Phosphorylation of ovine rhodopsin. Identification of the phosphorylated
RT sites.";
RL Biochem. J. 220:773-780(1984).
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).
CC {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100,
CC ECO:0000250|UniProtKB:P15409}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:6466303,
CC ECO:0000269|PubMed:7278988}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:6466303, ECO:0000269|PubMed:7278988}. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:6466303, ECO:0000269|PubMed:7278988}.
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:0000269|PubMed:6466303}.
CC -!- PTM: Contains one covalently linked retinal chromophore
CC (PubMed:7278988, PubMed:6370231). Upon light absorption, the covalently
CC bound 11-cis-retinal is converted to all-trans-retinal. After
CC hydrolysis of the Schiff base and release of the covalently bound all-
CC trans-retinal, active rhodopsin is regenerated by binding of a fresh
CC molecule of 11-cis-retinal (By similarity).
CC {ECO:0000250|UniProtKB:P02699, ECO:0000269|PubMed:6370231,
CC ECO:0000269|PubMed:7278988}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR PIR; A30407; OOSH.
DR AlphaFoldDB; P02700; -.
DR BMRB; P02700; -.
DR SMR; P02700; -.
DR STRING; 9940.ENSOARP00000015330; -.
DR iPTMnet; P02700; -.
DR eggNOG; KOG3656; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
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; Direct protein sequencing;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Phosphoprotein; Photoreceptor protein;
KW Receptor; Reference proteome; Retinal protein; Sensory transduction;
KW Transducer; Transmembrane; Transmembrane helix; Vision; Zinc.
FT CHAIN 1..348
FT /note="Rhodopsin"
FT /id="PRO_0000197719"
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:0000269|PubMed:6370231,
FT ECO:0000305|PubMed:7278988"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6466303"
FT MOD_RES 334
FT /note="Phosphoserine; by RK and GRK7"
FT /evidence="ECO:0000269|PubMed:6466303"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:6466303"
FT MOD_RES 335
FT /note="Phosphothreonine; by RK and GRK7"
FT /evidence="ECO:0000269|PubMed:6466303"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:6466303"
FT MOD_RES 336
FT /note="Phosphothreonine; by RK and GRK7"
FT /evidence="ECO:0000269|PubMed:6466303"
FT MOD_RES 338
FT /note="Phosphoserine; by RK and GRK7"
FT /evidence="ECO:0000269|PubMed:6466303"
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; by RK and GRK7"
FT /evidence="ECO:0000269|PubMed:6466303"
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"
SQ SEQUENCE 348 AA; 38892 MW; AAFD6F0D6A8BAEE5 CRC64;
MNGTEGPNFY VPFSNKTGVV RSPFEAPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLVGWSRYIP
QGMQCSCGAL YFTLKPEINN ESFVIYMFVV HFSIPLIVIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SDFGPIFMTI PAFFAKSSSV
YNPVIYIMMN KQFRNCMLTT LCCGKNPLGD DEASTTVSKT ETSQVAPA
