OPSD_CANLF
ID OPSD_CANLF Reviewed; 348 AA.
AC P32308; P79146; Q8MK70;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Rhodopsin;
GN Name=RHO;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Retina;
RX PubMed=8206388; DOI=10.1016/0378-1119(94)90111-2;
RA Petersen-Jones S.M., Sohal A.K., Sargan D.R.;
RT "Nucleotide sequence of the canine rod-opsin-encoding gene.";
RL Gene 143:281-284(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Labrador retriever;
RX PubMed=9522129; DOI=10.3109/10425179709020893;
RA Kylma T.J., Roos C., Paulin L., Kommonen B.;
RT "The introns of the canine rod opsin gene show higher sequence homology to
RT the human than to the rodent introns.";
RL DNA Seq. 8:99-104(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANT ADRP ARG-4.
RC STRAIN=English mastiff;
RX PubMed=11972042; DOI=10.1073/pnas.082714499;
RA Kijas J.W., Cideciyan A.V., Aleman T.S., Pianta M.J., Pearce-Kelling S.E.,
RA Miller B.J., Jacobson S.G., Aguirre G.D., Acland G.M.;
RT "Naturally occurring rhodopsin mutation in the dog causes retinal
RT dysfunction and degeneration mimicking human dominant retinitis
RT pigmentosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6328-6333(2002).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. Required for photoreceptor cell viability after birth
CC (PubMed:11972042). 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:11972042}.
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 -!- DISEASE: Note=Defects in RHO are a cause of autosomal dominant
CC retinitis pigmentosa (ADRP). The phenotypic features shared by dog and
CC man include a dramatically slowed time course of recovery of rod
CC photoreceptor function after light exposure and a distinctive
CC topographic pattern to the retinal degeneration. This disease was
CC identified in the English mastiff breed. {ECO:0000269|PubMed:11972042}.
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; X71380; CAA50502.1; -; Genomic_DNA.
DR EMBL; Y09004; CAA70209.1; -; Genomic_DNA.
DR EMBL; AY092841; AAM11432.1; -; mRNA.
DR PIR; S32696; S32696.
DR RefSeq; NP_001008277.1; NM_001008276.1.
DR RefSeq; XP_005632092.1; XM_005632035.2.
DR PDB; 4UE5; EM; 9.00 A; S=50-67.
DR PDBsum; 4UE5; -.
DR AlphaFoldDB; P32308; -.
DR SMR; P32308; -.
DR STRING; 9612.ENSCAFP00000006912; -.
DR PaxDb; P32308; -.
DR GeneID; 493763; -.
DR KEGG; cfa:493763; -.
DR CTD; 6010; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P32308; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR Proteomes; UP000002254; Unplaced.
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: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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
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 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 3D-structure; Acetylation; Cell projection; Chromophore; Disease variant;
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_0000197657"
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 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 VARIANT 4
FT /note="T -> R (in ADRP)"
FT /evidence="ECO:0000269|PubMed:11972042"
FT CONFLICT 176
FT /note="S -> SSLLSHSPLVL (in Ref. 2; CAA70209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38963 MW; BB1A007C00CA04A2 CRC64;
MNGTEGPNFY VPFSNKTGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NVEGFFATLG
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP
EGMQCSCGID YYTLKPEINN ESFVIYMFVV HFAIPMIVIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SDFGPIFMTL PAFFAKSSSI
YNPVIYIMMN KQFRNCMITT LCCGKNPLGD DEASASASKT ETSQVAPA
