OPSG_CAVPO
ID OPSG_CAVPO Reviewed; 364 AA.
AC Q9R024;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Medium-wave-sensitive opsin 1;
DE AltName: Full=Green cone photoreceptor pigment;
DE AltName: Full=Green-sensitive opsin;
DE AltName: Full=Medium wavelength-sensitive cone opsin;
GN Name=OPN1MW; Synonyms=GCP;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10511567; DOI=10.1093/genetics/153.2.919;
RA Yokoyama S., Radlwimmer F.B.;
RT "The molecular genetics of red and green color vision in mammals.";
RL Genetics 153:919-932(1999).
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. May increase spectral sensitivity in dim light.
CC -!- SUBUNIT: Monomer. Homodimer. Homotetramer.
CC {ECO:0000250|UniProtKB:P04001}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in cone photoreceptor cells.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:O35599}.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region. {ECO:0000250}.
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; AF132042; AAD30523.1; -; mRNA.
DR RefSeq; NP_001166460.1; NM_001172989.1.
DR AlphaFoldDB; Q9R024; -.
DR SMR; Q9R024; -.
DR STRING; 10141.ENSCPOP00000010067; -.
DR GeneID; 100135586; -.
DR KEGG; cpoc:100135586; -.
DR CTD; 2652; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; Q9R024; -.
DR OMA; EWGKQSF; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
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; IPR000378; Opsin_red/grn.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00575; OPSINREDGRN.
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 2: Evidence at transcript level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..364
FT /note="Medium-wave-sensitive opsin 1"
FT /id="PRO_0000197784"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT TRANSMEM 53..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..89
FT /note="Cytoplasmic"
FT TRANSMEM 90..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..129
FT /note="Extracellular"
FT TRANSMEM 130..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..168
FT /note="Cytoplasmic"
FT TRANSMEM 169..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..218
FT /note="Extracellular"
FT TRANSMEM 219..246
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..268
FT /note="Cytoplasmic"
FT TRANSMEM 269..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..300
FT /note="Extracellular"
FT TRANSMEM 301..325
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..364
FT /note="Cytoplasmic"
FT REGION 17..43
FT /note="Required for 11-cis-retinal regeneration"
FT /evidence="ECO:0000250|UniProtKB:P04001"
FT MOD_RES 312
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 126..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 364 AA; 40526 MW; A6373641C208782B CRC64;
MAQRWGPHAL SGVQAQDAYE DSTQASLFTY TNSNNTRGPF EGPNYHIAPR WVYHLTSAWM
TIVVIASIFT NGLVLVATMR FKKLRHPLNW ILVNLAVADL AETVIASTIS VVNQVYGYFV
LGHPLCVVEG YTVSLCGITG LWSLAIISWE RWLVVCKPFG NVRFDAKLAI VGIVFSWVWS
AVWTAPPIFG WSRYWPYGLK TSCGPDVFSG TSYPGVQSYM MVLMVTCCIT PLSIIVLCYL
HVWLAIRAVA KQQKESESTQ KAEKEVTRMV VVMVLAYCLC WGPYAFFACF ATANPGYSFH
PLVAALPAYF AKSATIYNPI IYVFMNRQFR NCILQLFGKK VEDSSELSST SRTEASSVSS
VSPA
