OPSG_RABIT
ID OPSG_RABIT Reviewed; 364 AA.
AC O18910; O62769;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 119.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9751808; DOI=10.1016/s0378-1119(98)00359-x;
RA Radlwimmer F.B., Yokoyama S.;
RT "Genetic analyses of the green visual pigments of rabbit (Oryctolagus
RT cuniculus) and rat (Rattus norvegicus).";
RL Gene 218:103-109(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-320.
RX PubMed=9580985; DOI=10.1093/oxfordjournals.molbev.a025956;
RA Yokoyama S., Radlwimmer F.B.;
RT "The 'five-sites' rule and the evolution of red and green color vision in
RT mammals.";
RL Mol. Biol. Evol. 15:560-567(1998).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=509 nm;
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.
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; AF054240; AAC64919.1; -; Genomic_DNA.
DR EMBL; AF054235; AAC64919.1; JOINED; Genomic_DNA.
DR EMBL; AF054236; AAC64919.1; JOINED; Genomic_DNA.
DR EMBL; AF054237; AAC64919.1; JOINED; Genomic_DNA.
DR EMBL; AF054238; AAC64919.1; JOINED; Genomic_DNA.
DR EMBL; AF054239; AAC64919.1; JOINED; Genomic_DNA.
DR EMBL; AF031526; AAB86944.1; -; mRNA.
DR RefSeq; NP_001309193.1; NM_001322264.1.
DR AlphaFoldDB; O18910; -.
DR SMR; O18910; -.
DR STRING; 9986.ENSOCUP00000009859; -.
DR Ensembl; ENSOCUT00000011463; ENSOCUP00000009859; ENSOCUG00000011466.
DR GeneID; 100008674; -.
DR KEGG; ocu:100008674; -.
DR CTD; 2652; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR InParanoid; O18910; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000011466; Expressed in blood.
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 1: Evidence at protein 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_0000197788"
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 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT CONFLICT 247..248
FT /note="RT -> PA (in Ref. 2; AAB86944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 40544 MW; B61B6B0F9DA0CAD8 CRC64;
MTQPWGPQML AGGQPPESHE DSTQASIFTY TNSNSTRGPF EGPNFHIAPR WVYHLTSAWM
ILVVIASVFT NGLVLVATMR FKKLRHPLNW ILVNLAVADL AETVIASTIS VVNQFYGYFV
LGHPLCVVEG YTVSLCGITG LWSLAIISWE RWLVVCKPFG NVRFDAKLAI AGIAFSWIWA
AVWTAPPIFG WSRYWPYGLK TSCGPDVFSG TSYPGVQSYM MVLMVTCCII PLSVIVLCYL
QVWMAIRTVA KQQKESESTQ KAEKEVTRMV VVMVFAYCLC WGPYTFFACF ATAHPGYSFH
PLVAAIPSYF AKSATIYNPI IYVFMNRQFR NCILQLFGKK VEDSSELSSA SRTEASSVSS
VSPA
