ID   OPSG_ODOVI              Reviewed;         273 AA.
AC   O18911;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Medium-wave-sensitive opsin 1;
DE   AltName: Full=Green cone photoreceptor pigment;
DE   AltName: Full=Green-sensitive opsin;
DE   Flags: Fragment;
GN   Name=OPN1MW; Synonyms=GCP;
OS   Odocoileus virginianus virginianus (Virginia white-tailed deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Odocoileinae; Odocoileus.
OX   NCBI_TaxID=9875;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
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.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=531 nm {ECO:0000269|PubMed:9580985};
CC   -!- SUBUNIT: Monomer. Homodimer. Homotetramer.
CC       {ECO:0000250|UniProtKB:P04001}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: The three color pigments are found in the cone
CC       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; AF031527; AAB86945.1; -; mRNA.
DR   AlphaFoldDB; O18911; -.
DR   SMR; O18911; -.
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   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00575; OPSINREDGRN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN           <1..>273
FT                   /note="Medium-wave-sensitive opsin 1"
FT                   /id="PRO_0000197787"
FT   TOPO_DOM        <1..5
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..30
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..42
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..68
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..82
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..102
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..145
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..171
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..199
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..245
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..253
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..273
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         265
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
FT   NON_TER         273
SQ   SEQUENCE   273 AA;  30490 MW;  F7407A2B77D28C20 CRC64;
     APRWVYHLTS AWMVFVVIAS VFTNGLVLAA TMRFKKLRHP LNWILVNLAI ADLVETIIAS
     TISVVNQMYG YFVLGHPLCV VEGYTASLCG ITGLWSLAII SWERWMVVCR PFGNVRFDAK
     LAIAGIAFSW IWAAVWTAPP IFGWSRYWPH GLKTSCGPDV FSGSSYPGVQ SYMIVLMITC
     CFIPLSVIVL CYLQVWLAIR AVAKQQKESE STQKAEKEVT RMVMVMIFAF CLCWGPYAFF
     ACFAAAHPGY AFHPLVAALP AYFAKSATIY NPI