OPSG_SCICA
ID OPSG_SCICA Reviewed; 364 AA.
AC O35478; Q9R023;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 88.
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 Sciurus carolinensis (Eastern gray squirrel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Sciurinae; Sciurini; Neosciurus.
OX NCBI_TaxID=30640;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
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)=532 nm {ECO:0000269|PubMed:10511567};
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; AF132044; AAD30525.1; -; mRNA.
DR EMBL; AF031530; AAB86948.1; -; mRNA.
DR AlphaFoldDB; O35478; -.
DR SMR; O35478; -.
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 Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein;
KW Receptor; Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..364
FT /note="Medium-wave-sensitive opsin 1"
FT /id="PRO_0000197790"
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 /evidence="ECO:0000255"
FT TRANSMEM 90..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..246
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
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"
FT DISULFID 126..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 216
FT /note="V -> M (in Ref. 2; AAB86948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 40630 MW; B6CDD9B5639F0837 CRC64;
MAQRWDPQRL AGGQPQDSHE DSTQSSIFTY TNSNATRGPF EGPNYHIAPR WVYHITSTWM
IIVVIASVFT NGLVLVATMK FKKLRHPLNW ILVNLAIADL AETVIASTIS VVNQLYGYFV
LGHPLCVVEG YTVSVCGITG LWSLAIISWE RWLVVCKPFG NMRFDAKLAI VGIAFSWIWS
AVWTAPPIFG WSRYWPYGLK TSCGPDVFSG TSYPGVQSYM MVLMVTCCII PLSIIILCYL
QVWLAIRAVA KQQKESESTQ KAEKEVTRMV VVMVFAYCLC WGPYTFFACF ATANPGYAFH
PLVAALPAYF AKSATIYNPI IYVFMNRQFR NCILQLFGKK VDDTSELSSA SKTEASSVSS
VSPA
