OPSG_CHICK
ID OPSG_CHICK Reviewed; 355 AA.
AC P28683;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Green-sensitive opsin;
DE AltName: Full=Green cone photoreceptor pigment;
GN Name=PRA1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 342-355.
RC TISSUE=Retina;
RX PubMed=1385866; DOI=10.1073/pnas.89.13.5932;
RA Okano T., Kojima D., Fukada Y., Shichida Y., Yoshizawa T.;
RT "Primary structures of chicken cone visual pigments: vertebrate rhodopsins
RT have evolved out of cone visual pigments.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5932-5936(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1554715; DOI=10.1021/bi00128a002;
RA Wang S.Z., Adler R., Nathans J.;
RT "A visual pigment from chicken that resembles rhodopsin: amino acid
RT sequence, gene structure, and functional expression.";
RL Biochemistry 31:3309-3315(1992).
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)=508 nm;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: The color pigments are found in the cone
CC photoreceptor cells.
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; M92038; AAA48786.1; -; mRNA.
DR EMBL; M88178; AAA49036.1; -; Genomic_DNA.
DR PIR; A42347; A42347.
DR RefSeq; NP_990821.1; NM_205490.1.
DR AlphaFoldDB; P28683; -.
DR SMR; P28683; -.
DR BioGRID; 676733; 1.
DR STRING; 9031.ENSGALP00000004483; -.
DR iPTMnet; P28683; -.
DR PaxDb; P28683; -.
DR Ensembl; ENSGALT00000004492; ENSGALP00000004483; ENSGALG00000002848.
DR GeneID; 396486; -.
DR KEGG; gga:396486; -.
DR CTD; 102098196; -.
DR VEuPathDB; HostDB:geneid_396486; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P28683; -.
DR OMA; MSVPAFF; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; P28683; -.
DR TreeFam; TF324998; -.
DR PRO; PR:P28683; -.
DR Proteomes; UP000000539; Chromosome 26.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR GO; GO:0016038; P:absorption of visible light; IDA: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:0016037; P:light absorption; IDA:AgBase.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
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 Chromophore; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..355
FT /note="Green-sensitive opsin"
FT /id="PRO_0000197782"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT TRANSMEM 74..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..113
FT /note="Extracellular"
FT TRANSMEM 114..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT TRANSMEM 153..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..202
FT /note="Extracellular"
FT TRANSMEM 203..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..252
FT /note="Cytoplasmic"
FT TRANSMEM 253..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..284
FT /note="Extracellular"
FT TRANSMEM 285..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..355
FT /note="Cytoplasmic"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 355 AA; 39967 MW; D02853424542042A CRC64;
MNGTEGINFY VPMSNKTGVV RSPFEYPQYY LAEPWKYRLV CCYIFFLIST GLPINLLTLL
VTFKHKKLRQ PLNYILVNLA VADLFMACFG FTVTFYTAWN GYFVFGPVGC AVEGFFATLG
GQVALWSLVV LAIERYIVVC KPMGNFRFSA THAMMGIAFT WVMAFSCAAP PLFGWSRYMP
EGMQCSCGPD YYTHNPDYHN ESYVLYMFVI HFIIPVVVIF FSYGRLICKV REAAAQQQES
ATTQKAEKEV TRMVILMVLG FMLAWTPYAV VAFWIFTNKG ADFTATLMAV PAFFSKSSSL
YNPIIYVLMN KQFRNCMITT ICCGKNPFGD EDVSSTVSQS KTEVSSVSSS QVSPA
