OPSG2_DANRE
ID OPSG2_DANRE Reviewed; 349 AA.
AC Q8AYM8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Green-sensitive opsin-2;
DE AltName: Full=Green cone photoreceptor pigment 2;
DE AltName: Full=Opsin RH2-2;
DE AltName: Full=Opsin-1, medium-wave-sensitive 2;
GN Name=opn1mw2; Synonyms=rh22;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=AB; TISSUE=Eye;
RX PubMed=12618404; DOI=10.1093/genetics/163.2.663;
RA Chinen A., Hamaoka T., Yamada Y., Kawamura S.;
RT "Gene duplication and spectral diversification of cone visual pigments of
RT zebrafish.";
RL Genetics 163:663-675(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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)=476 nm {ECO:0000269|PubMed:12618404};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; AB087806; BAC24130.1; -; Genomic_DNA.
DR EMBL; BC055605; AAH55605.1; -; mRNA.
DR RefSeq; NP_878311.1; NM_182891.2.
DR AlphaFoldDB; Q8AYM8; -.
DR SMR; Q8AYM8; -.
DR PaxDb; Q8AYM8; -.
DR PRIDE; Q8AYM8; -.
DR GeneID; 360151; -.
DR KEGG; dre:360151; -.
DR CTD; 728458; -.
DR ZFIN; ZDB-GENE-030728-5; opn1mw2.
DR InParanoid; Q8AYM8; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; Q8AYM8; -.
DR PRO; PR:Q8AYM8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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: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: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; 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..349
FT /note="Green-sensitive opsin-2"
FT /id="PRO_0000197776"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 328..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 198
FT /note="F -> Y (in Ref. 1; mRNA)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="E -> D (in Ref. 1; mRNA)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38706 MW; 29EF818A60935CC3 CRC64;
MNGTEGNNFY IPMSNRTGLV RSPYEYTQYY LADPWQFKAL AFYMFFLICF GLPINVLTLL
VTAQHKKLRQ PLNYILVNLA FAGTIMAFFG FTVTFYCSIN GYMALGPTGC AIEGFFATLG
GQVALWSLVV LAIERYIVVC KPMGSFKFSS NHAMAGIAFT WVMASSCAVP PLFGWSRYIP
EGMQTSCGPD YYTLNPEFNN ESYVLYMFSC HFCVPVTTIF FTYGSLVCTV KAAAAQQQES
ESTQKAEREV TRMVILMVLG FLVAWVPYAS FAAWIFFNRG AAFSAQAMAI PAFFSKASAL
FNPIIYVLLN KQFRSCMLNT LFCGKSPLGD DESSSVSTSK TEVSSVSPA
