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OPSG_RAT
ID   OPSG_RAT                Reviewed;         359 AA.
AC   O35476;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 133.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
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 43-315.
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; AF054246; AAC64920.1; -; Genomic_DNA.
DR   EMBL; AF054241; AAC64920.1; JOINED; Genomic_DNA.
DR   EMBL; AF054242; AAC64920.1; JOINED; Genomic_DNA.
DR   EMBL; AF054243; AAC64920.1; JOINED; Genomic_DNA.
DR   EMBL; AF054244; AAC64920.1; JOINED; Genomic_DNA.
DR   EMBL; AF054245; AAC64920.1; JOINED; Genomic_DNA.
DR   EMBL; AF031528; AAB86946.1; -; mRNA.
DR   RefSeq; NP_446000.1; NM_053548.1.
DR   AlphaFoldDB; O35476; -.
DR   SMR; O35476; -.
DR   STRING; 10116.ENSRNOP00000053164; -.
DR   GlyGen; O35476; 1 site.
DR   PhosphoSitePlus; O35476; -.
DR   PaxDb; O35476; -.
DR   Ensembl; ENSRNOT00000083147; ENSRNOP00000072867; ENSRNOG00000051529.
DR   GeneID; 89810; -.
DR   KEGG; rno:89810; -.
DR   CTD; 2652; -.
DR   RGD; 620978; Opn1mw.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234549; -.
DR   HOGENOM; CLU_009579_3_0_1; -.
DR   InParanoid; O35476; -.
DR   OMA; EWGKQSF; -.
DR   OrthoDB; 940057at2759; -.
DR   Reactome; R-RNO-2187335; The retinoid cycle in cones (daylight vision).
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-419771; Opsins.
DR   PRO; PR:O35476; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Genevisible; O35476; RN.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0009881; F:photoreceptor activity; ISO:RGD.
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:0032467; P:positive regulation of cytokinesis; ISO:RGD.
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..359
FT                   /note="Medium-wave-sensitive opsin 1"
FT                   /id="PRO_0000197789"
FT   TOPO_DOM        1..47
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..72
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..110
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..144
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..187
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..241
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..287
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..320
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          12..38
FT                   /note="Required for 11-cis-retinal regeneration"
FT                   /evidence="ECO:0000250|UniProtKB:P04001"
FT   MOD_RES         307
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        121..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   359 AA;  40200 MW;  08D9294EE6BE8A05 CRC64;
     MAQQLTGEQT LDHYEDSTQA SIFTYTNSNS TRGPFEGPNY HIAPRWVYHL TSTWMILVVI
     ASVFTNGLVL AATMRFKKLR HPLNWILVNL AVADLAETII ASTISVVNQI YGYFVLGHPL
     CVIEGYIVSL CGITGLWSLA IISWERWLVV CKPFGNVRFD AKLATVGIVF SWVWAAVWTA
     PPIFGWSRYW PYGLKTSCGP DVFSGTSYPG VQSYMMVLMV TCCIFPLSII VLCYLQVWLA
     IRAVAKQQKE SESTQKAEKE VTRMVVVMVF AYCLCWGPYT FFACFATAHP GYAFHPLVAS
     LPSYFAKSAT IYNPIIYVFM NRQFRNCILQ LFGKKVDDSS ELSSTSKTEV SSVSSVSPA
 
 
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