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OPSD_TAUBU
ID   OPSD_TAUBU              Reviewed;         287 AA.
AC   O42466;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Rhodopsin;
DE   Flags: Fragment;
GN   Name=rho;
OS   Taurulus bubalis (Long-spined sea scorpion) (Cottus bubalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Cottales; Cottidae; Taurulus.
OX   NCBI_TaxID=61643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9417898; DOI=10.1006/mpev.1997.0428;
RA   Hunt D.M., Fitzgibbon J., Slobodyanyuk S.J., Bowmaker J.K., Dulai K.S.;
RT   "Molecular evolution of the cottoid fish endemic to Lake Baikal deduced
RT   from nuclear DNA evidence.";
RL   Mol. Phylogenet. Evol. 8:415-422(1997).
CC   -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC       intensity. While most salt water fish species use retinal as
CC       chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of
CC       retinal and 3-dehydroretinal (By similarity). Light-induced
CC       isomerization of 11-cis to all-trans retinal triggers a conformational
CC       change that activates signaling via G-proteins. Subsequent receptor
CC       phosphorylation mediates displacement of the bound G-protein alpha
CC       subunit by arrestin and terminates signaling (By similarity).
CC       {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100,
CC       ECO:0000250|UniProtKB:P32309}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08100}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell projection,
CC       cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P35359}.
CC       Note=Synthesized in the inner segment (IS) of rod photoreceptor cells
CC       before vectorial transport to disk membranes in the rod outer segment
CC       (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region. {ECO:0000250|UniProtKB:P02699}.
CC   -!- PTM: Contains one covalently linked retinal chromophore.
CC       {ECO:0000250|UniProtKB:P02699}.
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; U97275; AAB61729.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42466; -.
DR   SMR; O42466; -.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
DR   GO; GO:0016038; P:absorption of visible light; ISS:UniProtKB.
DR   GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
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   Pfam; PF00001; 7tm_1; 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   3: Inferred from homology;
KW   Cell projection; Chromophore; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Phosphoprotein; Photoreceptor protein;
KW   Receptor; Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN           <1..>287
FT                   /note="Rhodopsin"
FT                   /id="PRO_0000197723"
FT   TOPO_DOM        <1..5
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        6..30
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        31..42
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        43..65
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        66..79
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        80..102
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        103..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        122..142
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        143..171
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        172..193
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        194..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        222..243
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        244..255
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TRANSMEM        256..277
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        278..>287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   MOTIF           103..105
FT                   /note="'Ionic lock' involved in activated form
FT                   stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   SITE            82
FT                   /note="Plays an important role in the conformation switch
FT                   to the active conformation"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   MOD_RES         265
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
FT   NON_TER         287
SQ   SEQUENCE   287 AA;  32265 MW;  F15E2AC799C50DDB CRC64;
     VNGAAYAGLC AYMFLLILVG FPVNFLTLYV TLEHKKLRTP LNYILLNLAV ADLFMVLGGF
     TTTMYTSAHG YFVLGRLGCN VEGFFATLGG EIALWSLVVL AVERWIVVCK PISNFRFTEE
     HAIMGLGFNW VMASACAVPP LVGWSRYIPE GMQCSCGINY YTRSEGFNNE SLVMKMLICH
     FLIPLFVIFF CYGRMLCAVK EAAAAQQESE TTQRAEREVS RMVVIMVISF LVCWLPYASV
     AWYIFCNQGS EFGPVFMTLP AFFAKSASIY NPLIYICMNK HSRHCMI
 
 
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