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BACR_HALAR
ID   BACR_HALAR              Reviewed;         250 AA.
AC   Q57101;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cruxrhodopsin-1;
DE            Short=COP-1;
DE            Short=CR-1;
GN   Name=cop1;
OS   Haloarcula argentinensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=43776;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX   PubMed=7979388; DOI=10.1006/abbi.1994.1480;
RA   Tateno M., Ihara K., Mukohata Y.;
RT   "The novel ion pump rhodopsins from Haloarcula form a family independent
RT   from both the bacteriorhodopsin and archaerhodopsin families/tribes.";
RL   Arch. Biochem. Biophys. 315:127-132(1994).
CC   -!- FUNCTION: Light-driven proton pump. {ECO:0000250|UniProtKB:Q53496}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P02945}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P02945};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P02945}.
CC   -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC       {ECO:0000305}.
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DR   EMBL; D31880; BAA06678.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q57101; -.
DR   SMR; Q57101; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001425; Arc/bac/fun_rhodopsins.
DR   InterPro; IPR018229; Rhodopsin_retinal_BS.
DR   PANTHER; PTHR28286; PTHR28286; 1.
DR   Pfam; PF01036; Bac_rhodopsin; 1.
DR   PRINTS; PR00251; BACTRLOPSIN.
DR   SMART; SM01021; Bac_rhodopsin; 1.
DR   PROSITE; PS00950; BACTERIAL_OPSIN_1; 1.
DR   PROSITE; PS00327; BACTERIAL_OPSIN_RET; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Chromophore; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Photoreceptor protein;
KW   Receptor; Retinal protein; Sensory transduction; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..250
FT                   /note="Cruxrhodopsin-1"
FT                   /id="PRO_0000196273"
FT   TOPO_DOM        1..9
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        10..27
FT                   /note="Helical; Name=Helix A"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        28..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        42..60
FT                   /note="Helical; Name=Helix B"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        61..77
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        78..94
FT                   /note="Helical; Name=Helix C"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        95..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        106..125
FT                   /note="Helical; Name=Helix D"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        126..138
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        139..158
FT                   /note="Helical; Name=Helix E"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        159..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        177..195
FT                   /note="Helical; Name=Helix F"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        196..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        208..227
FT                   /note="Helical; Name=Helix G"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        228..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   SITE            83
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   MOD_RES         220
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
SQ   SEQUENCE   250 AA;  27010 MW;  C415FA3AB6606021 CRC64;
     MPEPGSEAIW LWLGTAGMFL GMLYFIARGW GETDSRRQKF YIATILITAI AFVNYLAMAL
     GFGLTIVEFA GEEHPIYWAR YSDWLFTTPL LLYDLGLLAG ADRNTITSLV SLDVLMIGTG
     LVATLSPGSG VLSAGAERLV WWGISTAFLL VLLYFLFSSL SGRVADLPSD TRSTFKTLRN
     LVTVVWLVYP VWWLIGTEGI GLVGIGIETA GFMVIDLTAK VGFGIILLRS HGVLDGAAET
     TGTGATPADD
 
 
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