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