ID   BACH_HALAR              Reviewed;         131 AA.
AC   Q53461;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cruxhalorhodopsin-1;
DE            Short=CHR-1;
DE   Flags: Fragment;
GN   Name=choP1;
OS   Haloarcula argentinensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=43776;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 chloride pump.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; Q53461; -.
DR   SMR; Q53461; -.
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; PS00327; BACTERIAL_OPSIN_RET; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Chloride; Chromophore; Ion transport; Membrane;
KW   Photoreceptor protein; Receptor; Retinal protein; Sensory transduction;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           <1..>131
FT                   /note="Cruxhalorhodopsin-1"
FT                   /id="PRO_0000196267"
FT   TRANSMEM        <1..11
FT                   /note="Helical; Name=Helix C"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        12..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        15..38
FT                   /note="Helical; Name=Helix D"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        39..41
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        42..64
FT                   /note="Helical; Name=Helix E"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        65..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        77..100
FT                   /note="Helical; Name=Helix F"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        101..109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        110..>131
FT                   /note="Helical; Name=Helix G"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         125
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         131
SQ   SEQUENCE   131 AA;  13951 MW;  0958F574A9EE39AE CRC64;
     PMILLALGLL ADTDIASLFT AITMDIGMCV TGLAAALITS SHLLRWVFYG ISCAFFVAVL
     YVLLVQWPAD AEAAGTSEIF GTLKILTVVL WLGYPILWAL GSEGVALLSV GVTSWGYSGL
     DILAKYVFAF I