ID   BACH_HALHS              Reviewed;         276 AA.
AC   Q48314;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Halorhodopsin {ECO:0000303|PubMed:8541296};
DE            Short=HR {ECO:0000303|PubMed:8541296};
DE   Flags: Precursor;
GN   Name=hop {ECO:0000303|PubMed:8541296};
OS   Halobacterium halobium (strain shark).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=33005;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=shark;
RX   PubMed=8541296; DOI=10.1016/0005-2736(95)00211-1;
RA   Otomo J., Muramatsu T.;
RT   "Over-expression of a new photo-active halorhodopsin in Halobacterium
RT   salinarium.";
RL   Biochim. Biophys. Acta 1240:248-256(1995).
CC   -!- FUNCTION: Light-driven anion pump. {ECO:0000269|PubMed:8541296}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=~596 nm {ECO:0000269|PubMed:8541296};
CC         Note=The addition of chloride or nitrate, but not sulfate, at a
CC         concentration of 1000 mM leads to a shift in the absorption maximum
CC         to about 575-580 nm. {ECO:0000269|PubMed:8541296};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8541296};
CC       Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC       {ECO:0000305}.
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DR   EMBL; D43765; BAA07822.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q48314; -.
DR   SMR; Q48314; -.
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; Ion transport; Membrane; Photoreceptor protein;
KW   Receptor; Retinal protein; Sensory transduction; Transmembrane;
KW   Transmembrane helix; Transport.
FT   PROPEP          1..21
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000020242"
FT   CHAIN           22..276
FT                   /note="Halorhodopsin"
FT                   /id="PRO_0000020243"
FT   TOPO_DOM        22..25
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        26..51
FT                   /note="Helical; Name=Helix A"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        52..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        58..81
FT                   /note="Helical; Name=Helix B"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        82..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        106..127
FT                   /note="Helical; Name=Helix C"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        128..130
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        131..154
FT                   /note="Helical; Name=Helix D"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        155..157
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        158..180
FT                   /note="Helical; Name=Helix E"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        181..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        193..216
FT                   /note="Helical; Name=Helix F"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        217..225
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        226..254
FT                   /note="Helical; Name=Helix G"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        255..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         241
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  29041 MW;  A0D6C12BE96967E5 CRC64;
     MTAVSTTATT VLQATQSDVL QEIQSNFLLN SSIWVNIALA GVVILLFVAM GRDLESPRAK
     LIWVATMLVP LVSISSYAGL ASGLTVGFLQ MPPGHALAGQ EVLSPWGRYL TWTFSTPMIL
     LALGLLADTD IASLFTAITM DIGMCVTGLA AALITSSHLL RWVFYGISCA FFVAVLYVLL
     VQWPADAEAA GTSEIFGTLK ILTVVLWLGY PILWALGSEG VALLSVGVTS WGYSGLDILA
     KYVFAFLLLR WVAANEGTVS GSGMGIGSGG AAPADD