BACH_HALHP
ID BACH_HALHP Reviewed; 276 AA.
AC Q48315;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Halorhodopsin;
DE Short=HR;
DE Flags: Precursor;
GN Name=hop;
OS Halobacterium halobium (strain port).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=33004;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 chloride pump.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=578 nm;
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 EMBL; D43766; BAA07823.1; -; Genomic_DNA.
DR PIR; T48843; T48843.
DR AlphaFoldDB; Q48315; -.
DR SMR; Q48315; -.
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_0000020240"
FT CHAIN 22..276
FT /note="Halorhodopsin"
FT /id="PRO_0000020241"
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; 29045 MW; A2D024F474E593D7 CRC64;
MTAASTTATT MLQATQSDVL QEIQSNFLLN SSIWVNIALA GVVILLFVAM GRDIESPRAK
LIWVATMLVP LVSISSYAGL ASGLTVGFLQ MPPGHALAGQ EVLSPWGRYL TWTFSTPMIL
LALGLLADTD IASLFTAITM DIGMCVTGLA AALITSSHLL RWVFYGISCA FFVAVLYVLL
VQWPADAEAA GTSEIFGTLK ILTVVLWLGY PILWALGSEG VALLSVGVTS WGYSGLDILA
KYVFAFLLLR WVAANEGAVS GSGMSIGSGG AAPADD