BACH_HALSD
ID BACH_HALSD Reviewed; 282 AA.
AC O93742;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Halorhodopsin;
DE Short=HR;
GN Name=hop;
OS Halorubrum sodomense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=35743;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9878396; DOI=10.1006/jmbi.1998.2286;
RA Ihara K., Umemura T., Katagiri I., Kitajima-Ihara T., Sugiyama Y.,
RA Kimura Y., Mukohata Y.;
RT "Evolution of the archaeal rhodopsins: evolution rate changes by gene
RT duplication and functional differentiation.";
RL J. Mol. Biol. 285:163-174(1999).
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 EMBL; AB009622; BAA75202.1; -; Genomic_DNA.
DR PIR; T43840; T43840.
DR AlphaFoldDB; O93742; -.
DR SMR; O93742; -.
DR STRING; 35743.SAMN04487937_1656; -.
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 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..282
FT /note="Halorhodopsin"
FT /id="PRO_0000196263"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 30..55
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 56..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 62..85
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 86..109
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..131
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 132..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..158
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 159..161
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 162..184
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 185..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 197..220
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 221..229
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 230..258
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 259..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 245
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 282 AA; 30143 MW; 2CAC4CE98217A3AF CRC64;
MMETAADALA SGTVPLEMTQ TQIFEAIQGD TLLASSLWIN IALAGLSILL FVYMGRNLED
PRAQLIFVAT LMVPLVSISS YTGLVSGLTV SFLEMPAGHA LAGQEVLTPW GRYLTWALST
PMILVALGLL AGSNATKLFT AVTADIGMCV TGLAAALTTS SYLLRWVWYV ISCAFFVVVL
YVLLAEWAED AEVAGTAEIF NTLKLLTVVL WLGYPIFWAL GAEGLAVLDV AVTSWAYSGM
DIVAKYLFAF LLLRWVVDNE RTVAGMAAGL GAPLARCAPA DD
