BACH_HALSS
ID BACH_HALSS Reviewed; 284 AA.
AC P33742;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Halorhodopsin;
DE Short=HR;
GN Name=hop;
OS Halobacterium sp. (strain SG1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=33006;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8478333; DOI=10.1128/jb.175.9.2720-2726.1993;
RA Soppa J., Duschl J., Oesterhelt D.;
RT "Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate
RT Halobacterium sp. strain SG1: three new members of a growing family.";
RL J. Bacteriol. 175:2720-2726(1993).
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; X70292; CAA49773.1; -; Genomic_DNA.
DR PIR; S78781; S29988.
DR AlphaFoldDB; P33742; -.
DR SMR; P33742; -.
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..284
FT /note="Halorhodopsin"
FT /id="PRO_0000196265"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 31..56
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 57..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..86
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 87..110
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..132
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 136..159
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 160..162
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 163..185
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 186..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 198..221
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 222..230
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 231..259
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 260..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 246
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 284 AA; 30256 MW; 2C659F0A69D5CA13 CRC64;
MIETAAADIL AGGMVPLEMT QTQIFEAVQS DTLLASSLWI NIALAGLSIL LFVYMGRNVE
DPRAQLIFVA TLMVPLVSIS SYTGLVSGLT VSFLEMPAGH ALAGQEVLTP WGRYLTWALS
TPMILIAVGL LAGSNTTKLF TAVVADIGMC VTGLAAALTT SSYLLRWVWY AISCAFFVVV
LYILLAEWAE DAEIAGTADI FNTLKVLTVV LWLGYPIFWA LGAEGLAVLD VAITSWAYSG
MDIVAKYLFA FLLLRWVVNN ERTVADVASG LGSGSRGGAA PADD