BACH_HALVA
ID BACH_HALVA Reviewed; 276 AA.
AC P94853;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Cruxhalorhodopsin-3;
DE Short=CHR-3;
DE Flags: Precursor;
GN Name=choP3;
OS Haloarcula vallismortis (Halobacterium vallismortis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=28442;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29715 / DSM 3756 / JCM 8877 / NBRC 14741 / NCIMB 2082;
RX PubMed=8645307; DOI=10.1006/bbrc.1996.0407;
RA Kitajima T., Hirayama J., Ihara K., Sugiyama Y., Kamo N., Mukohata Y.;
RT "Novel bacterial rhodopsins from Haloarcula vallismortis.";
RL Biochem. Biophys. Res. Commun. 220:341-345(1996).
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; D31881; BAA06679.1; -; Genomic_DNA.
DR PIR; T48842; T48842.
DR RefSeq; WP_004517017.1; NZ_FNOF01000005.1.
DR AlphaFoldDB; P94853; -.
DR SMR; P94853; -.
DR STRING; 28442.SAMN05443574_10584; -.
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 PROPEP 1..21
FT /evidence="ECO:0000250"
FT /id="PRO_0000020244"
FT CHAIN 22..276
FT /note="Cruxhalorhodopsin-3"
FT /id="PRO_0000020245"
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; 29116 MW; 9EDAB70895778BB2 CRC64;
MPAASTAATT LLQASQSEVL GEIQSNFLLN SSLWVNIALA GVVILLFVAM GRELESSRAK
LIWVATMLVP LVSISSYAGL ASGLTVGFLQ MPPGHALAGQ EVLSPWGRYL TWTFSTPMIL
LALGLLADTD MASLFTAITM DIGMCITGLA AALVTSSHLL RWVFYGISCA FFIAVLYVLL
VEWPADAEAA GTSEIFGTLK LLTVVLWLGY PILWALGSEG VALLSVGVTS WGYSGLDILA
KYVFAFLLLR WVAANEDTVT QAGMSLGSGG AAPADD