BACH_HALS4
ID BACH_HALS4 Reviewed; 297 AA.
AC O93741;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Halorhodopsin;
DE Short=HR;
GN Name=hop;
OS Haloterrigena sp. (strain arg-4).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena; unclassified Haloterrigena.
OX NCBI_TaxID=160432;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA75201.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB009621; BAA75201.2; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; O93741; -.
DR SMR; O93741; -.
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.
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..297
FT /note="Halorhodopsin"
FT /id="PRO_0000196264"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 46..71
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 72..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 78..101
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 102..125
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 126..147
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 148..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 151..174
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 175..177
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 178..200
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 201..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 213..236
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 237..246
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 247..275
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 276..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 297 AA; 32042 MW; 5F3D1BB6EDE4766C CRC64;
MRSRTYHDQS VCGPYGSQRT DCDRDTDAGS DTDVHGAQVA TQIRTDTLLH SSLWVNIALA
GLSILVFLYM ARTVRANRAR LIVGATLMIP LVSLSSYLGL VTGLTAGPIE MPAAHALAGE
DVLSQWGRYL TWTLSTPMIL LALGWLAEVD TADLFVVIAA DIGMCLTGLA AALTTSSYAF
RWAFYLVSTA FFVVVLYALL AKWPTNAEAA GTGDIFGTLR WLTVILWLGY PILWALGVEG
FALVDSVGLT SWGYSLLDIG AKYLFAALLL RWVANNERTI AVGQRSGRGA IGDPVED
