BACS_HALSD
ID BACS_HALSD Reviewed; 254 AA.
AC O93743;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Sensory rhodopsin;
DE Short=SR;
GN Name=sop;
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: Involved in the control of phototaxis. {ECO:0000250}.
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; AB009623; BAA75203.1; -; Genomic_DNA.
DR PIR; T43843; T43843.
DR AlphaFoldDB; O93743; -.
DR SMR; O93743; -.
DR STRING; 35743.SAMN04487937_1712; -.
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; Membrane; Photoreceptor protein; Receptor;
KW Retinal protein; Sensory transduction; Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Sensory rhodopsin"
FT /id="PRO_0000196278"
FT TOPO_DOM 1..4
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 5..26
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 27..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 36..57
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 58..71
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 72..93
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 94..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 97..119
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 120..123
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 124..151
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 152..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..182
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 183..190
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 191..223
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 224..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 231..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="N6-(retinylidene)lysine"
SQ SEQUENCE 254 AA; 26282 MW; 92F5428824AD56D7 CRC64;
MTGAVTSAYW LAAVAFLIGV GITAALYAKL EGSRARTRLA ALAVIPGFAG LSYVGMALGI
GTVTVNGAEL VGLRYVDWVV TTPLLVGFIG YNAGASRRAI AGVMIADALM IVFGAAAVVS
GGTLKWALFG VSALFHVSLF AYLYVIFPGG IPDDPMQRGL FSLLKNHVGL LWLAYPFVWL
MGPAGIGFTG AVGAALTYAF LDVLAKVPYV YFFYARRQAF IDVTDSRAAA KGDGPAVGGE
APVATGDDAP TAAD