BACS1_HALSS
ID BACS1_HALSS Reviewed; 247 AA.
AC P33743;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sensory rhodopsin-1;
DE AltName: Full=Sensory rhodopsin I;
DE Short=SR-I;
GN Name=sop1; Synonyms=sopI;
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: Involved in the control of phototaxis. Mediates both
CC photoattractant (in the orange light) and photophobic (in the near UV
CC light) responses. The signal is then transmitted to the sensory
CC rhodopsin I transducer (HTR-I) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HTR-I. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; X70290; CAA49771.1; -; Genomic_DNA.
DR PIR; S78782; S29989.
DR AlphaFoldDB; P33743; -.
DR SMR; P33743; -.
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..247
FT /note="Sensory rhodopsin-1"
FT /id="PRO_0000196277"
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..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 206
FT /note="N6-(retinylidene)lysine"
SQ SEQUENCE 247 AA; 25748 MW; 807295627F0E6185 CRC64;
MTGAVSAAYW IAAVAFLVGL GITAALYAKL GESEDRGRLA ALAVIPGFAG LAYAGMALGI
GTVTVNGAEL VGLRYVDWIV TTPLLVGFIG YVAGASRRAI AGVMLADALM IAFGAGAVVT
GGTLKWVLFG VSSIFHVTLF AYLYVVFPRA VPDDPMQRGL FSLLKNHVGL LWLAYPFVWL
MGPAGIGFTT GVGAALTYAF LDVLAKVPYV YFFYARRQAF TDVVSAATAD REDATDAVGD
GAPTAAD