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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
 
 
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