BACS1_HALSA
ID BACS1_HALSA Reviewed; 239 AA.
AC P0DMH8; P25964; Q9HPF5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Sensory rhodopsin-1;
DE AltName: Full=Sensory rhodopsin I;
DE Short=SR-I;
GN Name=sop1; Synonyms=sopI; OrderedLocusNames=VNG_1660G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Flx5R;
RX PubMed=1465418; DOI=10.1073/pnas.89.24.11915;
RA Yao V.J., Spudich J.L.;
RT "Primary structure of an archaebacterial transducer, a methyl-accepting
RT protein associated with sensory rhodopsin I.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11915-11919(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [3]
RP SPECTROSCOPY, AND SUBCELLULAR LOCATION.
RC STRAIN=Flx5R;
RX PubMed=2036407; DOI=10.1021/bi00236a010;
RA Bosuche O., Spudich E.N., Pudich J.L., Rotschild K.J.;
RT "Conformational changes in sensory rhodopsin I: similarities and
RT differences with bacteriorhodopsin, halorhodopsin, and rhodopsin.";
RL Biochemistry 30:5395-5400(1991).
RN [4]
RP 3D-STRUCTURE MODELING.
RX PubMed=9153084; DOI=10.1093/protein/10.3.197;
RA Lin S.L., Yan B.;
RT "Three-dimensional model of sensory rhodopsin I reveals important
RT restraints between the protein and the chromophore.";
RL Protein Eng. 10:197-206(1997).
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:0000269|PubMed:2036407};
CC Multi-pass membrane protein {ECO:0000269|PubMed:2036407}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; L05603; AAA72316.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19914.1; -; Genomic_DNA.
DR PIR; F84318; F84318.
DR PIR; S09277; S09277.
DR RefSeq; WP_010903211.1; NC_002607.1.
DR AlphaFoldDB; P0DMH8; -.
DR SMR; P0DMH8; -.
DR STRING; 64091.VNG_1660G; -.
DR PaxDb; P0DMH8; -.
DR EnsemblBacteria; AAG19914; AAG19914; VNG_1660G.
DR GeneID; 5953902; -.
DR KEGG; hal:VNG_1660G; -.
DR PATRIC; fig|64091.14.peg.1265; -.
DR HOGENOM; CLU_054785_5_1_2; -.
DR OMA; SIMIMYM; -.
DR OrthoDB; 76330at2157; -.
DR PhylomeDB; P0DMH8; -.
DR Proteomes; UP000000554; Chromosome.
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 Reference proteome; Retinal protein; Sensory transduction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..239
FT /note="Sensory rhodopsin-1"
FT /id="PRO_0000196276"
FT TOPO_DOM 1..3
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 4..25
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 26..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 35..56
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 57..70
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..92
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 93..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 96..118
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..122
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..150
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 151..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 154..181
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 182..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..222
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="N6-(retinylidene)lysine"
SQ SEQUENCE 239 AA; 25501 MW; 2496161B60425DE3 CRC64;
MDAVATAYLG GAVALIVGVA FVWLLYRSLD GSPHQSALAP LAIIPVFAGL SYVGMAYDIG
TVIVNGNQIV GLRYIDWLVT TPILVGYVGY AAGASRRSII GVMVADALMI AVGAGAVVTD
GTLKWALFGV SSIFHLSLFA YLYVIFPRVV PDVPEQIGLF NLLKNHIGLL WLAYPLVWLF
GPAGIGEATA AGVALTYVFL DVLAKVPYVY FFYARRRVFM HSESPPAPEQ ATVEATAAD
