BACS2_HALSA
ID BACS2_HALSA Reviewed; 237 AA.
AC P71411; Q9HP82;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sensory rhodopsin-2;
DE AltName: Full=Sensory rhodopsin II;
DE Short=SR-II;
GN Name=sop2; Synonyms=sopII; OrderedLocusNames=VNG_1764G;
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=Flx15;
RX PubMed=8710852; DOI=10.1073/pnas.93.16.8230;
RA Zhang W., Brooun A., Mueller M.M., Alam M.;
RT "The primary structures of the Archaeon Halobacterium salinarium blue light
RT receptor sensory rhodopsin II and its transducer, a methyl-accepting
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8230-8235(1996).
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).
CC -!- FUNCTION: Photophobic photoreceptor responsible for the negative
CC phototaxis. Activates the sensory rhodopsin II transducer (HTR-II) in
CC response to blue light (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HTR-II. {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; U62676; AAC44370.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19988.1; -; Genomic_DNA.
DR PIR; H84327; H84327.
DR PIR; T44947; T44947.
DR RefSeq; WP_010903286.1; NC_002607.1.
DR AlphaFoldDB; P71411; -.
DR SMR; P71411; -.
DR STRING; 64091.VNG_1764G; -.
DR TCDB; 3.E.1.3.2; the ion-translocating microbial rhodopsin (mr) family.
DR PaxDb; P71411; -.
DR EnsemblBacteria; AAG19988; AAG19988; VNG_1764G.
DR GeneID; 5953098; -.
DR KEGG; hal:VNG_1764G; -.
DR PATRIC; fig|64091.14.peg.1343; -.
DR HOGENOM; CLU_054785_5_1_2; -.
DR InParanoid; P71411; -.
DR OMA; IFHYITA; -.
DR OrthoDB; 76330at2157; -.
DR PhylomeDB; P71411; -.
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 3: Inferred from homology;
KW Cell membrane; Chromophore; Membrane; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..237
FT /note="Sensory rhodopsin-2"
FT /id="PRO_0000196280"
FT TOPO_DOM 1..2
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 3..23
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 24..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 32..53
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 54..67
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..89
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 90..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 93..115
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 116..119
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 120..147
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 148..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 151..178
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 179..186
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 187..214
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 215..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 237 AA; 25280 MW; E0EB2882D2E7D33E CRC64;
MALTTWFWVG AVGMLAGTVL PIRDCIRHPS HRRYDLVLAG ITGLAAIAYT TMGLGITATT
VGDRTVYLAR YIDWLVTTPL IVLYLAMLAR PGHRTSAWLL AADVFVIAAG IAAALTTGVQ
RWLFFAVGAA GYAALLYGLL GTLPRALGDD PRVRSLFVTL RNITVVLWTL YPVVWLLSPA
GIGILQTEMY TIVVVYLDFI SKVAFVAFAV LGADAVSRLV AADAAAPATA EPTPDGD
