BAC3_HALVA
ID BAC3_HALVA Reviewed; 236 AA.
AC Q48334;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Bacterial rhodopsin CSR3;
OS Haloarcula vallismortis (Halobacterium vallismortis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=28442;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29715 / DSM 3756 / JCM 8877 / NBRC 14741 / NCIMB 2082;
RX PubMed=8645307; DOI=10.1006/bbrc.1996.0407;
RA Kitajima T., Hirayama J., Ihara K., Sugiyama Y., Kamo N., Mukohata Y.;
RT "Novel bacterial rhodopsins from Haloarcula vallismortis.";
RL Biochem. Biophys. Res. Commun. 220:341-345(1996).
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; D83748; BAA12098.1; -; Genomic_DNA.
DR RefSeq; WP_004518499.1; NZ_FNOF01000001.1.
DR AlphaFoldDB; Q48334; -.
DR SMR; Q48334; -.
DR STRING; 28442.SAMN05443574_101276; -.
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 Retinal protein; Sensory transduction; Transmembrane; Transmembrane helix.
FT CHAIN 1..236
FT /note="Bacterial rhodopsin CSR3"
FT /id="PRO_0000196279"
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..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 236 AA; 25128 MW; 22572C3306FA5568 CRC64;
MDAVAVVYGI TAAGFAVGVA IVGYLYASLE GSEERSILAA LALIPGFAGI SYVAMAFGIG
TVTIGETTLV GFRYLDWVVT TPLLVGFVGY AAGASRRAIF GVMVADALMI LTGVGAVVAD
GTLKWVLFGV STVFHVSLFA YLYLVFPRSV PDDPQRIGLF SLLKNHIGLL WIAYPLVWLA
GPEGLGLATY VGVSITYAFL DLLAKVPYVY FFYARRQVFA TKLLRDSGEV TATPAD