ID   BACS2_HALVA             Reviewed;         236 AA.
AC   P42197;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Sensory rhodopsin-2;
DE   AltName: Full=Sensory rhodopsin II;
DE            Short=SR-II;
GN   Name=sop2; Synonyms=sopII;
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=7708770; DOI=10.1073/pnas.92.7.3036;
RA   Seidel R., Scharf B., Gautel M., Kleine K., Oesterhelt D., Engelhard M.;
RT   "The primary structure of sensory rhodopsin II: a member of an additional
RT   retinal protein subgroup is coexpressed with its transducer, the
RT   halobacterial transducer of rhodopsin II.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3036-3040(1995).
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; Z35308; CAA84550.1; -; Genomic_DNA.
DR   PIR; S55297; S55297.
DR   AlphaFoldDB; P42197; -.
DR   SMR; P42197; -.
DR   STRING; 28442.SAMN05443574_101538; -.
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="Sensory rhodopsin-2"
FT                   /id="PRO_0000196281"
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..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        34..55
FT                   /note="Helical; Name=Helix B"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        56..69
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        70..91
FT                   /note="Helical; Name=Helix C"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        92..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        95..117
FT                   /note="Helical; Name=Helix D"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        118..121
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        122..149
FT                   /note="Helical; Name=Helix E"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        150..153
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        154..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..236
FT                   /note="Helical; Name=Helix G"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         206
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   236 AA;  25053 MW;  DCB6DC5713C150E1 CRC64;
     MATITTWFTL GLLGELLGTA VLAYGYTLVP EETRKRYLLL IAIPGIAIVA YALMALGFGS
     IQSEGHAVYV VRYVDWLLTT PLNVWFLALL AGASREDTVK LVVLQALTIV FGFAGAVTPS
     PVSYALFAVG GALFGGVIYL LYRNIAVAAK STLSDIEVSL YRTLRNFVVV LWLVYPVVWL
     LGAAGVGLMD VETATLVVVY LDVVTKVGFG VIALLAMIDL GSAGETAEEP TAVAGD