BACR_HALVA
ID BACR_HALVA Reviewed; 250 AA.
AC P94854;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cruxrhodopsin-3 {ECO:0000303|PubMed:25268964, ECO:0000303|PubMed:8645307};
DE Short=COP-3;
DE Short=CR-3 {ECO:0000303|PubMed:8645307};
GN Name=cop3;
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).
RN [2] {ECO:0007744|PDB:4JR8, ECO:0007744|PDB:4L35}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL
RP AND BACTERIORUBERIN, SUBCELLULAR LOCATION, TOPOLOGY, AND SUBUNIT.
RX PubMed=25268964; DOI=10.1371/journal.pone.0108362;
RA Chan S.K., Kitajima-Ihara T., Fujii R., Gotoh T., Murakami M., Ihara K.,
RA Kouyama T.;
RT "Crystal structure of Cruxrhodopsin-3 from Haloarcula vallismortis.";
RL PLoS ONE 9:E108362-E108362(2014).
CC -!- FUNCTION: Light-driven proton pump. {ECO:0000250|UniProtKB:Q53496}.
CC -!- SUBUNIT: Homotrimer. Binds bacterioruberin in the crevice between
CC neighboring subunits. {ECO:0000269|PubMed:25268964}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25268964};
CC Multi-pass membrane protein {ECO:0000269|PubMed:25268964}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D31882; BAA06680.1; -; Genomic_DNA.
DR RefSeq; WP_074654814.1; NZ_FNOF01000001.1.
DR PDB; 4JR8; X-ray; 2.30 A; A=1-250.
DR PDB; 4L35; X-ray; 2.10 A; A=1-250.
DR PDBsum; 4JR8; -.
DR PDBsum; 4L35; -.
DR AlphaFoldDB; P94854; -.
DR SMR; P94854; -.
DR STRING; 28442.SAMN05443574_101167; -.
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 3D-structure; Cell membrane; Chromophore; Hydrogen ion transport;
KW Ion transport; Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..250
FT /note="Cruxrhodopsin-3"
FT /id="PRO_0000196275"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TRANSMEM 10..27
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TOPO_DOM 28..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TRANSMEM 42..60
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TOPO_DOM 61..77
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TRANSMEM 78..94
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TOPO_DOM 95..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TRANSMEM 106..125
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TOPO_DOM 126..138
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TRANSMEM 139..158
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TOPO_DOM 159..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TRANSMEM 177..195
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TOPO_DOM 196..207
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TRANSMEM 208..227
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000269|PubMed:25268964"
FT TOPO_DOM 228..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25268964"
FT SITE 83
FT /note="Primary proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P02945"
FT MOD_RES 220
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000269|PubMed:25268964,
FT ECO:0007744|PDB:4JR8, ECO:0007744|PDB:4L35"
FT HELIX 8..29
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 35..59
FT /evidence="ECO:0007829|PDB:4L35"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:4L35"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4L35"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 79..99
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 103..125
FT /evidence="ECO:0007829|PDB:4L35"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 134..158
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 169..195
FT /evidence="ECO:0007829|PDB:4L35"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 205..227
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:4L35"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4L35"
SQ SEQUENCE 250 AA; 26852 MW; B2F25512CAAE5949 CRC64;
MPAPEGEAIW LWLGTAGMFL GMLYFIARGW GETDSRRQKF YIATILITAI AFVNYLAMAL
GFGLTIVEIA GEQRPIYWAR YSDWLFTTPL LLYDLGLLAG ADRNTISSLV SLDVLMIGTG
LVATLSAGSG VLSAGAERLV WWGISTAFLL VLLYFLFSSL SGRVADLPSD TRSTFKTLRN
LVTVVWLVYP VWWLVGTEGI GLVGIGIETA GFMVIDLVAK VGFGIILLRS HGVLDGAAET
TGAGATATAD
