ID   BACR_HALSR              Reviewed;         255 AA.
AC   Q53496;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cruxrhodopsin-2;
DE            Short=COP-2;
DE            Short=CR-2;
GN   Name=cop2;
OS   Haloarcula sp. (strain arg-2 / Andes heights).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula; unclassified Haloarcula.
OX   NCBI_TaxID=69009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 47-67, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=7803445; DOI=10.1016/0005-2728(94)90047-7;
RA   Sugiyama Y., Yamada N., Mukohata Y.;
RT   "The light-driven proton pump, cruxrhodopsin-2 in Haloarcula sp. arg-2
RT   (bR+, hR-), and its coupled ATP formation.";
RL   Biochim. Biophys. Acta 1188:287-292(1994).
CC   -!- FUNCTION: Light-driven proton pump. May generate a protonmotive force
CC       sufficient to synthesize ATP in the light.
CC       {ECO:0000269|PubMed:7803445}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P02945}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:7803445};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P02945}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7803445}.
CC   -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC       {ECO:0000305}.
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DR   EMBL; S76743; AAB32951.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53496; -.
DR   SMR; Q53496; -.
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; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Photoreceptor protein;
KW   Receptor; Retinal protein; Sensory transduction; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..255
FT                   /note="Cruxrhodopsin-2"
FT                   /id="PRO_0000196274"
FT   TOPO_DOM        1..16
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        17..34
FT                   /note="Helical; Name=Helix A"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        35..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        49..67
FT                   /note="Helical; Name=Helix B"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        68..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        85..101
FT                   /note="Helical; Name=Helix C"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        102..112
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        113..132
FT                   /note="Helical; Name=Helix D"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        133..145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        146..165
FT                   /note="Helical; Name=Helix E"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        166..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        184..202
FT                   /note="Helical; Name=Helix F"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        203..214
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TRANSMEM        215..234
FT                   /note="Helical; Name=Helix G"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   TOPO_DOM        235..255
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   SITE            90
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
FT   MOD_RES         227
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02945"
SQ   SEQUENCE   255 AA;  27545 MW;  E665DDE946475708 CRC64;
     MLQSGMSTYV PGGESIFLWV GTAGMFLGML YFIARGWSVS DQRRQKFYIA TIMIAAIAFV
     NYLSMALGFG VTTIELGGEE RAIYWARYTD WLFTTPLLLY DLALLAGADR NTIYSLVGLD
     VLMIGTGALA TLSAGSGVLP AGAERLVWWG ISTGFLLVLL YFLFSNLTDR ASELSGDLQS
     KFSTLRNLVL VLWLVYPVLW LVGTEGLGLV GLPIETAAFM VLDLTAKIGF GIILLQSHAV
     LDEGQTASEG AAVAD