BACR1_HALC1
ID BACR1_HALC1 Reviewed; 260 AA.
AC P69051; P19585;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Archaerhodopsin-1;
DE Short=AR 1;
DE Flags: Precursor;
OS Halorubrum chaoviator (strain DSM 11365 / JCM 9573 / AUS-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=335819;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2592356; DOI=10.1016/s0021-9258(19)30014-6;
RA Sugiyama Y., Maeda M., Futai M., Mukohata Y.;
RT "Isolation of a gene that encodes a new retinal protein, archaerhodopsin,
RT from Halobacterium sp. aus-1.";
RL J. Biol. Chem. 264:20859-20862(1989).
RN [2]
RP PROTEIN SEQUENCE OF 7-39.
RX PubMed=2833260; DOI=10.1016/s0006-291x(88)80509-6;
RA Mukohata Y., Sugiyama Y., Ihara K., Yoshida M.;
RT "An Australian halobacterium contains a novel proton pump retinal protein:
RT archaerhodopsin.";
RL Biochem. Biophys. Res. Commun. 151:1339-1345(1988).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 21-260.
RA Enami N., Okumua H., Kouyama T.;
RT "X-ray crystallographic studies of archaerhodopsin.";
RL J. Photosci. 9:320-322(2002).
CC -!- FUNCTION: Light-driven proton pump. It may interact with
CC bacterioruberin in the claret membrane.
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; J05165; AAA72220.1; -; Genomic_DNA.
DR PIR; A34178; A34178.
DR PDB; 1UAZ; X-ray; 3.40 A; A/B=7-260.
DR PDBsum; 1UAZ; -.
DR AlphaFoldDB; P69051; -.
DR SMR; P69051; -.
DR EvolutionaryTrace; P69051; -.
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; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Photoreceptor protein;
KW Receptor; Retinal protein; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..6
FT /evidence="ECO:0000269|PubMed:2833260"
FT /id="PRO_0000020248"
FT CHAIN 7..260
FT /note="Archaerhodopsin-1"
FT /id="PRO_0000020249"
FT TOPO_DOM 7..20
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 21..42
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 43..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 52..73
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 74..91
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 92..113
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 114..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..139
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..143
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 144..172
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 173..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 177..204
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 205..212
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 213..245
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 246..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 228
FT /note="N6-(retinylidene)lysine"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1UAZ"
FT HELIX 22..43
FT /evidence="ECO:0007829|PDB:1UAZ"
FT HELIX 51..74
FT /evidence="ECO:0007829|PDB:1UAZ"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1UAZ"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1UAZ"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1UAZ"
FT HELIX 93..111
FT /evidence="ECO:0007829|PDB:1UAZ"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1UAZ"
FT HELIX 117..138
FT /evidence="ECO:0007829|PDB:1UAZ"
FT HELIX 143..165
FT /evidence="ECO:0007829|PDB:1UAZ"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:1UAZ"
FT HELIX 177..203
FT /evidence="ECO:0007829|PDB:1UAZ"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:1UAZ"
FT HELIX 213..236
FT /evidence="ECO:0007829|PDB:1UAZ"
SQ SEQUENCE 260 AA; 27852 MW; 64E1277EA641EB91 CRC64;
MDPIALTAAV GADLLGDGRP ETLWLGIGTL LMLIGTFYFI VKGWGVTDKE AREYYSITIL
VPGIASAAYL SMFFGIGLTE VQVGSEMLDI YYARYADWLF TTPLLLLDLA LLAKVDRVSI
GTLVGVDALM IVTGLVGALS HTPLARYTWW LFSTICMIVV LYFLATSLRA AAKERGPEVA
STFNTLTALV LVLWTAYPIL WIIGTEGAGV VGLGIETLLF MVLDVTAKVG FGFILLRSRA
ILGDTEAPEP SAGAEASAAD
