AQR1_CANGA
ID AQR1_CANGA Reviewed; 592 AA.
AC Q6FNQ2;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Multidrug transporter AQR1 {ECO:0000303|PubMed:23805133};
DE AltName: Full=Drug:H(+) antiporter AQR1 {ECO:0000303|PubMed:27148215};
DE Short=DHA AQR1 {ECO:0000303|PubMed:27148215};
DE AltName: Full=Flucytosine exporter AQR1 {ECO:0000303|PubMed:23805133};
GN Name=AQR1 {ECO:0000303|PubMed:23805133}; OrderedLocusNames=CAGL0J09944g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23805133; DOI=10.3389/fmicb.2013.00170;
RA Costa C., Henriques A., Pires C., Nunes J., Ohno M., Chibana H.,
RA Sa-Correia I., Teixeira M.C.;
RT "The dual role of candida glabrata drug:H+ antiporter CgAqr1 (ORF
RT CAGL0J09944g) in antifungal drug and acetic acid resistance.";
RL Front. Microbiol. 4:170-170(2013).
RN [3]
RP FUNCTION.
RX PubMed=27148215; DOI=10.3389/fmicb.2016.00526;
RA Costa C., Ribeiro J., Miranda I.M., Silva-Dias A., Cavalheiro M.,
RA Costa-de-Oliveira S., Rodrigues A.G., Teixeira M.C.;
RT "Clotrimazole drug resistance in Candida glabrata clinical isolates
RT correlates with increased expression of the drug:H(+) antiporters CgAqr1,
RT CgTpo1_1, CgTpo3, and CgQdr2.";
RL Front. Microbiol. 7:526-526(2016).
CC -!- FUNCTION: Multidrug transporter acts as a determinant of resistance to
CC acetic acid, flucytosine and clotrimazole, these 3 compounds acting
CC synergistically against the pathogen (PubMed:23805133,
CC PubMed:27148215). Reduces the intracellular accumulation of the
CC antifungal agents flucytosine and, to a moderate extent, of
CC clotrimazole (PubMed:23805133). Its role in acetic acid resistance may
CC be indirect, presumably through the transport of a still unidentified
CC physiological substrate (PubMed:23805133).
CC {ECO:0000269|PubMed:23805133, ECO:0000269|PubMed:27148215}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23805133};
CC Multi-pass membrane protein {ECO:0000255}. Note=Localizes also to
CC membrane vesicles (PubMed:23805133). {ECO:0000269|PubMed:23805133}.
CC -!- DISRUPTION PHENOTYPE: Leads to intracellular accumulation of
CC flucytosine and clotrimazole (PubMed:23805133).
CC {ECO:0000269|PubMed:23805133}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC {ECO:0000305}.
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DR EMBL; CR380956; CAG61093.1; -; Genomic_DNA.
DR RefSeq; XP_448142.1; XM_448142.1.
DR AlphaFoldDB; Q6FNQ2; -.
DR STRING; 5478.XP_448142.1; -.
DR EnsemblFungi; CAG61093; CAG61093; CAGL0J09944g.
DR GeneID; 2889427; -.
DR KEGG; cgr:CAGL0J09944g; -.
DR CGD; CAL0133042; AQR1.
DR VEuPathDB; FungiDB:CAGL0J09944g; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_8_4_1; -.
DR InParanoid; Q6FNQ2; -.
DR OMA; KYDNPDY; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0015299; F:solute:proton antiporter activity; IMP:CGD.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0032973; P:amino acid export across plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0071311; P:cellular response to acetate; IMP:CGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:CGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..592
FT /note="Multidrug transporter AQR1"
FT /id="PRO_0000443409"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 592 AA; 64860 MW; A4E401059A4622F3 CRC64;
MVESGPHSIN DDLSTNEYIE QPKFYHDDHA SDSNSLSDID DDNKKHGGLY GTVSRTTTRE
LPEDLESEIS STHSQDAKED LEIQHNAAPY SLLNYRDKWC MVALLTACGF WSSLGSPIYY
PALKQLEKQF DIDENMVNIT VVVYLLFQGL APTCSGGLAD KFGRRPVLLI GMLIYVVASI
GLACAPSYGV IVFLRCVQSI GISPSIAISS GVVGDFTVKS ERGTFVGATS GFVLLGQAFG
SLIGAALAAA WDWRAIFWFL TIGCGASFAI CFALLPETKR SIVGNLSIRP KNPLNIAPVT
LLPAARRKLK YDNPDYETLD KTKPVFDLTS AFKICALPEI FLSLLPPGLA FAMWTLMLSA
ISSELSAAPY NYKLTIIGVC YLPAGIGGLI GSFATGKIID FQYKKKLKVF EEKKAAGIIP
EDEKFNIMGA RLQSVLPQNF LCVVTYILFG WSCDKGWKIP SILITSCVSS FCAMSTLSAM
STLLVDLYPG KSSTASSCFN FMRCSLSAIL MGCFAKMKHS LTVGGTFTLL AGLVFVGNFL
MFIPMKHGMR WREEREQRAA LKAKSMDQAN ENGYKLFSKI KFSSPFKSEE KV
