QDR2_CANGA
ID QDR2_CANGA Reviewed; 583 AA.
AC Q6FSQ7;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Multidrug transporter QDR2 {ECO:0000303|PubMed:23629708};
DE AltName: Full=Clotrimazole exporter QDR2 {ECO:0000303|PubMed:23629708};
DE AltName: Full=Drug:H(+) antiporter QDR2 {ECO:0000303|PubMed:27148215};
DE Short=DHA QDR2 {ECO:0000303|PubMed:27148215};
GN Name=QDR2 {ECO:0000303|PubMed:23629708}; OrderedLocusNames=CAGL0G08624g;
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, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23629708; DOI=10.1128/aac.00811-12;
RA Costa C., Pires C., Cabrito T.R., Renaudin A., Ohno M., Chibana H.,
RA Sa-Correia I., Teixeira M.C.;
RT "Candida glabrata drug:H+ antiporter CgQdr2 confers imidazole drug
RT resistance, being activated by transcription factor CgPdr1.";
RL Antimicrob. Agents Chemother. 57:3159-3167(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 resistance transporter involved in resistance to
CC the antifungal drugs miconazole, tioconazole, clotrimazole, and
CC ketoconazole; as well as to quinidine (PubMed:23629708,
CC PubMed:27148215). Decreases the intracellular accumulation of
CC clotrimazole in and plays a role in the extrusion of this antifungal
CC from preloaded cells (PubMed:23629708, PubMed:27148215).
CC {ECO:0000269|PubMed:23629708, ECO:0000269|PubMed:27148215}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23629708};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is up-regulated by clotrimazole and quinidine
CC (PubMed:23629708). Expression is regulated by the pleiotropic drug
CC resistance transcription factor PDR1 (PubMed:23629708).
CC {ECO:0000269|PubMed:23629708}.
CC -!- DISRUPTION PHENOTYPE: Leads to intracellular accumulation of
CC clotrimazole (PubMed:23629708). {ECO:0000269|PubMed:23629708}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC {ECO:0000305}.
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DR EMBL; CR380953; CAG59664.1; -; Genomic_DNA.
DR RefSeq; XP_446737.1; XM_446737.1.
DR AlphaFoldDB; Q6FSQ7; -.
DR STRING; 5478.XP_446737.1; -.
DR TCDB; 2.A.1.2.115; the major facilitator superfamily (mfs).
DR EnsemblFungi; CAG59664; CAG59664; CAGL0G08624g.
DR GeneID; 2888131; -.
DR KEGG; cgr:CAGL0G08624g; -.
DR CGD; CAL0130703; QDR2.
DR VEuPathDB; FungiDB:CAGL0G08624g; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_8_4_1; -.
DR InParanoid; Q6FSQ7; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; 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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..583
FT /note="Multidrug transporter QDR2"
FT /id="PRO_0000443413"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 23..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 583 AA; 64364 MW; F51C5A8B0197D6C4 CRC64;
MMEDQQSLHS FISDYDQRSH AVEKYDGPDL SEVDSEDNDK MIKTNEDEAV KEPIYRTRSN
QTEPDIANAP PYSRFDAKYK MALVLQCAYT GLFSTMAGAI YYPVLSVIEK QFHITEELVN
ITVVVYFIFQ GIAPTLMGGL ADSLGRRPVV LFAVTVYFGA CIGLACAQTY AQIVVLRCLQ
AAGISPVIAI NSGIIGDVTT RAERGGYVGY ISGFQVLGSA FGALIGAGLS SRWGWRSIFW
FLAIGSGVCL VFSIIMLPET KRTIVGNGSV TPRNYLNRAP LLMFPLIRRK LHLDDPEYET
LEPRTQLSLL APLSILKVKE ISILLVTAGI QFATWSTHQT ALSTVLSKNY HLSVAKIGLC
YLPTGICTLI SIVTSGRYLN WSYRRRFAKH KVWLKEQEEI LVKENGYSRE EVQNIINNDP
KYVFNLVQTR LHAAFVTLLL SSSGFVAFGW CIDVKAPLAS VLVMSGFASL FSNCILTFST
TLIVDIFPSK TSTATGCLNL FRCLLSALFI GCLSKMATSM TYGGVFTFLG ALTALSACPL
FYLLKNGREI TLKRKRKEDA SRAFALSVAN EKAEAEGKAE ESR
