YBT1_CANGA
ID YBT1_CANGA Reviewed; 1648 AA.
AC Q6FWS5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Pleiotropic ABC efflux transporter of multiple drugs YBT1 {ECO:0000303|PubMed:20547810};
GN Name=YBT1 {ECO:0000303|PubMed:20547810}; OrderedLocusNames=CAGL0C03289g;
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 INDUCTION.
RX PubMed=16803598; DOI=10.1111/j.1365-2958.2006.05235.x;
RA Vermitsky J.P., Earhart K.D., Smith W.L., Homayouni R., Edlind T.D.,
RA Rogers P.D.;
RT "Pdr1 regulates multidrug resistance in Candida glabrata: gene disruption
RT and genome-wide expression studies.";
RL Mol. Microbiol. 61:704-722(2006).
RN [3]
RP INDUCTION, AND FUNCTION.
RX PubMed=20547810; DOI=10.1128/aac.00535-10;
RA Tsai H.F., Sammons L.R., Zhang X., Suffis S.D., Su Q., Myers T.G.,
RA Marr K.A., Bennett J.E.;
RT "Microarray and molecular analyses of the azole resistance mechanism in
RT Candida glabrata oropharyngeal isolates.";
RL Antimicrob. Agents Chemother. 54:3308-3317(2010).
RN [4]
RP INDUCTION.
RX PubMed=21321146; DOI=10.1128/aac.01271-10;
RA Ferrari S., Sanguinetti M., De Bernardis F., Torelli R., Posteraro B.,
RA Vandeputte P., Sanglard D.;
RT "Loss of mitochondrial functions associated with azole resistance in
RT Candida glabrata results in enhanced virulence in mice.";
RL Antimicrob. Agents Chemother. 55:1852-1860(2011).
RN [5]
RP INDUCTION.
RX PubMed=21193550; DOI=10.1128/ec.00073-10;
RA Caudle K.E., Barker K.S., Wiederhold N.P., Xu L., Homayouni R.,
RA Rogers P.D.;
RT "Genomewide expression profile analysis of the Candida glabrata Pdr1
RT regulon.";
RL Eukaryot. Cell 10:373-383(2011).
RN [6]
RP INDUCTION.
RX PubMed=25199772; DOI=10.1128/aac.03921-14;
RA Paul S., Bair T.B., Moye-Rowley W.S.;
RT "Identification of genomic binding sites for Candida glabrata Pdr1
RT transcription factor in wild-type and rho0 cells.";
RL Antimicrob. Agents Chemother. 58:6904-6912(2014).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter that might be involved in
CC the resistance to azoles such as fluconazole.
CC {ECO:0000269|PubMed:20547810}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Azole exposure induces expression via regulation by the
CC transcription factor PDR1 that stimulates gene expression via binding
CC to elements called pleiotropic drug response elements (PDREs)
CC (PubMed:16803598, PubMed:20547810, PubMed:21193550, PubMed:25199772).
CC Expression is highly up-regulated azole-resistant isolates
CC (PubMed:20547810, PubMed:21321146). {ECO:0000269|PubMed:16803598,
CC ECO:0000269|PubMed:20547810, ECO:0000269|PubMed:21193550,
CC ECO:0000269|PubMed:21321146, ECO:0000269|PubMed:25199772}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; CR380949; CAG58225.1; -; Genomic_DNA.
DR RefSeq; XP_445319.1; XM_445319.1.
DR AlphaFoldDB; Q6FWS5; -.
DR SMR; Q6FWS5; -.
DR STRING; 5478.XP_445319.1; -.
DR EnsemblFungi; CAG58225; CAG58225; CAGL0C03289g.
DR GeneID; 2886961; -.
DR KEGG; cgr:CAGL0C03289g; -.
DR CGD; CAL0127212; YBT1.
DR VEuPathDB; FungiDB:CAGL0C03289g; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_6_1; -.
DR InParanoid; Q6FWS5; -.
DR OMA; PWYLLNT; -.
DR Proteomes; UP000002428; Chromosome C.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0010038; P:response to metal ion; IEA:EnsemblFungi.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:EnsemblFungi.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1648
FT /note="Pleiotropic ABC efflux transporter of multiple drugs
FT YBT1"
FT /id="PRO_0000445275"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1168..1188
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1191..1211
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1282..1302
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1305..1325
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 361..674
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 706..947
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1032..1333
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1372..1622
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 741..748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1406..1413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1042
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1648 AA; 186792 MW; DB4C46AE5820475F CRC64;
MVVEAMSSCQ FWYFDDITKY GRIEVLNNYV PTTLVTISIL ILLHNFFIRF YKYDIKKETP
TPSLSLKLSS LNLSESDEEM PLTMHAQHNY GSHPSPSELN TDSSALYDRH FSINNIDSGE
VNDPTKYHLI KRNMFEKFRV VIEFVIVAFQ LLLHCYLSIE KSNLNGDLQK FHFKPHVLLW
TILFTLATLR VLNLNQNNKF VNKYSGNIWL VSFANYTVIF LAHILPFRSA LIGHVNDYGS
SQYYKSQFWL NLVLMALLLT SPIGNNLPVL YQPQQDRAPS PEPYVSLLTF FSFHWVQPFI
NKAYKNNSLS HSDLWSLKLE DYSINVMKSF LEFRNRPSMR SSRFGISLLR YFLNLFMFQW
CFTTISAFSI FVPTILLKKL LDFIEHKDKG SMNLAWFYVF GMFISRFIVA ICDHCNLFLG
RRVCVRMKSI IISEIYSKAL KRKITKQSKP ADENNENDMI KHDEVSPQEV NDTTHVNADE
ESYSSNLGSI INLMSVDAFK ISELCAYLHY FLETAIMLTV SLILLYKVIG TAAFVGILIT
IIIIPINSKL YAVVGTLQAG NLACTDKRVE KLNESFQAIR IIKYFSWEDK FKEGIMLVRE
KELALLLKRC MVWCVLAFSW FITPTLITGC TFAYSILIEK KQLTTPVAFT ALSLFTLLRD
PLDRISDMLS YLIQSKISLD RVQRFLETEE TDKYDQLTVD KNGKRLAFEN VTLRWDSDKD
SFVLRNLDIE FMTGKLNVIV GATGSGKTSI LMGLLGEMQL SEGKIIVPSL SPRHEYQSQA
GVINDSIAYC SQAAWLLNDT VRNNILFNAP FDQARYDAVV EACSLKRDFQ ILKAGDSTEI
GEKGITLSGG QKQRVSLARA LYSSAGHLLL DDCLSAVDSH TALWIYDKCI SGPLMEGRTC
ILVTHNIALT MKNADFVVMI EDGKVKEKGT PIELLAKGLL GEDENMKKSI ISRSASSASL
KGKSERSLGT TPAPVEIVQD STPVNDDGKL IEEEGKAMGF VGKEIYKWYI KMYGGWYTIV
ALASVFTAIL CLQITQAWWI RNWTVKRFSD VDESNYNLPA STFIVESRNR VLLTNEAGKK
ESENQNAGIA KFLVVYCLIG VMSSIIGSIK TFVNSLFGIR ASKLIFDSLL DRVLHARVRF
FDSTPIGRIM NRFSKDIESI DQEIPPNIQS VFYSAIEVFA TLLLISYITP AFFPVAIIIV
LGYSIVGFFY LTTSRELKRL DSISKSPIFQ HFSETLVGVT TIRAFGDEQR FIKENLSMID
QNSMPFFYLW VVNRWLSFRI DLIGALVIFS SGVFILLNIN NIDAGLAGIS LTYAISFTEA
ALWLVRQYSE LEMNMNSVER VLEYMNIEQE PLIADPANAV TPPPQWPDSG KVEVNNLSLK
YAPHLPYVIK DVTFTIEPLE KVGIVGRTGA GKSTIITALF RFLEADTGSI KLDGVNIANI
DLKRLRRSIT IIPQDPTLFA GSIRSNLDPY DEYSDEEIFT ALKRVNLVST EEMEASTSEI
QSNSSKNVNK FLNLESEIAE GGSNFSQGQR QLMCLARSLL RMPKVILLDE ATASIDYNSD
AKIQETIRQE FNNSTVLTIA HRLRSIVDYD KILVMDAGEV KEFDHPYSLL LEKKSIFYNM
CEDSGELDVL IDLAKKSFIS RLNSDSKK
