PDR5_YEAST
ID PDR5_YEAST Reviewed; 1511 AA.
AC P33302; D6W2L0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Pleiotropic ABC efflux transporter of multiple drugs;
DE AltName: Full=Pleiotropic drug resistance protein 5;
DE AltName: Full=Suppressor of toxicity of sporidesmin;
GN Name=PDR5; Synonyms=LEM1, STS1, YDR1; OrderedLocusNames=YOR153W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX PubMed=7882421; DOI=10.1007/bf00310491;
RA Hirata D., Yano K., Miyahara K., Miyakawa T.;
RT "Saccharomyces cerevisiae YDR1, which encodes a member of the ATP-binding
RT cassette (ABC) superfamily, is required for multidrug resistance.";
RL Curr. Genet. 26:285-294(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, TOPOLOGY, AND
RP DOMAINS.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8294477; DOI=10.1016/s0021-9258(17)42155-7;
RA Balzi E., Wang M., Leterme S., van Dyck L., Goffeau A.;
RT "PDR5, a novel yeast multidrug resistance conferring transporter controlled
RT by the transcription regulator PDR1.";
RL J. Biol. Chem. 269:2206-2214(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=8307980; DOI=10.1016/s0021-9258(17)41760-1;
RA Bissinger P.H., Kuchler K.;
RT "Molecular cloning and expression of the Saccharomyces cerevisiae STS1 gene
RT product. A yeast ABC transporter conferring mycotoxin resistance.";
RL J. Biol. Chem. 269:4180-4186(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP TRANSCRIPTION REGULATION.
RX PubMed=3316228; DOI=10.1016/s0021-9258(18)45464-6;
RA Balzi E., Chen W., Ulaszewski S., Capieaux E., Goffeau A.;
RT "The multidrug resistance gene PDR1 from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 262:16871-16879(1987).
RN [8]
RP TRANSCRIPTION REGULATION.
RX PubMed=1319843; DOI=10.1007/bf00351651;
RA Meyers S., Schauer W., Balzi E., Wagner M., Goffeau A., Golin J.;
RT "Interaction of the yeast pleiotropic drug resistance genes PDR1 and
RT PDR5.";
RL Curr. Genet. 21:431-436(1992).
RN [9]
RP SUBSTRATES.
RX PubMed=7840595; DOI=10.1128/aac.38.10.2492;
RA Leonard P.J., Rathod P.K., Golin J.;
RT "Loss of function mutation in the yeast multiple drug resistance gene PDR5
RT causes a reduction in chloramphenicol efflux.";
RL Antimicrob. Agents Chemother. 38:2492-2494(1994).
RN [10]
RP PURIFICATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8175692; DOI=10.1016/s0021-9258(18)99946-1;
RA Decottignies A., Kolaczkowski M., Balzi E., Goffeau A.;
RT "Solubilization and characterization of the overexpressed PDR5 multidrug
RT resistance nucleotide triphosphatase of yeast.";
RL J. Biol. Chem. 269:12797-12803(1994).
RN [11]
RP TRANSCRIPTION REGULATION.
RX PubMed=8007969; DOI=10.1128/mcb.14.7.4653-4661.1994;
RA Katzmann D.J., Burnett P.E., Golin J., Mahe Y., Moye-Rowley W.S.;
RT "Transcriptional control of the yeast PDR5 gene by the PDR3 gene product.";
RL Mol. Cell. Biol. 14:4653-4661(1994).
RN [12]
RP TRANSCRIPTION REGULATION.
RX PubMed=7623800; DOI=10.1128/mcb.15.8.4043;
RA Delahodde A., Delaveau T., Jacq C.;
RT "Positive autoregulation of the yeast transcription factor Pdr3p, which is
RT involved in control of drug resistance.";
RL Mol. Cell. Biol. 15:4043-4051(1995).
RN [13]
RP DEGRADATION.
RX PubMed=7565740; DOI=10.1128/mcb.15.11.5879;
RA Egner R., Mahe Y., Pandjaitan R., Kuchler K.;
RT "Endocytosis and vacuolar degradation of the plasma membrane-localized Pdr5
RT ATP-binding cassette multidrug transporter in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 15:5879-5887(1995).
RN [14]
RP FUNCTION.
RX PubMed=7753868; DOI=10.1073/pnas.92.10.4701;
RA Kralli A., Bohen S.P., Yamamoto K.R.;
RT "LEM1, an ATP-binding-cassette transporter, selectively modulates the
RT biological potency of steroid hormones.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4701-4705(1995).
RN [15]
RP TRANSCRIPTION REGULATION.
RX PubMed=8821655; DOI=10.1007/bf02221572;
RA Miyahara K., Hirata D., Miyakawa T.;
RT "yAP-1- and yAP-2-mediated, heat shock-induced transcriptional activation
RT of the multidrug resistance ABC transporter genes in Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 29:103-105(1996).
RN [16]
RP DEGRADATION.
RX PubMed=8549828; DOI=10.1016/0014-5793(95)01450-0;
RA Egner R., Kuchler K.;
RT "The yeast multidrug transporter Pdr5 of the plasma membrane is
RT ubiquitinated prior to endocytosis and degradation in the vacuole.";
RL FEBS Lett. 378:177-181(1996).
RN [17]
RP FUNCTION.
RX PubMed=8985171; DOI=10.1016/s0014-5793(96)01353-1;
RA Miyahara K., Mizunuma M., Hirata D., Tsuchiya E., Miyakawa T.;
RT "The involvement of the Saccharomyces cerevisiae multidrug resistance
RT transporters Pdr5p and Snq2p in cation resistance.";
RL FEBS Lett. 399:317-320(1996).
RN [18]
RP INHIBITORS.
RX PubMed=8663352; DOI=10.1074/jbc.271.29.17152;
RA Kralli A., Yamamoto K.R.;
RT "An FK506-sensitive transporter selectively decreases intracellular levels
RT and potency of steroid hormones.";
RL J. Biol. Chem. 271:17152-17156(1996).
RN [19]
RP FUNCTION.
RX PubMed=8810273; DOI=10.1074/jbc.271.41.25167;
RA Mahe Y., Lemoine Y., Kuchler K.;
RT "The ATP binding cassette transporters Pdr5 and Snq2 of Saccharomyces
RT cerevisiae can mediate transport of steroids in vivo.";
RL J. Biol. Chem. 271:25167-25172(1996).
RN [20]
RP FUNCTION.
RX PubMed=8940170; DOI=10.1074/jbc.271.49.31543;
RA Kolaczkowski M., van der Rest M., Cybularz-Kolaczkowska A.,
RA Soumillion J.P., Konings W.N., Goffeau A.;
RT "Anticancer drugs, ionophoric peptides, and steroids as substrates of the
RT yeast multidrug transporter Pdr5p.";
RL J. Biol. Chem. 271:31543-31548(1996).
RN [21]
RP SUBSTRATES.
RX PubMed=9115278; DOI=10.1074/jbc.272.18.12091;
RA Reid R.J.D., Kauh E.A., Bjornsti M.-A.;
RT "Camptothecin sensitivity is mediated by the pleiotropic drug resistance
RT network in yeast.";
RL J. Biol. Chem. 272:12091-12099(1997).
RN [22]
RP TRANSCRIPTION REGULATION.
RX PubMed=9393437; DOI=10.1007/s004380050583;
RA Nourani A., Papajova D., Delahodde A., Jacq C., Subik J.;
RT "Clustered amino acid substitutions in the yeast transcription regulator
RT Pdr3p increase pleiotropic drug resistance and identify a new central
RT regulatory domain.";
RL Mol. Gen. Genet. 256:397-405(1997).
RN [23]
RP INDUCTION.
RX PubMed=9393438; DOI=10.1007/s004380050584;
RA Carvajal E., van den Hazel H.B., Cybularz-Kolaczkowska A., Balzi E.,
RA Goffeau A.;
RT "Molecular and phenotypic characterization of yeast PDR1 mutants that show
RT hyperactive transcription of various ABC multidrug transporter genes.";
RL Mol. Gen. Genet. 256:406-415(1997).
RN [24]
RP PROTEIN FAMILY.
RX PubMed=9020838; DOI=10.1038/ng0297-137;
RA Decottignies A., Goffeau A.;
RT "Complete inventory of the yeast ABC proteins.";
RL Nat. Genet. 15:137-145(1997).
RN [25]
RP SUBSTRATES.
RX PubMed=9559778; DOI=10.1128/aac.42.4.755;
RA Ogawa A., Hashida-Okado T., Endo M., Yoshioka H., Tsuruo T., Takesako K.,
RA Kato I.;
RT "Role of ABC transporters in aureobasidin A resistance.";
RL Antimicrob. Agents Chemother. 42:755-761(1998).
RN [26]
RP TRAFFICKING.
RX PubMed=9830032; DOI=10.1074/jbc.273.49.32848;
RA Plemper R.K., Egner R., Kuchler K., Wolf D.H.;
RT "Endoplasmic reticulum degradation of a mutated ATP-binding cassette
RT transporter Pdr5 proceeds in a concerted action of Sec61 and the
RT proteasome.";
RL J. Biol. Chem. 273:32848-32856(1998).
RN [27]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=9450972; DOI=10.1091/mbc.9.2.523;
RA Egner R., Rosenthal F.E., Kralli A., Sanglard D., Kuchler K.;
RT "Genetic separation of FK506 susceptibility and drug transport in the yeast
RT Pdr5 ATP-binding cassette multidrug resistance transporter.";
RL Mol. Biol. Cell 9:523-543(1998).
RN [28]
RP FUNCTION.
RX PubMed=9818966; DOI=10.1089/mdr.1998.4.143;
RA Kolaczkowski M., Kolaczowska A., Luczynski J., Witek S., Goffeau A.;
RT "In vivo characterization of the drug resistance profile of the major ABC
RT transporters and other components of the yeast pleiotropic drug resistance
RT network.";
RL Microb. Drug Resist. 4:143-158(1998).
RN [29]
RP PHOSPHORYLATION BY CK1.
RX PubMed=10601275; DOI=10.1074/jbc.274.52.37139;
RA Decottignies A., Owsianik G., Ghislain M.;
RT "Casein kinase I-dependent phosphorylation and stability of the yeast
RT multidrug transporter Pdr5p.";
RL J. Biol. Chem. 274:37139-37146(1999).
RN [30]
RP SUBSTRATES.
RX PubMed=10602734; DOI=10.1128/aac.44.1.134-138.2000;
RA Golin J., Barkatt A., Cronin S., Eng G., May L.;
RT "Chemical specificity of the PDR5 multidrug resistance gene product of
RT Saccharomyces cerevisiae based on studies with tri-n-alkyltin chlorides.";
RL Antimicrob. Agents Chemother. 44:134-138(2000).
RN [31]
RP SUBSTRATES.
RX PubMed=10639374; DOI=10.1128/aac.44.2.418-420.2000;
RA Michalkova-Papajova D., Obernauerova M., Subik J.;
RT "Role of the PDR gene network in yeast susceptibility to the antifungal
RT antibiotic mucidin.";
RL Antimicrob. Agents Chemother. 44:418-420(2000).
RN [32]
RP TOPOLOGY, AND MUTAGENESIS.
RX PubMed=10712705; DOI=10.1046/j.1365-2958.2000.01798.x;
RA Egner R., Bauer B.E., Kuchler K.;
RT "The transmembrane domain 10 of the yeast Pdr5p ABC antifungal efflux pump
RT determines both substrate specificity and inhibitor susceptibility.";
RL Mol. Microbiol. 35:1255-1263(2000).
RN [33]
RP TRANSCRIPTION REGULATION.
RX PubMed=10734226; DOI=10.1016/s0014-5793(00)01294-1;
RA DeRisi J., van den Hazel B., Marc P., Balzi E., Brown P., Jacq C.,
RA Goffeau A.;
RT "Genome microarray analysis of transcriptional activation in multidrug
RT resistance yeast mutants.";
RL FEBS Lett. 470:156-160(2000).
RN [34]
RP FUNCTION, AND INHIBITORS.
RX PubMed=10841772; DOI=10.1021/bi000040f;
RA Conseil G., Decottignies A., Jault J.-M., Comte G., Barron D., Goffeau A.,
RA Di Pietro A.;
RT "Prenyl-flavonoids as potent inhibitors of the Pdr5p multidrug ABC
RT transporter from Saccharomyces cerevisiae.";
RL Biochemistry 39:6910-6917(2000).
RN [35]
RP INHIBITORS.
RX PubMed=11327879; DOI=10.1021/bi002453m;
RA Conseil G., Perez-Victoria J.M., Jault J.-M., Gamarro F., Goffeau A.,
RA Hofmann J., Di Pietro A.;
RT "Protein kinase C effectors bind to multidrug ABC transporters and inhibit
RT their activity.";
RL Biochemistry 40:2564-2571(2001).
RN [36]
RP BIOTECHNOLOGY.
RX PubMed=11515543; DOI=10.1271/bbb.65.1589;
RA Hiraga K., Wanigasekera A., Sugi H., Hamanaka N., Oda K.;
RT "A novel screening for inhibitors of a pleiotropic drug resistant pump,
RT Pdr5, in Saccharomyces cerevisiae.";
RL Biosci. Biotechnol. Biochem. 65:1589-1595(2001).
RN [37]
RP INHIBITORS.
RX PubMed=11758940; DOI=10.1271/bbb.65.2353;
RA Wanigasekera A., Hiraga K., Hamanaka N., Oda K.;
RT "Purification and some properties of an inhibitor for a yeast pleiotropic
RT drug resistant pump from Kitasatospora sp. E-420.";
RL Biosci. Biotechnol. Biochem. 65:2353-2357(2001).
RN [38]
RP SUBSTRATES.
RX PubMed=11422371; DOI=10.1046/j.1432-1327.2001.02245.x;
RA Hu W., Feng Q., Palli S.R., Krell P.J., Arif B.M., Retnakaran A.;
RT "The ABC transporter Pdr5p mediates the efflux of nonsteroidal ecdysone
RT agonists in Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 268:3416-3422(2001).
RN [39]
RP METABOLIC REGULATION.
RX PubMed=11602584; DOI=10.1074/jbc.m106285200;
RA Zhang X., Moye-Rowley W.S.;
RT "Saccharomyces cerevisiae multidrug resistance gene expression inversely
RT correlates with the status of the F(0) component of the mitochondrial
RT ATPase.";
RL J. Biol. Chem. 276:47844-47852(2001).
RN [40]
RP FUNCTION.
RX PubMed=11321575;
RA Rogers B., Decottignies A., Kolaczkowski M., Carvajal E., Balzi E.,
RA Goffeau A.;
RT "The pleitropic drug ABC transporters from Saccharomyces cerevisiae.";
RL J. Mol. Microbiol. Biotechnol. 3:207-214(2001).
RN [41]
RP TRANSCRIPTION REGULATION.
RX PubMed=11882665; DOI=10.1074/jbc.m201637200;
RA Hellauer K., Akache B., MacPherson S., Sirard E., Turcotte B.;
RT "Zinc cluster protein Rdr1p is a transcriptional repressor of the PDR5 gene
RT encoding a multidrug transporter.";
RL J. Biol. Chem. 277:17671-17676(2002).
RN [42]
RP TRANSCRIPTION REGULATION.
RX PubMed=11943786; DOI=10.1074/jbc.m202566200;
RA Akache B., Turcotte B.;
RT "New regulators of drug sensitivity in the family of yeast zinc cluster
RT proteins.";
RL J. Biol. Chem. 277:21254-21260(2002).
RN [43]
RP SUBCELLULAR LOCATION.
RX PubMed=12469340;
RX DOI=10.1002/1615-9861(200212)2:12<1706::aid-prot1706>3.0.co;2-k;
RA Navarre C., Degand H., Bennett K.L., Crawford J.S., Moertz E., Boutry M.;
RT "Subproteomics: identification of plasma membrane proteins from the yeast
RT Saccharomyces cerevisiae.";
RL Proteomics 2:1706-1714(2002).
RN [44]
RP FUNCTION, AND INHIBITORS.
RX PubMed=12896805; DOI=10.1016/s0005-2736(03)00193-7;
RA Conseil G., Perez-Victoria J.M., Renoir J.M., Goffeau A., Di Pietro A.;
RT "Potent competitive inhibition of drug binding to the Saccharomyces
RT cerevisiae ABC exporter Pdr5p by the hydrophobic estradiol-derivative
RT RU49953.";
RL Biochim. Biophys. Acta 1614:131-134(2003).
RN [45]
RP FUNCTION, AND INHIBITORS.
RX PubMed=13678835; DOI=10.1016/s0924-8579(03)00214-0;
RA Kolaczkowski M., Michalak K., Motohashi N.;
RT "Phenothiazines as potent modulators of yeast multidrug resistance.";
RL Int. J. Antimicrob. Agents 22:279-283(2003).
RN [46]
RP SUBSTRATES.
RX PubMed=12496287; DOI=10.1074/jbc.m210908200;
RA Golin J., Ambudkar S.V., Gottesman M.M., Habib A.D., Sczepanski J.,
RA Ziccardi W., May L.;
RT "Studies with novel Pdr5p substrates demonstrate a strong size dependence
RT for xenobiotic efflux.";
RL J. Biol. Chem. 278:5963-5969(2003).
RN [47]
RP TRANSCRIPTION REGULATION.
RX PubMed=12529331; DOI=10.1074/jbc.m208549200;
RA Hikkel I., Lucau-Danila A., Delaveau T., Marc P., Devaux F., Jacq C.;
RT "A general strategy to uncover transcription factor properties identifies a
RT new regulator of drug resistance in yeast.";
RL J. Biol. Chem. 278:11427-11432(2003).
RN [48]
RP PURIFICATION, AND ELECTRON MICROSCOPY.
RX PubMed=12551908; DOI=10.1074/jbc.m212198200;
RA Ferreira-Pereira A., Marco S., Decottignies A., Nader J., Goffeau A.,
RA Rigaud J.L.;
RT "Three-dimensional reconstruction of the Saccharomyces cerevisiae multidrug
RT resistance protein Pdr5p.";
RL J. Biol. Chem. 278:11995-11999(2003).
RN [49]
RP SUBSTRATES.
RX PubMed=12754197; DOI=10.1074/jbc.m303300200;
RA Gupta S.S., Ton V.-K., Beaudry V., Rulli S., Cunningham K., Rao R.;
RT "Antifungal activity of amiodarone is mediated by disruption of calcium
RT homeostasis.";
RL J. Biol. Chem. 278:28831-28839(2003).
RN [50]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [51]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [52]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [53]
RP BIOTECHNOLOGY.
RX PubMed=14599467; DOI=10.1016/s0887-2333(03)00129-2;
RA Lichtenberg-Frate H., Schmitt M., Gellert G., Ludwig J.;
RT "A yeast-based method for the detection of cyto and genotoxicity.";
RL Toxicol. in Vitro 17:709-716(2003).
RN [54]
RP BIOTECHNOLOGY.
RX PubMed=15047528; DOI=10.1128/aac.48.4.1256-1271.2004;
RA Niimi K., Harding D.R., Parshot R., King A., Lun D.J., Decottignies A.,
RA Niimi M., Lin S., Cannon R.D., Goffeau A., Monk B.C.;
RT "Chemosensitization of fluconazole resistance in Saccharomyces cerevisiae
RT and pathogenic fungi by a D-octapeptide derivative.";
RL Antimicrob. Agents Chemother. 48:1256-1271(2004).
RN [55]
RP SUBSTRATES.
RX PubMed=15009193; DOI=10.1111/j.1432-1033.2004.04018.x;
RA Wehrschutz-Sigl E., Jungwirth H., Bergler H., Hogenauer G.;
RT "The transporters Pdr5p and Snq2p mediate diazaborine resistance and are
RT under the control of the gain-of-function allele PDR1-12.";
RL Eur. J. Biochem. 271:1145-1152(2004).
RN [56]
RP FUNCTION.
RX PubMed=14960317; DOI=10.1016/s0014-5793(04)00046-8;
RA Mamnun Y.M., Schuller C., Kuchler K.;
RT "Expression regulation of the yeast PDR5 ATP-binding cassette (ABC)
RT transporter suggests a role in cellular detoxification during the
RT exponential growth phase.";
RL FEBS Lett. 559:111-117(2004).
RN [57]
RP INDUCTION.
RX PubMed=15294907; DOI=10.1074/jbc.m406363200;
RA Gao C., Wang L., Milgrom E., Shen W.C.;
RT "On the mechanism of constitutive Pdr1 activator-mediated PDR5
RT transcription in Saccharomyces cerevisiae: evidence for enhanced
RT recruitment of coactivators and altered nucleosome structures.";
RL J. Biol. Chem. 279:42677-42686(2004).
RN [58]
RP INHIBITORS.
RX PubMed=15707993; DOI=10.1016/j.bbrc.2005.01.075;
RA Hiraga K., Yamamoto S., Fukuda H., Hamanaka N., Oda K.;
RT "Enniatin has a new function as an inhibitor of Pdr5p, one of the ABC
RT transporters in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 328:1119-1125(2005).
RN [59]
RP INHIBITORS.
RX PubMed=15796929; DOI=10.1016/j.bbrc.2005.03.009;
RA Yamamoto S., Hiraga K., Abiko A., Hamanaka N., Oda K.;
RT "A new function of isonitrile as an inhibitor of the Pdr5p multidrug ABC
RT transporter in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 330:622-628(2005).
RN [60]
RP SUBSTRATES.
RX PubMed=16008355; DOI=10.1021/bi0502994;
RA Hanson L., May L., Tuma P., Keeven J., Mehl P., Ferenz M., Ambudkar S.V.,
RA Golin J.;
RT "The role of hydrogen bond acceptor groups in the interaction of substrates
RT with Pdr5p, a major yeast drug transporter.";
RL Biochemistry 44:9703-9713(2005).
RN [61]
RP METABOLIC REGULATION.
RX PubMed=15896930; DOI=10.1016/j.gene.2005.03.019;
RA Moye-Rowley W.S.;
RT "Retrograde regulation of multidrug resistance in Saccharomyces
RT cerevisiae.";
RL Gene 354:15-21(2005).
RN [62]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=15836770; DOI=10.1111/j.1365-2443.2005.00847.x;
RA Tutulan-Cunita A.C., Mikoshi M., Mizunuma M., Hirata D., Miyakawa T.;
RT "Mutational analysis of the yeast multidrug resistance ABC transporter
RT Pdr5p with altered drug specificity.";
RL Genes Cells 10:409-420(2005).
RN [63]
RP INDUCTION.
RX PubMed=16061415; DOI=10.1016/j.biocel.2005.06.005;
RA Malac J., Urbankova E., Sigler K., Gaskova D.;
RT "Activity of yeast multidrug resistance pumps during growth is controlled
RT by carbon source and the composition of growth-depleted medium: DiS-C3(3)
RT fluorescence assay.";
RL Int. J. Biochem. Cell Biol. 37:2536-2543(2005).
RN [64]
RP SUBSTRATES.
RX PubMed=16141212; DOI=10.1074/jbc.m503147200;
RA Sano T., Kihara A., Kurotsu F., Iwaki S., Igarashi Y.;
RT "Regulation of the sphingoid long-chain base kinase Lcb4p by ergosterol and
RT heme: studies in phytosphingosine-resistant mutants.";
RL J. Biol. Chem. 280:36674-36682(2005).
RN [65]
RP INDUCTION.
RX PubMed=15713640; DOI=10.1128/mcb.25.5.1860-1868.2005;
RA Lucau-Danila A., Lelandais G., Kozovska Z., Tanty V., Delaveau T.,
RA Devaux F., Jacq C.;
RT "Early expression of yeast genes affected by chemical stress.";
RL Mol. Cell. Biol. 25:1860-1868(2005).
RN [66]
RP INDUCTION.
RX PubMed=16487346; DOI=10.1111/j.1567-1364.2006.00041.x;
RA Teixeira M.C., Fernandes A.R., Mira N.P., Becker J.D., Sa-Correia I.;
RT "Early transcriptional response of Saccharomyces cerevisiae to stress
RT imposed by the herbicide 2,4-dichlorophenoxyacetic acid.";
RL FEMS Yeast Res. 6:230-248(2006).
RN [67]
RP INDUCTION.
RX PubMed=17156010; DOI=10.1111/j.1567-1364.2006.00095.x;
RA Alenquer M., Tenreiro S., Sa-Correia I.;
RT "Adaptive response to the antimalarial drug artesunate in yeast involves
RT Pdr1p/Pdr3p-mediated transcriptional activation of the resistance
RT determinants TPO1 and PDR5.";
RL FEMS Yeast Res. 6:1130-1139(2006).
RN [68]
RP METABOLIC REGULATION, AND FUNCTION.
RX PubMed=16751665; DOI=10.1534/genetics.106.057596;
RA Souid A.K., Gao C., Wang L., Milgrom E., Shen W.C.;
RT "ELM1 is required for multidrug resistance in Saccharomyces cerevisiae.";
RL Genetics 173:1919-1937(2006).
RN [69]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [70]
RP FUNCTION.
RX PubMed=17316560; DOI=10.1016/j.bbrc.2007.02.011;
RA Golin J., Ambudkar S.V., May L.;
RT "The yeast Pdr5p multidrug transporter: how does it recognize so many
RT substrates?";
RL Biochem. Biophys. Res. Commun. 356:1-5(2007).
RN [71]
RP TRANSCRIPTION REGULATION.
RX PubMed=17158869; DOI=10.1074/jbc.m610197200;
RA Fardeau V., Lelandais G., Oldfield A., Salin H., Lemoine S., Garcia M.,
RA Tanty V., Le Crom S., Jacq C., Devaux F.;
RT "The central role of PDR1 in the foundation of yeast drug resistance.";
RL J. Biol. Chem. 282:5063-5074(2007).
RN [72]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-54; SER-61; SER-837;
RP SER-849; SER-850 AND SER-854, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [73]
RP TRAFFICKING.
RX PubMed=17302805; DOI=10.1111/j.1365-2958.2006.05562.x;
RA de Thozee C.P., Cronin S., Goj A., Golin J., Ghislain M.;
RT "Subcellular trafficking of the yeast plasma membrane ABC transporter,
RT Pdr5, is impaired by a mutation in the N-terminal nucleotide-binding
RT fold.";
RL Mol. Microbiol. 63:811-825(2007).
RN [74]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837; SER-840 AND SER-841, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [75]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837; SER-849 AND SER-850, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [76]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-51; SER-54; SER-58;
RP SER-849; SER-850 AND SER-854, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Active efflux of weakly charged organic compounds of 90 cubic
CC Angstroms to 300 cubic Angstroms surface volume. Confers resistance to
CC numerous chemicals including cycloheximide, sulfomethuron methyl,
CC steroids, antiseptics, antibiotics, anticancer, herbicides, mycotoxins,
CC insecticides, ionophores, alkaloids, flavonoids, phenothiazines,
CC organotin compounds, carbazoles, lysosomotropic aminoesters,
CC detergents, rhodamines and other fluorophores, azoles and other
CC antifungals. Exhibits nucleoside triphosphatase activity.
CC {ECO:0000269|PubMed:10841772, ECO:0000269|PubMed:11321575,
CC ECO:0000269|PubMed:12896805, ECO:0000269|PubMed:13678835,
CC ECO:0000269|PubMed:14960317, ECO:0000269|PubMed:15836770,
CC ECO:0000269|PubMed:16751665, ECO:0000269|PubMed:17316560,
CC ECO:0000269|PubMed:7753868, ECO:0000269|PubMed:8810273,
CC ECO:0000269|PubMed:8940170, ECO:0000269|PubMed:8985171,
CC ECO:0000269|PubMed:9450972, ECO:0000269|PubMed:9818966}.
CC -!- ACTIVITY REGULATION: FK506, isonitrile, enniatin, RU49953,
CC kitasatospora E420, staurosporine CGP42700, prenyl-flavonoids, D-
CC octapeptides were found to be inhibitors in vivo. Vanadate and
CC oligomycin were found to be inhibitors in vitro.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for MgATP {ECO:0000269|PubMed:8175692};
CC Vmax=2.5 umol/min/mg enzyme {ECO:0000269|PubMed:8175692};
CC Note=Activity measured in plasma membranes.;
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:8175692};
CC -!- INTERACTION:
CC P33302; Q12200: NCR1; NbExp=2; IntAct=EBI-13038, EBI-32032;
CC P33302; Q02785: PDR12; NbExp=3; IntAct=EBI-13038, EBI-13065;
CC P33302; P33302: PDR5; NbExp=4; IntAct=EBI-13038, EBI-13038;
CC P33302; P32568: SNQ2; NbExp=4; IntAct=EBI-13038, EBI-17590;
CC P33302; P40062: YER097W; NbExp=2; IntAct=EBI-13038, EBI-20799372;
CC P33302; Q08234: YOL075C; NbExp=3; IntAct=EBI-13038, EBI-29278;
CC P33302; P32804: ZRT1; NbExp=2; IntAct=EBI-13038, EBI-29677;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12469340};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12469340}. Note=The
CC ERAD mutants 'Pro-183' and 'Tyr-1427' fail to reach the plasma
CC membrane. The mutant 'Pro-183' accumulates into ER-associated
CC compartments.
CC -!- INDUCTION: Expressed during exponential growth. Transcription is
CC transiently activated within 40 min after induction by benomyl and
CC other toxic chemicals. Multidrug resistance and PDR5 mRNA level are
CC activated by the transcription regulators PDR1, PDR3, YAP1, YAP2, STB5
CC and by the mitochondrial rho zero mutation. Mutations or deletion in
CC the PDR1 or PDR3 transcription factors strongly activate PDR5 mRNA and
CC PDR5 translation. The transcription regulator RDR1 represses PDR5
CC expression. {ECO:0000269|PubMed:15294907, ECO:0000269|PubMed:15713640,
CC ECO:0000269|PubMed:16061415, ECO:0000269|PubMed:16487346,
CC ECO:0000269|PubMed:17156010, ECO:0000269|PubMed:9393438}.
CC -!- DOMAIN: The N-terminal ABC transporter domain (positions 161 to 410)
CC contains degenerated Walker A and B ATP-binding motifs, suggesting that
CC it may be less efficient in ATP binding or not functional at all. This
CC is a distinctive feature of the PDR subfamily.
CC {ECO:0000269|PubMed:8294477}.
CC -!- DOMAIN: The unusual length of the two extracellular loops at positions
CC 686 to 774 and 1408 to 1476 is another specific feature of the PDR
CC subfamily which may have an important role for function.
CC {ECO:0000269|PubMed:8294477}.
CC -!- PTM: Ubiquitinylation mediates endocytosis and vacuolar degradation.
CC Phosphorylation by casein kinase I stabilizes the protein half-life.
CC {ECO:0000269|PubMed:10601275}.
CC -!- BIOTECHNOLOGY: Strains lacking PDR5 are used for toxicity tests.
CC Strains overexpressing PDR5 are used for screening antifungal
CC sensitizers. {ECO:0000269|PubMed:11515543, ECO:0000269|PubMed:14599467,
CC ECO:0000269|PubMed:15047528}.
CC -!- MISCELLANEOUS: Present with 42000 molecules/cell in log phase SD medium
CC in log phase SD medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Full-sized PDR5 orthologs are found only in fungi and
CC plants. Their topology and substrate specificity are distinct from
CC mammalian MDR transporters.
CC -!- MISCELLANEOUS: This protein has been 'adopted' by Andre Goffeau from
CC the Catholic University of Louvain (Belgium). The above-mentioned
CC scientist has agreed to help us to curate information available on this
CC protein. We are grateful to that person for committing precious time to
CC help producing annotation useful to the whole community. However, that
CC person is not responsible for any errors or omissions in this
CC UniProtKB/Swiss-Prot entry. If you have found something wrong or
CC missing in this entry you should submit an update report to:
CC help@uniprot.org.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05547.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; D26548; BAA05547.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X74113; CAA52212.1; -; Genomic_DNA.
DR EMBL; L19922; AAB53769.1; -; Genomic_DNA.
DR EMBL; U55020; AAC49639.1; -; Genomic_DNA.
DR EMBL; Z75061; CAA99359.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10926.1; -; Genomic_DNA.
DR PIR; A53151; A53151.
DR RefSeq; NP_014796.3; NM_001183572.3.
DR PDB; 7P03; EM; 3.45 A; A=1-1511.
DR PDB; 7P04; EM; 2.85 A; A=1-1511.
DR PDB; 7P05; EM; 3.13 A; A=1-1511.
DR PDB; 7P06; EM; 3.77 A; A=1-1511.
DR PDBsum; 7P03; -.
DR PDBsum; 7P04; -.
DR PDBsum; 7P05; -.
DR PDBsum; 7P06; -.
DR AlphaFoldDB; P33302; -.
DR SMR; P33302; -.
DR BioGRID; 34549; 131.
DR DIP; DIP-6776N; -.
DR IntAct; P33302; 45.
DR MINT; P33302; -.
DR STRING; 4932.YOR153W; -.
DR BindingDB; P33302; -.
DR ChEMBL; CHEMBL1697658; -.
DR DrugCentral; P33302; -.
DR SwissLipids; SLP:000000523; -.
DR TCDB; 3.A.1.205.1; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P33302; -.
DR MaxQB; P33302; -.
DR PaxDb; P33302; -.
DR PRIDE; P33302; -.
DR EnsemblFungi; YOR153W_mRNA; YOR153W; YOR153W.
DR GeneID; 854324; -.
DR KEGG; sce:YOR153W; -.
DR SGD; S000005679; PDR5.
DR VEuPathDB; FungiDB:YOR153W; -.
DR eggNOG; KOG0065; Eukaryota.
DR GeneTree; ENSGT00940000176297; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; P33302; -.
DR OMA; IAEATLC; -.
DR BioCyc; YEAST:G3O-33670-MON; -.
DR PRO; PR:P33302; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P33302; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030003; P:cellular cation homeostasis; IMP:SGD.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0046898; P:response to cycloheximide; IEA:UniProtKB-KW.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:SGD.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR005285; Drug-R_PDR/CDR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00956; 3a01205; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cell membrane;
KW Cycloheximide resistance; Direct protein sequencing; Glycoprotein;
KW Isopeptide bond; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..1511
FT /note="Pleiotropic ABC efflux transporter of multiple
FT drugs"
FT /id="PRO_0000093442"
FT TOPO_DOM 1..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..558
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 629..631
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..685
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 686..774
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..1237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1238..1260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1261..1291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1292..1313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1314..1324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1325..1349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1350..1354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1355..1379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1380..1388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1389..1407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1408..1476
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1477..1499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1500..1511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 161..410
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 869..1112
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 905..912
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 825
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131,
FT ECO:0000269|PubMed:14557538"
FT MUTAGEN 183
FT /note="L->P: Activates ER-associated degradation."
FT MUTAGEN 257
FT /note="T->I: Alters drug specificity."
FT MUTAGEN 302
FT /note="G->D: Confers generalized drug resistance."
FT MUTAGEN 648
FT /note="S->F: Alters drug specificity."
FT MUTAGEN 905
FT /note="G->S: Inactivates drug transport."
FT MUTAGEN 908
FT /note="G->S: Inactivates drug transport."
FT MUTAGEN 1009
FT /note="G->C: Confers generalized drug resistance."
FT MUTAGEN 1040
FT /note="G->D: Alters drug specificity."
FT MUTAGEN 1048
FT /note="S->V: Alters drug specificity."
FT MUTAGEN 1289
FT /note="E->K: Alters drug specificity."
FT MUTAGEN 1311
FT /note="Y->S: Alters drug specificity."
FT MUTAGEN 1360
FT /note="S->F: Alters drug specificity."
FT MUTAGEN 1393
FT /note="T->I: Alters drug specificity."
FT MUTAGEN 1427
FT /note="C->Y: Activates ER-associated degradation."
FT CONFLICT 171
FT /note="N -> L (in Ref. 1; BAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="V -> I (in Ref. 1; BAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="D -> T (in Ref. 1; BAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="G -> V (in Ref. 1; BAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 340..345
FT /note="Missing (in Ref. 1; BAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="R -> H (in Ref. 1; BAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="Missing (in Ref. 1; BAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="D -> H (in Ref. 1; BAA05547)"
FT /evidence="ECO:0000305"
FT HELIX 37..55
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:7P05"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 311..325
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 333..338
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 341..358
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 394..404
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 414..420
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 431..435
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 455..469
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 501..518
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 520..540
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 541..544
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 553..570
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 575..590
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 591..593
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 596..606
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 608..626
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 632..659
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:7P05"
FT HELIX 663..679
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 681..685
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 687..689
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 695..700
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 702..715
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 730..732
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 752..755
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 756..763
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 768..770
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 773..795
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 810..815
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 869..882
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 885..895
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 900..904
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 906..908
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 911..918
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 924..933
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 942..944
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 946..949
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 961..972
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 975..977
FT /evidence="ECO:0007829|PDB:7P03"
FT HELIX 979..992
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 996..998
FT /evidence="ECO:0007829|PDB:7P05"
FT STRAND 1006..1010
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1012..1024
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1029..1038
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1043..1059
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1063..1066
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1072..1076
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1079..1085
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 1086..1088
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1089..1095
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1098..1100
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1101..1108
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 1109..1111
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1121..1128
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1129..1134
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1141..1146
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1149..1163
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1180..1182
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1184..1199
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1203..1223
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 1224..1226
FT /evidence="ECO:0007829|PDB:7P05"
FT HELIX 1231..1245
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1248..1268
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 1269..1274
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1278..1305
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 1306..1309
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1310..1316
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1320..1348
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1352..1368
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1370..1374
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 1376..1378
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1381..1383
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1384..1389
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1391..1404
FT /evidence="ECO:0007829|PDB:7P04"
FT TURN 1413..1415
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1416..1419
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1427..1437
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1442..1444
FT /evidence="ECO:0007829|PDB:7P04"
FT STRAND 1452..1456
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1460..1467
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1471..1473
FT /evidence="ECO:0007829|PDB:7P04"
FT HELIX 1474..1499
FT /evidence="ECO:0007829|PDB:7P04"
SQ SEQUENCE 1511 AA; 170438 MW; 4540DC0BF04744BA CRC64;
MPEAKLNNNV NDVTSYSSAS SSTENAADLH NYNGFDEHTE ARIQKLARTL TAQSMQNSTQ
SAPNKSDAQS IFSSGVEGVN PIFSDPEAPG YDPKLDPNSE NFSSAAWVKN MAHLSAADPD
FYKPYSLGCA WKNLSASGAS ADVAYQSTVV NIPYKILKSG LRKFQRSKET NTFQILKPMD
GCLNPGELLV VLGRPGSGCT TLLKSISSNT HGFDLGADTK ISYSGYSGDD IKKHFRGEVV
YNAEADVHLP HLTVFETLVT VARLKTPQNR IKGVDRESYA NHLAEVAMAT YGLSHTRNTK
VGNDIVRGVS GGERKRVSIA EVSICGSKFQ CWDNATRGLD SATALEFIRA LKTQADISNT
SATVAIYQCS QDAYDLFNKV CVLDDGYQIY YGPADKAKKY FEDMGYVCPS RQTTADFLTS
VTSPSERTLN KDMLKKGIHI PQTPKEMNDY WVKSPNYKEL MKEVDQRLLN DDEASREAIK
EAHIAKQSKR ARPSSPYTVS YMMQVKYLLI RNMWRLRNNI GFTLFMILGN CSMALILGSM
FFKIMKKGDT STFYFRGSAM FFAILFNAFS SLLEIFSLYE ARPITEKHRT YSLYHPSADA
FASVLSEIPS KLIIAVCFNI IFYFLVDFRR NGGVFFFYLL INIVAVFSMS HLFRCVGSLT
KTLSEAMVPA SMLLLALSMY TGFAIPKKKI LRWSKWIWYI NPLAYLFESL LINEFHGIKF
PCAEYVPRGP AYANISSTES VCTVVGAVPG QDYVLGDDFI RGTYQYYHKD KWRGFGIGMA
YVVFFFFVYL FLCEYNEGAK QKGEILVFPR SIVKRMKKRG VLTEKNANDP ENVGERSDLS
SDRKMLQESS EEESDTYGEI GLSKSEAIFH WRNLCYEVQI KAETRRILNN VDGWVKPGTL
TALMGASGAG KTTLLDCLAE RVTMGVITGD ILVNGIPRDK SFPRSIGYCQ QQDLHLKTAT
VRESLRFSAY LRQPAEVSIE EKNRYVEEVI KILEMEKYAD AVVGVAGEGL NVEQRKRLTI
GVELTAKPKL LVFLDEPTSG LDSQTAWSIC QLMKKLANHG QAILCTIHQP SAILMQEFDR
LLFMQRGGKT VYFGDLGEGC KTMIDYFESH GAHKCPADAN PAEWMLEVVG AAPGSHANQD
YYEVWRNSEE YRAVQSELDW MERELPKKGS ITAAEDKHEF SQSIIYQTKL VSIRLFQQYW
RSPDYLWSKF ILTIFNQLFI GFTFFKAGTS LQGLQNQMLA VFMFTVIFNP ILQQYLPSFV
QQRDLYEARE RPSRTFSWIS FIFAQIFVEV PWNILAGTIA YFIYYYPIGF YSNASAAGQL
HERGALFWLF SCAFYVYVGS MGLLVISFNQ VAESAANLAS LLFTMSLSFC GVMTTPSAMP
RFWIFMYRVS PLTYFIQALL AVGVANVDVK CADYELLEFT PPSGMTCGQY MEPYLQLAKT
GYLTDENATD TCSFCQISTT NDYLANVNSF YSERWRNYGI FICYIAFNYI AGVFFYWLAR
VPKKNGKLSK K
