PDR1_YEAST
ID PDR1_YEAST Reviewed; 1068 AA.
AC P12383; D6VUC4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transcription factor PDR1;
DE AltName: Full=Pleiotropic drug resistance protein 1;
GN Name=PDR1; Synonyms=AMY1, ANT1, BOR2, CYH3, NRA2, SMR2, TIL1, TPE1, TPE3;
GN OrderedLocusNames=YGL013C;
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 46191 / IL125-2B;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1882553; DOI=10.1002/yea.320070311;
RA Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.;
RT "The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and
RT ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6
RT gene, a new member of the genetic network controlling pleiotropic drug
RT resistance.";
RL Yeast 7:287-299(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930 AND SER-948, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-942 AND SER-948, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [9]
RP DOMAIN.
RX PubMed=27618436; DOI=10.1371/journal.pone.0162842;
RA Piskacek M., Havelka M., Rezacova M., Knight A.;
RT "The 9aaTAD transactivation domains: From Gal4 to p53.";
RL PLoS ONE 11:E0162842-E0162842(2016).
CC -!- FUNCTION: Positive regulator of proteins involved in permeability. PDR1
CC and PDR3 jointly control the transcription level of both SNQ2 and PDR5.
CC -!- INTERACTION:
CC P12383; P19659: GAL11; NbExp=5; IntAct=EBI-13019, EBI-7305;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: the 9aaTAD motif (residues 1054 to 1062) is a transactivation
CC domain present in a large number of yeast and animal transcription
CC factors. {ECO:0000305|PubMed:27618436}.
CC -!- MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; J03487; AAA34849.1; -; Genomic_DNA.
DR EMBL; S58126; AAD13897.2; -; Genomic_DNA.
DR EMBL; Z72535; CAA96713.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08085.1; -; Genomic_DNA.
DR PIR; S64015; S64015.
DR RefSeq; NP_011502.1; NM_001180878.1.
DR AlphaFoldDB; P12383; -.
DR SMR; P12383; -.
DR BioGRID; 33233; 226.
DR DIP; DIP-978N; -.
DR IntAct; P12383; 18.
DR MINT; P12383; -.
DR STRING; 4932.YGL013C; -.
DR iPTMnet; P12383; -.
DR MaxQB; P12383; -.
DR PaxDb; P12383; -.
DR PRIDE; P12383; -.
DR EnsemblFungi; YGL013C_mRNA; YGL013C; YGL013C.
DR GeneID; 852871; -.
DR KEGG; sce:YGL013C; -.
DR SGD; S000002981; PDR1.
DR VEuPathDB; FungiDB:YGL013C; -.
DR eggNOG; ENOG502QV4Q; Eukaryota.
DR GeneTree; ENSGT00940000176364; -.
DR HOGENOM; CLU_304446_0_0_1; -.
DR InParanoid; P12383; -.
DR OMA; HRWEFYV; -.
DR BioCyc; YEAST:G3O-30534-MON; -.
DR PHI-base; PHI:2814; -.
DR PRO; PR:P12383; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P12383; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071409; P:cellular response to cycloheximide; IMP:CAFA.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:CAFA.
DR GO; GO:2001040; P:positive regulation of cellular response to drug; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..1068
FT /note="Transcription factor PDR1"
FT /id="PRO_0000114961"
FT DNA_BIND 46..72
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1054..1062
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:27618436"
FT COMPBIAS 14..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 411
FT /note="Q -> K (in Ref. 1; AAA34849 and 2; AAD13897)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="A -> R (in Ref. 2; AAD13897)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="T -> A (in Ref. 1; AAA34849 and 2; AAD13897)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="T -> I (in Ref. 1; AAA34849 and 2; AAD13897)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="T -> S (in Ref. 1; AAA34849 and 2; AAD13897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1015..1019
FT /note="Missing (in Ref. 1; AAA34849 and 2; AAD13897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1068 AA; 121794 MW; 391BA6C52770436C CRC64;
MRGLTPKNGV HIETGPDTES SADSSNFSTG FSGKIRKPRS KVSKACDNCR KRKIKCNGKF
PCASCEIYSC ECTFSTRQGG ARIKNLHKTS LEGTTVQVKE ETDSSSTSFS NPQRCTDGPC
AVEQPTKFFE NFKLGGRSSG DNSGSDGKND DDVNRNGFYE DDSESQATLT SLQTTLKNLK
EMAHLGTHVT SAIESIELQI SDLLKRWEPK VRTKELATTK FYPNKSIETQ LMKNKYCDVV
HLTRYAAWSN NKKDQDTSSQ PLIDEIFGLY SPFQFLSLQG IGKCFQNYRS KSKCEIFPRT
AKETIYIMLR FFDVCFHHIN QGCVSIANPL ENYLQKMNLL PSTPSSISSA GSPNTAHTKS
HVALVINHLP QPFVRNITGI SNSELLSEMN NDISMFGILL KMLDMHKNSY QNFLMEITSN
PSVAKNTQSI DVLQEFIHYC QAGEALIALC YSYYNSTLYN YVDFTCDITH LEQLLYFLDL
LFWLSEIYGF EKVLNVAVHF VSRVGLSRWE FYVGLDENFA ERRRNLWWKA FYFEKTLASK
LGYPSNIDDS KINCLLPKNF RDVGFLDNRD FIENVHLVRR SEAFDNMCIS DLKYYGELAV
LQIVSHFSSS VLFNEKFTSI RNTSKPSVVR EKLLFEVLEI FNETEMKYDA IKEQTGKLFD
IAFSKDSTEL KVSREDKIMA SKFVLFYEHH FCRMVNESDN IVARLCVHRR PSILIENLKI
YLHKIYKSWT DMNKILLDFD NDYSVYRSFA HYSISCIILV SQAFSVAEFI KVNDVVNMIR
VFKRFLDIKI FSENETNEHV FNSQSFKDYT RAFSFLTIVT RIMLLAYGES SSTNLDVISK
YIDENAPDLK GIIELVLDTN SCAYRFLLEP VQKSGFHLTV SQMLKNRKFQ EPLMSNEDNK
QMKHNSGKNL NPDLPSLKTG TSCLLNGIES PQLPFNGRSA PSPVRNNSLP EFAQLPSFRS
LSVSDMINPD YAQPTNGQNN TQVQSNKPIN AQQQIPTSVQ VPFMNTNEIN NNNNNNNNNK
NNINNINNNN SNNFSATSFN LGTLDEFVNN GDLEDLYSIL WSDVYPDS
