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Protein

Pleiotropic ABC efflux transporter of multiple drugs

Gene

PDR5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Active efflux of weakly charged organic compounds of 90 cubic Angstroms to 300 cubic Angstroms surface volume. Confers resistance to numerous chemicals including cycloheximide, sulfomethuron methyl, steroids, antiseptics, antibiotics, anticancer, herbicides, mycotoxins, insecticides, ionophores, alkaloids, flavonoids, phenothiazines, organotin compounds, carbazoles, lysosomotropic aminoesters, detergents, rhodamines and other fluorophores, azoles and other antifungals. Exhibits nucleoside triphosphatase activity.14 Publications

Enzyme regulationi

FK506, isonitrile, enniatin, RU49953, kitasatospora E420, staurosporine CGP42700, prenyl-flavonoids, D-octapeptides were found to be inhibitors in vivo. Vanadate and oligomycin were found to be inhibitors in vitro.

Kineticsi

Activity measured in plasma membranes.

  1. KM=0.5 mM for MgATP1 Publication
  1. Vmax=2.5 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi905 – 912ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • xenobiotic-transporting ATPase activity Source: SGD

GO - Biological processi

  • cellular cation homeostasis Source: SGD
  • cellular response to drug Source: GO_Central
  • drug export Source: InterPro
  • drug transport Source: SGD
  • response to antibiotic Source: UniProtKB-KW
  • response to cycloheximide Source: UniProtKB-KW
  • response to drug Source: SGD
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Cycloheximide resistance, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33670-MONOMER.

Protein family/group databases

TCDBi3.A.1.205.1. the atp-binding cassette (abc) superfamily.

Chemistry databases

SwissLipidsiSLP:000000523.

Names & Taxonomyi

Protein namesi
Recommended name:
Pleiotropic ABC efflux transporter of multiple drugs
Alternative name(s):
Pleiotropic drug resistance protein 5
Suppressor of toxicity of sporidesmin
Gene namesi
Name:PDR5
Synonyms:LEM1, STS1, YDR1
Ordered Locus Names:YOR153W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR153W.
SGDiS000005679. PDR5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 517CytoplasmicSequence analysisAdd BLAST517
Transmembranei518 – 542HelicalSequence analysisAdd BLAST25
Topological domaini543 – 558ExtracellularSequence analysisAdd BLAST16
Transmembranei559 – 579HelicalSequence analysisAdd BLAST21
Topological domaini580 – 611CytoplasmicSequence analysisAdd BLAST32
Transmembranei612 – 628HelicalSequence analysisAdd BLAST17
Topological domaini629 – 631ExtracellularSequence analysis3
Transmembranei632 – 650HelicalSequence analysisAdd BLAST19
Topological domaini651 – 665CytoplasmicSequence analysisAdd BLAST15
Transmembranei666 – 685HelicalSequence analysisAdd BLAST20
Topological domaini686 – 774ExtracellularSequence analysisAdd BLAST89
Transmembranei775 – 793HelicalSequence analysisAdd BLAST19
Topological domaini794 – 1237CytoplasmicSequence analysisAdd BLAST444
Transmembranei1238 – 1260HelicalSequence analysisAdd BLAST23
Topological domaini1261 – 1291ExtracellularSequence analysisAdd BLAST31
Transmembranei1292 – 1313HelicalSequence analysisAdd BLAST22
Topological domaini1314 – 1324CytoplasmicSequence analysisAdd BLAST11
Transmembranei1325 – 1349HelicalSequence analysisAdd BLAST25
Topological domaini1350 – 1354ExtracellularSequence analysis5
Transmembranei1355 – 1379HelicalSequence analysisAdd BLAST25
Topological domaini1380 – 1388CytoplasmicSequence analysis9
Transmembranei1389 – 1407HelicalSequence analysisAdd BLAST19
Topological domaini1408 – 1476ExtracellularSequence analysisAdd BLAST69
Transmembranei1477 – 1499HelicalSequence analysisAdd BLAST23
Topological domaini1500 – 1511CytoplasmicSequence analysisAdd BLAST12

GO - Cellular componenti

  • integral component of membrane Source: GO_Central
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Biotechnological usei

Strains lacking PDR5 are used for toxicity tests. Strains overexpressing PDR5 are used for screening antifungal sensitizers.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi183L → P: Activates ER-associated degradation. 1
Mutagenesisi257T → I: Alters drug specificity. 1
Mutagenesisi302G → D: Confers generalized drug resistance. 1
Mutagenesisi648S → F: Alters drug specificity. 1
Mutagenesisi905G → S: Inactivates drug transport. 1
Mutagenesisi908G → S: Inactivates drug transport. 1
Mutagenesisi1009G → C: Confers generalized drug resistance. 1
Mutagenesisi1040G → D: Alters drug specificity. 1
Mutagenesisi1048S → V: Alters drug specificity. 1
Mutagenesisi1289E → K: Alters drug specificity. 1
Mutagenesisi1311Y → S: Alters drug specificity. 1
Mutagenesisi1360S → F: Alters drug specificity. 1
Mutagenesisi1393T → I: Alters drug specificity. 1
Mutagenesisi1427C → Y: Activates ER-associated degradation. 1

Chemistry databases

ChEMBLiCHEMBL1697658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000934421 – 1511Pleiotropic ABC efflux transporter of multiple drugsAdd BLAST1511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22PhosphoserineCombined sources1
Modified residuei49PhosphothreonineCombined sources1
Modified residuei51PhosphothreonineCombined sources1
Modified residuei54PhosphoserineCombined sources1
Modified residuei58PhosphoserineCombined sources1
Modified residuei61PhosphoserineCombined sources1
Glycosylationi734N-linked (GlcNAc...)Sequence analysis1
Cross-linki825Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei837PhosphoserineCombined sources1
Modified residuei840PhosphoserineCombined sources1
Modified residuei841PhosphoserineCombined sources1
Modified residuei849PhosphoserineCombined sources1
Modified residuei850PhosphoserineCombined sources1
Modified residuei854PhosphoserineCombined sources1
Glycosylationi1447N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Ubiquitinylation mediates endocytosis and vacuolar degradation. Phosphorylation by casein kinase I stabilizes the protein half-life.1 Publication

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP33302.
PRIDEiP33302.

PTM databases

iPTMnetiP33302.

Expressioni

Inductioni

Expressed during exponential growth. Transcription is transiently activated within 40 min after induction by benomyl and other toxic chemicals. Multidrug resistance and PDR5 mRNA level are activated by the transcription regulators PDR1, PDR3, YAP1, YAP2, STB5 and by the mitochondrial rho zero mutation. Mutations or deletion in the PDR1 or PDR3 transcription factors strongly activate PDR5 mRNA and PDR5 translation. The transcription regulator RDR1 represses PDR5 expression.6 Publications

Interactioni

Protein-protein interaction databases

BioGridi34549. 104 interactors.
DIPiDIP-6776N.
IntActiP33302. 18 interactors.
MINTiMINT-636136.

Chemistry databases

BindingDBiP33302.

Structurei

3D structure databases

ProteinModelPortaliP33302.
SMRiP33302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini161 – 410ABC transporter 1PROSITE-ProRule annotationAdd BLAST250
Domaini869 – 1112ABC transporter 2PROSITE-ProRule annotationAdd BLAST244

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi784 – 787Poly-Phe4

Domaini

The N-terminal ABC transporter domain (positions 161 to 410) contains degenerated Walker A and B ATP-binding motifs, suggesting that it may be less efficient in ATP binding or not functional at all. This is a distinctive feature of the PDR subfamily.1 Publication
The unusual length of the two extracellular loops at positions 686 to 774 and 1408 to 1476 is another specific feature of the PDR subfamily which may have an important role for function.1 Publication

Sequence similaritiesi

Contains 2 ABC transporter domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000075308.
HOGENOMiHOG000162078.
InParanoidiP33302.
KOiK08711.
OMAiEHTEARI.
OrthoDBiEOG092C1HKF.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR013525. ABC_2_trans.
IPR029481. ABC_trans_N.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR005285. Drug-R_PDR/CDR.
IPR027417. P-loop_NTPase.
IPR010929. PDR_CDR_ABC.
[Graphical view]
PfamiPF01061. ABC2_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
PF14510. ABC_trans_N. 1 hit.
PF06422. PDR_CDR. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00956. 3a01205. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33302-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEAKLNNNV NDVTSYSSAS SSTENAADLH NYNGFDEHTE ARIQKLARTL
60 70 80 90 100
TAQSMQNSTQ SAPNKSDAQS IFSSGVEGVN PIFSDPEAPG YDPKLDPNSE
110 120 130 140 150
NFSSAAWVKN MAHLSAADPD FYKPYSLGCA WKNLSASGAS ADVAYQSTVV
160 170 180 190 200
NIPYKILKSG LRKFQRSKET NTFQILKPMD GCLNPGELLV VLGRPGSGCT
210 220 230 240 250
TLLKSISSNT HGFDLGADTK ISYSGYSGDD IKKHFRGEVV YNAEADVHLP
260 270 280 290 300
HLTVFETLVT VARLKTPQNR IKGVDRESYA NHLAEVAMAT YGLSHTRNTK
310 320 330 340 350
VGNDIVRGVS GGERKRVSIA EVSICGSKFQ CWDNATRGLD SATALEFIRA
360 370 380 390 400
LKTQADISNT SATVAIYQCS QDAYDLFNKV CVLDDGYQIY YGPADKAKKY
410 420 430 440 450
FEDMGYVCPS RQTTADFLTS VTSPSERTLN KDMLKKGIHI PQTPKEMNDY
460 470 480 490 500
WVKSPNYKEL MKEVDQRLLN DDEASREAIK EAHIAKQSKR ARPSSPYTVS
510 520 530 540 550
YMMQVKYLLI RNMWRLRNNI GFTLFMILGN CSMALILGSM FFKIMKKGDT
560 570 580 590 600
STFYFRGSAM FFAILFNAFS SLLEIFSLYE ARPITEKHRT YSLYHPSADA
610 620 630 640 650
FASVLSEIPS KLIIAVCFNI IFYFLVDFRR NGGVFFFYLL INIVAVFSMS
660 670 680 690 700
HLFRCVGSLT KTLSEAMVPA SMLLLALSMY TGFAIPKKKI LRWSKWIWYI
710 720 730 740 750
NPLAYLFESL LINEFHGIKF PCAEYVPRGP AYANISSTES VCTVVGAVPG
760 770 780 790 800
QDYVLGDDFI RGTYQYYHKD KWRGFGIGMA YVVFFFFVYL FLCEYNEGAK
810 820 830 840 850
QKGEILVFPR SIVKRMKKRG VLTEKNANDP ENVGERSDLS SDRKMLQESS
860 870 880 890 900
EEESDTYGEI GLSKSEAIFH WRNLCYEVQI KAETRRILNN VDGWVKPGTL
910 920 930 940 950
TALMGASGAG KTTLLDCLAE RVTMGVITGD ILVNGIPRDK SFPRSIGYCQ
960 970 980 990 1000
QQDLHLKTAT VRESLRFSAY LRQPAEVSIE EKNRYVEEVI KILEMEKYAD
1010 1020 1030 1040 1050
AVVGVAGEGL NVEQRKRLTI GVELTAKPKL LVFLDEPTSG LDSQTAWSIC
1060 1070 1080 1090 1100
QLMKKLANHG QAILCTIHQP SAILMQEFDR LLFMQRGGKT VYFGDLGEGC
1110 1120 1130 1140 1150
KTMIDYFESH GAHKCPADAN PAEWMLEVVG AAPGSHANQD YYEVWRNSEE
1160 1170 1180 1190 1200
YRAVQSELDW MERELPKKGS ITAAEDKHEF SQSIIYQTKL VSIRLFQQYW
1210 1220 1230 1240 1250
RSPDYLWSKF ILTIFNQLFI GFTFFKAGTS LQGLQNQMLA VFMFTVIFNP
1260 1270 1280 1290 1300
ILQQYLPSFV QQRDLYEARE RPSRTFSWIS FIFAQIFVEV PWNILAGTIA
1310 1320 1330 1340 1350
YFIYYYPIGF YSNASAAGQL HERGALFWLF SCAFYVYVGS MGLLVISFNQ
1360 1370 1380 1390 1400
VAESAANLAS LLFTMSLSFC GVMTTPSAMP RFWIFMYRVS PLTYFIQALL
1410 1420 1430 1440 1450
AVGVANVDVK CADYELLEFT PPSGMTCGQY MEPYLQLAKT GYLTDENATD
1460 1470 1480 1490 1500
TCSFCQISTT NDYLANVNSF YSERWRNYGI FICYIAFNYI AGVFFYWLAR
1510
VPKKNGKLSK K
Length:1,511
Mass (Da):170,438
Last modified:February 1, 1994 - v1
Checksum:i4540DC0BF04744BA
GO

Sequence cautioni

The sequence BAA05547 differs from that shown. Reason: Frameshift at position 61.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti171N → L in BAA05547 (PubMed:7882421).Curated1
Sequence conflicti190V → I in BAA05547 (PubMed:7882421).Curated1
Sequence conflicti214D → T in BAA05547 (PubMed:7882421).Curated1
Sequence conflicti308G → V in BAA05547 (PubMed:7882421).Curated1
Sequence conflicti340 – 345Missing in BAA05547 (PubMed:7882421).Curated6
Sequence conflicti476R → H in BAA05547 (PubMed:7882421).Curated1
Sequence conflicti648Missing in BAA05547 (PubMed:7882421).Curated1
Sequence conflicti770D → H in BAA05547 (PubMed:7882421).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26548 Genomic DNA. Translation: BAA05547.1. Frameshift.
X74113 Genomic DNA. Translation: CAA52212.1.
L19922 Genomic DNA. Translation: AAB53769.1.
U55020 Genomic DNA. Translation: AAC49639.1.
Z75061 Genomic DNA. Translation: CAA99359.1.
BK006948 Genomic DNA. Translation: DAA10926.1.
PIRiA53151.
RefSeqiNP_014796.3. NM_001183572.3.

Genome annotation databases

EnsemblFungiiYOR153W; YOR153W; YOR153W.
GeneIDi854324.
KEGGisce:YOR153W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26548 Genomic DNA. Translation: BAA05547.1. Frameshift.
X74113 Genomic DNA. Translation: CAA52212.1.
L19922 Genomic DNA. Translation: AAB53769.1.
U55020 Genomic DNA. Translation: AAC49639.1.
Z75061 Genomic DNA. Translation: CAA99359.1.
BK006948 Genomic DNA. Translation: DAA10926.1.
PIRiA53151.
RefSeqiNP_014796.3. NM_001183572.3.

3D structure databases

ProteinModelPortaliP33302.
SMRiP33302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34549. 104 interactors.
DIPiDIP-6776N.
IntActiP33302. 18 interactors.
MINTiMINT-636136.

Chemistry databases

BindingDBiP33302.
ChEMBLiCHEMBL1697658.
SwissLipidsiSLP:000000523.

Protein family/group databases

TCDBi3.A.1.205.1. the atp-binding cassette (abc) superfamily.

PTM databases

iPTMnetiP33302.

Proteomic databases

MaxQBiP33302.
PRIDEiP33302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR153W; YOR153W; YOR153W.
GeneIDi854324.
KEGGisce:YOR153W.

Organism-specific databases

EuPathDBiFungiDB:YOR153W.
SGDiS000005679. PDR5.

Phylogenomic databases

GeneTreeiENSGT00550000075308.
HOGENOMiHOG000162078.
InParanoidiP33302.
KOiK08711.
OMAiEHTEARI.
OrthoDBiEOG092C1HKF.

Enzyme and pathway databases

BioCyciYEAST:G3O-33670-MONOMER.

Miscellaneous databases

PROiP33302.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR013525. ABC_2_trans.
IPR029481. ABC_trans_N.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR005285. Drug-R_PDR/CDR.
IPR027417. P-loop_NTPase.
IPR010929. PDR_CDR_ABC.
[Graphical view]
PfamiPF01061. ABC2_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
PF14510. ABC_trans_N. 1 hit.
PF06422. PDR_CDR. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR00956. 3a01205. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDR5_YEAST
AccessioniPrimary (citable) accession number: P33302
Secondary accession number(s): D6W2L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 177 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 42000 molecules/cell in log phase SD medium in log phase SD medium.1 Publication
Full-sized PDR5 orthologs are found only in fungi and plants. Their topology and substrate specificity are distinct from mammalian MDR transporters.
This protein has been 'adopted' by Andre Goffeau from the Catholic University of Louvain (Belgium). The above-mentioned scientist has agreed to help us to curate information available on this protein. We are grateful to that person for committing precious time to help producing annotation useful to the whole community. However, that person is not responsible for any errors or omissions in this UniProtKB/Swiss-Prot entry. If you have found something wrong or missing in this entry you should submit an update report to: help@uniprot.org.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.