P33302 · PDR5_YEAST

Function

function

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.

Miscellaneous

Present with 42000 molecules/cell in log phase SD medium in log phase SD medium.
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.

Activity regulation

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.

Biotechnology

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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.5 mMMgATP
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
2.5 μmol/min/mg
Activity measured in plasma membranes.

pH Dependence

Optimum pH is 7.0.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site905-912ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcell periphery
Cellular Componentmitochondrion
Cellular Componentplasma membrane
Molecular FunctionABC-type xenobiotic transporter activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionidentical protein binding
Biological Processintracellular monoatomic cation homeostasis
Biological Processresponse to antibiotic
Biological Processresponse to cycloheximide
Biological Processresponse to xenobiotic stimulus
Biological Processxenobiotic detoxification by transmembrane export across the plasma membrane

Keywords

Enzyme and pathway databases

Protein family/group databases

Chemistry

Names & Taxonomy

Protein names

  • Recommended name
    Pleiotropic ABC efflux transporter of multiple drugs
  • Alternative names
    • Pleiotropic drug resistance protein 5
    • Suppressor of toxicity of sporidesmin

Gene names

    • Name
      PDR5
    • Synonyms
      LEM1, STS1, YDR1
    • Ordered locus names
      YOR153W

Organism names

Accessions

  • Primary accession
    P33302
  • Secondary accessions
    • D6W2L0

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Note: The ERAD mutants 'Pro-183' and 'Tyr-1427' fail to reach the plasma membrane. The mutant 'Pro-183' accumulates into ER-associated compartments.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-517Cytoplasmic
Transmembrane518-542Helical
Topological domain543-558Extracellular
Transmembrane559-579Helical
Topological domain580-611Cytoplasmic
Transmembrane612-628Helical
Topological domain629-631Extracellular
Transmembrane632-650Helical
Topological domain651-665Cytoplasmic
Transmembrane666-685Helical
Topological domain686-774Extracellular
Transmembrane775-793Helical
Topological domain794-1237Cytoplasmic
Transmembrane1238-1260Helical
Topological domain1261-1291Extracellular
Transmembrane1292-1313Helical
Topological domain1314-1324Cytoplasmic
Transmembrane1325-1349Helical
Topological domain1350-1354Extracellular
Transmembrane1355-1379Helical
Topological domain1380-1388Cytoplasmic
Transmembrane1389-1407Helical
Topological domain1408-1476Extracellular
Transmembrane1477-1499Helical
Topological domain1500-1511Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis183Activates ER-associated degradation.
Mutagenesis257Alters drug specificity.
Mutagenesis302Confers generalized drug resistance.
Mutagenesis648Alters drug specificity.
Mutagenesis905Inactivates drug transport.
Mutagenesis908Inactivates drug transport.
Mutagenesis1009Confers generalized drug resistance.
Mutagenesis1040Alters drug specificity.
Mutagenesis1048Alters drug specificity.
Mutagenesis1289Alters drug specificity.
Mutagenesis1311Alters drug specificity.
Mutagenesis1360Alters drug specificity.
Mutagenesis1393Alters drug specificity.
Mutagenesis1427Activates ER-associated degradation.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 130 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue, glycosylation, cross-link.

TypeIDPosition(s)Description
ChainPRO_00000934421-1511Pleiotropic ABC efflux transporter of multiple drugs
Modified residue22Phosphoserine
Modified residue49Phosphothreonine
Modified residue51Phosphothreonine
Modified residue54Phosphoserine
Modified residue58Phosphoserine
Modified residue61Phosphoserine
Glycosylation734N-linked (GlcNAc...) asparagine
Cross-link825Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue837Phosphoserine
Modified residue840Phosphoserine
Modified residue841Phosphoserine
Modified residue849Phosphoserine
Modified residue850Phosphoserine
Modified residue854Phosphoserine
Glycosylation1447N-linked (GlcNAc...) asparagine

Post-translational modification

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

Keywords

Proteomic databases

PTM databases

Expression

Induction

Expressed during exponential growth. Transcription is transiently activated within 40 minutes 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.

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-32Disordered
Compositional bias7-29Polar residues
Region52-71Disordered
Domain161-410ABC transporter 1
Compositional bias824-851Basic and acidic residues
Region824-858Disordered
Domain869-1112ABC transporter 2

Domain

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.
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.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,511
  • Mass (Da)
    170,438
  • Last updated
    1994-02-01 v1
  • Checksum
    4540DC0BF04744BA
MPEAKLNNNVNDVTSYSSASSSTENAADLHNYNGFDEHTEARIQKLARTLTAQSMQNSTQSAPNKSDAQSIFSSGVEGVNPIFSDPEAPGYDPKLDPNSENFSSAAWVKNMAHLSAADPDFYKPYSLGCAWKNLSASGASADVAYQSTVVNIPYKILKSGLRKFQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRIKGVDRESYANHLAEVAMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPSRQTTADFLTSVTSPSERTLNKDMLKKGIHIPQTPKEMNDYWVKSPNYKELMKEVDQRLLNDDEASREAIKEAHIAKQSKRARPSSPYTVSYMMQVKYLLIRNMWRLRNNIGFTLFMILGNCSMALILGSMFFKIMKKGDTSTFYFRGSAMFFAILFNAFSSLLEIFSLYEARPITEKHRTYSLYHPSADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGVFFFYLLINIVAVFSMSHLFRCVGSLTKTLSEAMVPASMLLLALSMYTGFAIPKKKILRWSKWIWYINPLAYLFESLLINEFHGIKFPCAEYVPRGPAYANISSTESVCTVVGAVPGQDYVLGDDFIRGTYQYYHKDKWRGFGIGMAYVVFFFFVYLFLCEYNEGAKQKGEILVFPRSIVKRMKKRGVLTEKNANDPENVGERSDLSSDRKMLQESSEEESDTYGEIGLSKSEAIFHWRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFGDLGEGCKTMIDYFESHGAHKCPADANPAEWMLEVVGAAPGSHANQDYYEVWRNSEEYRAVQSELDWMERELPKKGSITAAEDKHEFSQSIIYQTKLVSIRLFQQYWRSPDYLWSKFILTIFNQLFIGFTFFKAGTSLQGLQNQMLAVFMFTVIFNPILQQYLPSFVQQRDLYEARERPSRTFSWISFIFAQIFVEVPWNILAGTIAYFIYYYPIGFYSNASAAGQLHERGALFWLFSCAFYVYVGSMGLLVISFNQVAESAANLASLLFTMSLSFCGVMTTPSAMPRFWIFMYRVSPLTYFIQALLAVGVANVDVKCADYELLEFTPPSGMTCGQYMEPYLQLAKTGYLTDENATDTCSFCQISTTNDYLANVNSFYSERWRNYGIFICYIAFNYIAGVFFYWLARVPKKNGKLSKK

Sequence caution

The sequence BAA05547.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias7-29Polar residues
Sequence conflict171in Ref. 1; BAA05547
Sequence conflict190in Ref. 1; BAA05547
Sequence conflict214in Ref. 1; BAA05547
Sequence conflict308in Ref. 1; BAA05547
Sequence conflict340-345in Ref. 1; BAA05547
Sequence conflict476in Ref. 1; BAA05547
Sequence conflict648in Ref. 1; BAA05547
Sequence conflict770in Ref. 1; BAA05547
Compositional bias824-851Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D26548
EMBL· GenBank· DDBJ
BAA05547.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift
X74113
EMBL· GenBank· DDBJ
CAA52212.1
EMBL· GenBank· DDBJ
Genomic DNA
L19922
EMBL· GenBank· DDBJ
AAB53769.1
EMBL· GenBank· DDBJ
Genomic DNA
U55020
EMBL· GenBank· DDBJ
AAC49639.1
EMBL· GenBank· DDBJ
Genomic DNA
Z75061
EMBL· GenBank· DDBJ
CAA99359.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006948
EMBL· GenBank· DDBJ
DAA10926.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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