P33302 · PDR5_YEAST
- ProteinPleiotropic ABC efflux transporter of multiple drugs
- GenePDR5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1511 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 mM | MgATP |
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell periphery | |
Cellular Component | mitochondrion | |
Cellular Component | plasma membrane | |
Molecular Function | ABC-type xenobiotic transporter activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | identical protein binding | |
Biological Process | intracellular monoatomic cation homeostasis | |
Biological Process | response to antibiotic | |
Biological Process | response to cycloheximide | |
Biological Process | response to xenobiotic stimulus | |
Biological Process | xenobiotic detoxification by transmembrane export across the plasma membrane |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended namePleiotropic ABC efflux transporter of multiple drugs
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP33302
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-517 | Cytoplasmic | ||||
Sequence: MPEAKLNNNVNDVTSYSSASSSTENAADLHNYNGFDEHTEARIQKLARTLTAQSMQNSTQSAPNKSDAQSIFSSGVEGVNPIFSDPEAPGYDPKLDPNSENFSSAAWVKNMAHLSAADPDFYKPYSLGCAWKNLSASGASADVAYQSTVVNIPYKILKSGLRKFQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRIKGVDRESYANHLAEVAMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPSRQTTADFLTSVTSPSERTLNKDMLKKGIHIPQTPKEMNDYWVKSPNYKELMKEVDQRLLNDDEASREAIKEAHIAKQSKRARPSSPYTVSYMMQVKYLLIRNMWRLR | ||||||
Transmembrane | 518-542 | Helical | ||||
Sequence: NNIGFTLFMILGNCSMALILGSMFF | ||||||
Topological domain | 543-558 | Extracellular | ||||
Sequence: KIMKKGDTSTFYFRGS | ||||||
Transmembrane | 559-579 | Helical | ||||
Sequence: AMFFAILFNAFSSLLEIFSLY | ||||||
Topological domain | 580-611 | Cytoplasmic | ||||
Sequence: EARPITEKHRTYSLYHPSADAFASVLSEIPSK | ||||||
Transmembrane | 612-628 | Helical | ||||
Sequence: LIIAVCFNIIFYFLVDF | ||||||
Topological domain | 629-631 | Extracellular | ||||
Sequence: RRN | ||||||
Transmembrane | 632-650 | Helical | ||||
Sequence: GGVFFFYLLINIVAVFSMS | ||||||
Topological domain | 651-665 | Cytoplasmic | ||||
Sequence: HLFRCVGSLTKTLSE | ||||||
Transmembrane | 666-685 | Helical | ||||
Sequence: AMVPASMLLLALSMYTGFAI | ||||||
Topological domain | 686-774 | Extracellular | ||||
Sequence: PKKKILRWSKWIWYINPLAYLFESLLINEFHGIKFPCAEYVPRGPAYANISSTESVCTVVGAVPGQDYVLGDDFIRGTYQYYHKDKWRG | ||||||
Transmembrane | 775-793 | Helical | ||||
Sequence: FGIGMAYVVFFFFVYLFLC | ||||||
Topological domain | 794-1237 | Cytoplasmic | ||||
Sequence: EYNEGAKQKGEILVFPRSIVKRMKKRGVLTEKNANDPENVGERSDLSSDRKMLQESSEEESDTYGEIGLSKSEAIFHWRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFGDLGEGCKTMIDYFESHGAHKCPADANPAEWMLEVVGAAPGSHANQDYYEVWRNSEEYRAVQSELDWMERELPKKGSITAAEDKHEFSQSIIYQTKLVSIRLFQQYWRSPDYLWSKFILTIFNQLFIGFTFFKAGTSLQGLQNQ | ||||||
Transmembrane | 1238-1260 | Helical | ||||
Sequence: MLAVFMFTVIFNPILQQYLPSFV | ||||||
Topological domain | 1261-1291 | Extracellular | ||||
Sequence: QQRDLYEARERPSRTFSWISFIFAQIFVEVP | ||||||
Transmembrane | 1292-1313 | Helical | ||||
Sequence: WNILAGTIAYFIYYYPIGFYSN | ||||||
Topological domain | 1314-1324 | Cytoplasmic | ||||
Sequence: ASAAGQLHERG | ||||||
Transmembrane | 1325-1349 | Helical | ||||
Sequence: ALFWLFSCAFYVYVGSMGLLVISFN | ||||||
Topological domain | 1350-1354 | Extracellular | ||||
Sequence: QVAES | ||||||
Transmembrane | 1355-1379 | Helical | ||||
Sequence: AANLASLLFTMSLSFCGVMTTPSAM | ||||||
Topological domain | 1380-1388 | Cytoplasmic | ||||
Sequence: PRFWIFMYR | ||||||
Transmembrane | 1389-1407 | Helical | ||||
Sequence: VSPLTYFIQALLAVGVANV | ||||||
Topological domain | 1408-1476 | Extracellular | ||||
Sequence: DVKCADYELLEFTPPSGMTCGQYMEPYLQLAKTGYLTDENATDTCSFCQISTTNDYLANVNSFYSERWR | ||||||
Transmembrane | 1477-1499 | Helical | ||||
Sequence: NYGIFICYIAFNYIAGVFFYWLA | ||||||
Topological domain | 1500-1511 | Cytoplasmic | ||||
Sequence: RVPKKNGKLSKK |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 183 | Activates ER-associated degradation. | ||||
Sequence: L → P | ||||||
Mutagenesis | 257 | Alters drug specificity. | ||||
Sequence: T → I | ||||||
Mutagenesis | 302 | Confers generalized drug resistance. | ||||
Sequence: G → D | ||||||
Mutagenesis | 648 | Alters drug specificity. | ||||
Sequence: S → F | ||||||
Mutagenesis | 905 | Inactivates drug transport. | ||||
Sequence: G → S | ||||||
Mutagenesis | 908 | Inactivates drug transport. | ||||
Sequence: G → S | ||||||
Mutagenesis | 1009 | Confers generalized drug resistance. | ||||
Sequence: G → C | ||||||
Mutagenesis | 1040 | Alters drug specificity. | ||||
Sequence: G → D | ||||||
Mutagenesis | 1048 | Alters drug specificity. | ||||
Sequence: S → V | ||||||
Mutagenesis | 1289 | Alters drug specificity. | ||||
Sequence: E → K | ||||||
Mutagenesis | 1311 | Alters drug specificity. | ||||
Sequence: Y → S | ||||||
Mutagenesis | 1360 | Alters drug specificity. | ||||
Sequence: S → F | ||||||
Mutagenesis | 1393 | Alters drug specificity. | ||||
Sequence: T → I | ||||||
Mutagenesis | 1427 | Activates ER-associated degradation. | ||||
Sequence: C → Y |
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.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000093442 | 1-1511 | Pleiotropic ABC efflux transporter of multiple drugs | |||
Sequence: MPEAKLNNNVNDVTSYSSASSSTENAADLHNYNGFDEHTEARIQKLARTLTAQSMQNSTQSAPNKSDAQSIFSSGVEGVNPIFSDPEAPGYDPKLDPNSENFSSAAWVKNMAHLSAADPDFYKPYSLGCAWKNLSASGASADVAYQSTVVNIPYKILKSGLRKFQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRIKGVDRESYANHLAEVAMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPSRQTTADFLTSVTSPSERTLNKDMLKKGIHIPQTPKEMNDYWVKSPNYKELMKEVDQRLLNDDEASREAIKEAHIAKQSKRARPSSPYTVSYMMQVKYLLIRNMWRLRNNIGFTLFMILGNCSMALILGSMFFKIMKKGDTSTFYFRGSAMFFAILFNAFSSLLEIFSLYEARPITEKHRTYSLYHPSADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGVFFFYLLINIVAVFSMSHLFRCVGSLTKTLSEAMVPASMLLLALSMYTGFAIPKKKILRWSKWIWYINPLAYLFESLLINEFHGIKFPCAEYVPRGPAYANISSTESVCTVVGAVPGQDYVLGDDFIRGTYQYYHKDKWRGFGIGMAYVVFFFFVYLFLCEYNEGAKQKGEILVFPRSIVKRMKKRGVLTEKNANDPENVGERSDLSSDRKMLQESSEEESDTYGEIGLSKSEAIFHWRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFGDLGEGCKTMIDYFESHGAHKCPADANPAEWMLEVVGAAPGSHANQDYYEVWRNSEEYRAVQSELDWMERELPKKGSITAAEDKHEFSQSIIYQTKLVSIRLFQQYWRSPDYLWSKFILTIFNQLFIGFTFFKAGTSLQGLQNQMLAVFMFTVIFNPILQQYLPSFVQQRDLYEARERPSRTFSWISFIFAQIFVEVPWNILAGTIAYFIYYYPIGFYSNASAAGQLHERGALFWLFSCAFYVYVGSMGLLVISFNQVAESAANLASLLFTMSLSFCGVMTTPSAMPRFWIFMYRVSPLTYFIQALLAVGVANVDVKCADYELLEFTPPSGMTCGQYMEPYLQLAKTGYLTDENATDTCSFCQISTTNDYLANVNSFYSERWRNYGIFICYIAFNYIAGVFFYWLARVPKKNGKLSKK | ||||||
Modified residue | 22 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 49 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 51 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 54 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 58 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 61 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 734 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Cross-link | 825 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 837 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 840 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 841 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 849 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 850 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 854 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 1447 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Ubiquitinylation mediates endocytosis and vacuolar degradation. Phosphorylation by casein kinase I stabilizes the protein half-life.
Keywords
- PTM
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.
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P33302 | HXT1 P32465 | 3 | EBI-13038, EBI-8759 | |
BINARY | P33302 | NCR1 Q12200 | 2 | EBI-13038, EBI-32032 | |
BINARY | P33302 | PDR12 Q02785 | 3 | EBI-13038, EBI-13065 | |
BINARY | P33302 | PDR5 P33302 | 4 | EBI-13038, EBI-13038 | |
BINARY | P33302 | SNQ2 P32568 | 5 | EBI-13038, EBI-17590 | |
BINARY | P33302 | YER097W P40062 | 2 | EBI-13038, EBI-20799372 | |
BINARY | P33302 | YOL075C Q08234 | 3 | EBI-13038, EBI-29278 | |
BINARY | P33302 | ZRT1 P32804 | 2 | EBI-13038, EBI-29677 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MPEAKLNNNVNDVTSYSSASSSTENAADLHNY | ||||||
Compositional bias | 7-29 | Polar residues | ||||
Sequence: NNNVNDVTSYSSASSSTENAADL | ||||||
Region | 52-71 | Disordered | ||||
Sequence: AQSMQNSTQSAPNKSDAQSI | ||||||
Domain | 161-410 | ABC transporter 1 | ||||
Sequence: LRKFQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRIKGVDRESYANHLAEVAMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPS | ||||||
Compositional bias | 824-851 | Basic and acidic residues | ||||
Sequence: EKNANDPENVGERSDLSSDRKMLQESSE | ||||||
Region | 824-858 | Disordered | ||||
Sequence: EKNANDPENVGERSDLSSDRKMLQESSEEESDTYG | ||||||
Domain | 869-1112 | ABC transporter 2 | ||||
Sequence: FHWRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFGDLGEGCKTMIDYFESHGA |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,511
- Mass (Da)170,438
- Last updated1994-02-01 v1
- Checksum4540DC0BF04744BA
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-29 | Polar residues | ||||
Sequence: NNNVNDVTSYSSASSSTENAADL | ||||||
Sequence conflict | 171 | in Ref. 1; BAA05547 | ||||
Sequence: N → L | ||||||
Sequence conflict | 190 | in Ref. 1; BAA05547 | ||||
Sequence: V → I | ||||||
Sequence conflict | 214 | in Ref. 1; BAA05547 | ||||
Sequence: D → T | ||||||
Sequence conflict | 308 | in Ref. 1; BAA05547 | ||||
Sequence: G → V | ||||||
Sequence conflict | 340-345 | in Ref. 1; BAA05547 | ||||
Sequence: Missing | ||||||
Sequence conflict | 476 | in Ref. 1; BAA05547 | ||||
Sequence: R → H | ||||||
Sequence conflict | 648 | in Ref. 1; BAA05547 | ||||
Sequence: Missing | ||||||
Sequence conflict | 770 | in Ref. 1; BAA05547 | ||||
Sequence: D → H | ||||||
Compositional bias | 824-851 | Basic and acidic residues | ||||
Sequence: EKNANDPENVGERSDLSSDRKMLQESSE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |