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Entry version 200 (03 Jul 2019)
Sequence version 1 (01 Feb 1994)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi905 – 912ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processAntibiotic resistance, Cycloheximide resistance, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33670-MONOMER

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.1.205.1 the atp-binding cassette (abc) superfamily

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000523

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Pleiotropic ABC efflux transporter of multiple drugs
Alternative name(s):
Pleiotropic drug resistance protein 5
Suppressor of toxicity of sporidesmin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PDR5
Synonyms:LEM1, STS1, YDR1
Ordered Locus Names:YOR153W
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YOR153W

Saccharomyces Genome Database

More...
SGDi
S000005679 PDR5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 517CytoplasmicSequence analysisAdd BLAST517
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>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

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1697658

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000934421 – 1511Pleiotropic ABC efflux transporter of multiple drugsAdd BLAST1511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei22PhosphoserineCombined sources1
Modified residuei49PhosphothreonineCombined sources1
Modified residuei51PhosphothreonineCombined sources1
Modified residuei54PhosphoserineCombined sources1
Modified residuei58PhosphoserineCombined sources1
Modified residuei61PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi734N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P33302

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P33302

PRoteomics IDEntifications database

More...
PRIDEi
P33302

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P33302

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34549, 127 interactors

Database of interacting proteins

More...
DIPi
DIP-6776N

Protein interaction database and analysis system

More...
IntActi
P33302, 45 interactors

Molecular INTeraction database

More...
MINTi
P33302

STRING: functional protein association networks

More...
STRINGi
4932.YOR153W

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P33302

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P33302

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini161 – 410ABC transporter 1PROSITE-ProRule annotationAdd BLAST250
Domaini869 – 1112ABC transporter 2PROSITE-ProRule annotationAdd BLAST244

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi784 – 787Poly-Phe4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176297

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000162078

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P33302

KEGG Orthology (KO)

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KOi
K08711

Identification of Orthologs from Complete Genome Data

More...
OMAi
PAVWRDS

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03233 ABCG_PDR_domain1, 1 hit
cd03232 ABCG_PDR_domain2, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR013525 ABC_2_trans
IPR029481 ABC_trans_N
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR034001 ABCG_PDR_1
IPR034003 ABCG_PDR_2
IPR005285 Drug-R_PDR/CDR
IPR027417 P-loop_NTPase
IPR010929 PDR_CDR_ABC

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01061 ABC2_membrane, 2 hits
PF00005 ABC_tran, 2 hits
PF14510 ABC_trans_N, 1 hit
PF06422 PDR_CDR, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382 AAA, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00956 3a01205, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4540DC0BF04744BA
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

Protein sequence database of the Protein Information Resource

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PIRi
A53151

NCBI Reference Sequences

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RefSeqi
NP_014796.3, NM_001183572.3

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YOR153W_mRNA; YOR153W_mRNA; YOR153W

Database of genes from NCBI RefSeq genomes

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GeneIDi
854324

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YOR153W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

SMRiP33302
ModBaseiSearch...

Protein-protein interaction databases

BioGridi34549, 127 interactors
DIPiDIP-6776N
IntActiP33302, 45 interactors
MINTiP33302
STRINGi4932.YOR153W

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
PaxDbiP33302
PRIDEiP33302

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR153W_mRNA; YOR153W_mRNA; YOR153W
GeneIDi854324
KEGGisce:YOR153W

Organism-specific databases

EuPathDBiFungiDB:YOR153W
SGDiS000005679 PDR5

Phylogenomic databases

GeneTreeiENSGT00940000176297
HOGENOMiHOG000162078
InParanoidiP33302
KOiK08711
OMAiPAVWRDS

Enzyme and pathway databases

BioCyciYEAST:G3O-33670-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P33302

Family and domain databases

CDDicd03233 ABCG_PDR_domain1, 1 hit
cd03232 ABCG_PDR_domain2, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR013525 ABC_2_trans
IPR029481 ABC_trans_N
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR034001 ABCG_PDR_1
IPR034003 ABCG_PDR_2
IPR005285 Drug-R_PDR/CDR
IPR027417 P-loop_NTPase
IPR010929 PDR_CDR_ABC
PfamiView protein in Pfam
PF01061 ABC2_membrane, 2 hits
PF00005 ABC_tran, 2 hits
PF14510 ABC_trans_N, 1 hit
PF06422 PDR_CDR, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SUPFAMiSSF52540 SSF52540, 2 hits
TIGRFAMsiTIGR00956 3a01205, 1 hit
PROSITEiView protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPDR5_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P33302
Secondary accession number(s): D6W2L0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 3, 2019
This is version 200 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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