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Protein

[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial

Gene

PTC6

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

Catalyzes the dephosphorylation and concomitant reactivation of the E1 alpha subunit (PDA1) of the pyruvate dehydrogenase complex. Required for efficient mitophagy in stationary phase cells.3 Publications

Catalytic activityi

[Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate.

GO - Molecular functioni

  1. [pyruvate dehydrogenase (lipoamide)] phosphatase activity Source: UniProtKB-EC
  2. protein serine/threonine phosphatase activity Source: SGD

GO - Biological processi

  1. macroautophagy Source: SGD
  2. mitochondrion degradation Source: SGD
  3. positive regulation of catalytic activity Source: SGD
  4. protein dephosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciYEAST:G3O-29400-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial (EC:3.1.3.43)
Short name:
PDP 2
Alternative name(s):
Autophagy-related protein phosphatase 1
Phosphatase two C protein 6
Protein phosphatase 2C homolog 6
Short name:
PP2C-6
Protein phosphatase of PDH protein 2
Pyruvate dehydrogenase complex phosphatase 2
Short name:
PDC phosphatase 2
Gene namesi
Name:PTC6
Synonyms:AUP1, PPP2
Ordered Locus Names:YCR079W
ORF Names:YCR79C, YCR79W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCR079w.
SGDiS000002133. PTC6.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: SGD
  2. mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Confers rapamycin-sensitivity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434MitochondrionSequence AnalysisAdd
BLAST
Chaini35 – 442408[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrialPRO_0000057788Add
BLAST

Proteomic databases

PaxDbiP25646.

Expressioni

Gene expression databases

GenevestigatoriP25646.

Interactioni

Subunit structurei

Interacts with PRO2.1 Publication

Protein-protein interaction databases

BioGridi31053. 72 interactions.
DIPiDIP-2963N.
IntActiP25646. 9 interactions.
MINTiMINT-501031.
STRINGi4932.YCR079W.

Structurei

3D structure databases

ProteinModelPortaliP25646.
SMRiP25646. Positions 238-414.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 402295PP2C-likeAdd
BLAST

Sequence similaritiesi

Contains 1 PP2C-like domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000000910.
InParanoidiP25646.
OMAiDKNGIAH.
OrthoDBiEOG7Q8CZ1.

Family and domain databases

Gene3Di3.60.40.10. 2 hits.
InterProiIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25646-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLGNAYAYC KPSQNVGLKL DLLRGLPGYV GHATSRINRL ENQDNYSIKM
60 70 80 90 100
MRSWPNAYGS ALNCSVFDGH GEKGAQLSQL LADKLCSSLD FPEPSWDKQD
110 120 130 140 150
LKKLVQEYAR RFPEGNYWKH KLSTFEKFYN KFIKNCNSKQ ELLLMKEGDS
160 170 180 190 200
AILGQNGGRM IFDKMGNIID KIALLTELDR LRLFYGFARF DLDQCCGLGT
210 220 230 240 250
AAGSTASSIF LYPYDDPNAP IDEGKDDDSW IISHSGLLKL IVTQVGDSKI
260 270 280 290 300
ILCDQDGIAH ALTTTHHINS SRERHRLSID PSRLDPDAFG ETRFLNNFAN
310 320 330 340 350
TRSFGDVAGK PYGISSEPDI FSFLVGNTLH LPRSERSKLP FNGDECFLAL
360 370 380 390 400
VTDGITNKLA DQEVVDLITS TVNSWGLKKA TPQFVAEETI KFIQAIATKH
410 420 430 440
SDNATCVVVR LSNWGNWPNV DRTGPQRETK LMNAQSNETK LN
Length:442
Mass (Da):49,421
Last modified:October 10, 2003 - v2
Checksum:i0F3303047F957515
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42991.1.
BK006937 Genomic DNA. Translation: DAA07550.1.
PIRiS19493.
RefSeqiNP_010003.2. NM_001180034.1.

Genome annotation databases

EnsemblFungiiYCR079W; YCR079W; YCR079W.
GeneIDi850441.
KEGGisce:YCR079W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42991.1.
BK006937 Genomic DNA. Translation: DAA07550.1.
PIRiS19493.
RefSeqiNP_010003.2. NM_001180034.1.

3D structure databases

ProteinModelPortaliP25646.
SMRiP25646. Positions 238-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31053. 72 interactions.
DIPiDIP-2963N.
IntActiP25646. 9 interactions.
MINTiMINT-501031.
STRINGi4932.YCR079W.

Proteomic databases

PaxDbiP25646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCR079W; YCR079W; YCR079W.
GeneIDi850441.
KEGGisce:YCR079W.

Organism-specific databases

CYGDiYCR079w.
SGDiS000002133. PTC6.

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000000910.
InParanoidiP25646.
OMAiDKNGIAH.
OrthoDBiEOG7Q8CZ1.

Enzyme and pathway databases

BioCyciYEAST:G3O-29400-MONOMER.

Miscellaneous databases

NextBioi966045.

Gene expression databases

GenevestigatoriP25646.

Family and domain databases

Gene3Di3.60.40.10. 2 hits.
InterProiIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Valles G., Volckaerts G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Maris A.F.
    Submitted (JUN-2002) to UniProtKB
    Cited for: EXPRESSION, INTERACTION WITH PRO2.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "The YCR079w gene confers a rapamycin-resistant function and encodes the sixth type 2C protein phosphatase in Saccharomyces cerevisiae."
    Ruan H., Yan Z., Sun H., Jiang L.
    FEMS Yeast Res. 7:209-215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival."
    Tal R., Winter G., Ecker N., Klionsky D.J., Abeliovich H.
    J. Biol. Chem. 282:5617-5624(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases."
    Gey U., Czupalla C., Hoflack B., Rodel G., Krause-Buchholz U.
    J. Biol. Chem. 283:9759-9767(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPDP2_YEAST
AccessioniPrimary (citable) accession number: P25646
Secondary accession number(s): D6VR81, Q8NIL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 10, 2003
Last modified: January 7, 2015
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 432 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

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 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.