ID   PDP2_YEAST              Reviewed;         442 AA.
AC   P25646; D6VR81; Q8NIL5;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 2.
DT   20-JAN-2016, entry version 112.
DE   RecName: Full=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial {ECO:0000305};
DE            Short=PDP 2 {ECO:0000305};
DE            EC=3.1.3.16 {ECO:0000269|PubMed:17002782};
DE            EC=3.1.3.43 {ECO:0000269|PubMed:18180296};
DE   AltName: Full=Autophagy-related protein phosphatase 1 {ECO:0000303|PubMed:17166847};
DE   AltName: Full=Phosphatase two C protein 6 {ECO:0000303|PubMed:17002782};
DE   AltName: Full=Protein phosphatase 2C homolog 6 {ECO:0000305};
DE            Short=PP2C-6 {ECO:0000305};
DE   AltName: Full=Protein phosphatase of PDH protein 2;
DE   AltName: Full=Pyruvate dehydrogenase complex phosphatase 2 {ECO:0000303|PubMed:18180296};
DE            Short=PDC phosphatase 2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PTC6 {ECO:0000303|PubMed:17002782};
GN   Synonyms=AUP1 {ECO:0000303|PubMed:17166847},
GN   PPP2 {ECO:0000303|PubMed:18180296};
GN   OrderedLocusNames=YCR079W {ECO:0000312|SGD:S000002133};
GN   ORFNames=YCR79C {ECO:0000312|SGD:S000002133},
GN   YCR79W {ECO:0000312|SGD:S000002133};
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
RA   Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
RA   Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
RA   Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
RA   Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
RA   de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
RA   Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
RA   Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
RA   Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
RA   Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
RA   Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
RA   Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
RA   Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
RA   van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
RA   Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
RA   Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Valles G., Volckaerts G.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   EXPRESSION, AND INTERACTION WITH PRO2.
RA   Maris A.F.;
RL   Submitted (JUN-2002) to UniProtKB.
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=17002782; DOI=10.1111/j.1567-1364.2006.00160.x;
RA   Ruan H., Yan Z., Sun H., Jiang L.;
RT   "The YCR079w gene confers a rapamycin-resistant function and encodes
RT   the sixth type 2C protein phosphatase in Saccharomyces cerevisiae.";
RL   FEMS Yeast Res. 7:209-215(2007).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17166847; DOI=10.1074/jbc.M605940200;
RA   Tal R., Winter G., Ecker N., Klionsky D.J., Abeliovich H.;
RT   "Aup1p, a yeast mitochondrial protein phosphatase homolog, is required
RT   for efficient stationary phase mitophagy and cell survival.";
RL   J. Biol. Chem. 282:5617-5624(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=18180296; DOI=10.1074/jbc.M708779200;
RA   Gey U., Czupalla C., Hoflack B., Rodel G., Krause-Buchholz U.;
RT   "Yeast pyruvate dehydrogenase complex is regulated by a concerted
RT   activity of two kinases and two phosphatases.";
RL   J. Biol. Chem. 283:9759-9767(2008).
CC   -!- FUNCTION: Protein phosphatase that shows typical type 2C protein
CC       phosphatase (PP2C) activity (PubMed:17002782). Catalyzes the
CC       dephosphorylation and concomitant reactivation of the E1 alpha
CC       subunit (PDA1) of the pyruvate dehydrogenase complex
CC       (PubMed:18180296). Required for efficient mitophagy in stationary
CC       phase cells (PubMed:17166847). {ECO:0000269|PubMed:17002782,
CC       ECO:0000269|PubMed:17166847, ECO:0000269|PubMed:18180296}.
CC   -!- CATALYTIC ACTIVITY: [Pyruvate dehydrogenase (acetyl-transferring)]
CC       phosphate + H(2)O = [pyruvate dehydrogenase (acetyl-transferring)]
CC       + phosphate. {ECO:0000269|PubMed:18180296}.
CC   -!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
CC       = [a protein]-serine/threonine + phosphate.
CC       {ECO:0000269|PubMed:17002782}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:17002782};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:17002782};
CC   -!- SUBUNIT: Interacts with PRO2. {ECO:0000269|Ref.4}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:17166847, ECO:0000269|PubMed:18180296}.
CC       Mitochondrion matrix {ECO:0000269|PubMed:17166847,
CC       ECO:0000269|PubMed:18180296}.
CC   -!- DISRUPTION PHENOTYPE: Confers rapamycin-sensitivity.
CC       {ECO:0000269|PubMed:17002782}.
CC   -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Contains 1 PPM-type phosphatase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU01082}.
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DR   EMBL; X59720; CAC42991.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07550.1; -; Genomic_DNA.
DR   PIR; S19493; S19493.
DR   RefSeq; NP_010003.2; NM_001180034.1.
DR   ProteinModelPortal; P25646; -.
DR   SMR; P25646; 238-414.
DR   BioGrid; 31053; 73.
DR   DIP; DIP-2963N; -.
DR   IntAct; P25646; 9.
DR   MINT; MINT-501031; -.
DR   iPTMnet; P25646; -.
DR   EnsemblFungi; CAC42991; CAC42991; CAC42991.
DR   EnsemblFungi; YCR079W; YCR079W; YCR079W.
DR   GeneID; 850441; -.
DR   KEGG; sce:YCR079W; -.
DR   EuPathDB; FungiDB:YCR079W; -.
DR   SGD; S000002133; PTC6.
DR   HOGENOM; HOG000000910; -.
DR   InParanoid; P25646; -.
DR   OMA; DKNGIAH; -.
DR   OrthoDB; EOG7Q8CZ1; -.
DR   BioCyc; YEAST:G3O-29400-MONOMER; -.
DR   NextBio; 966045; -.
DR   PRO; PR:P25646; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR   GO; GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
DR   GO; GO:0016236; P:macroautophagy; IGI:SGD.
DR   GO; GO:0000422; P:mitophagy; IMP:SGD.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IMP:SGD.
DR   GO; GO:0006470; P:protein dephosphorylation; IMP:SGD.
DR   Gene3D; 3.60.40.10; -; 2.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 4.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 2.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Complete proteome; Hydrolase; Magnesium; Manganese;
KW   Mitochondrion; Protein phosphatase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     34       Mitochondrion. {ECO:0000255}.
FT   CHAIN        35    442       [Pyruvate dehydrogenase [acetyl-
FT                                transferring]]-phosphatase 2,
FT                                mitochondrial.
FT                                /FTId=PRO_0000057788.
FT   DOMAIN       35    411       PPM-type phosphatase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01082}.
SQ   SEQUENCE   442 AA;  49421 MW;  0F3303047F957515 CRC64;
     MRLGNAYAYC KPSQNVGLKL DLLRGLPGYV GHATSRINRL ENQDNYSIKM MRSWPNAYGS
     ALNCSVFDGH GEKGAQLSQL LADKLCSSLD FPEPSWDKQD LKKLVQEYAR RFPEGNYWKH
     KLSTFEKFYN KFIKNCNSKQ ELLLMKEGDS AILGQNGGRM IFDKMGNIID KIALLTELDR
     LRLFYGFARF DLDQCCGLGT AAGSTASSIF LYPYDDPNAP IDEGKDDDSW IISHSGLLKL
     IVTQVGDSKI ILCDQDGIAH ALTTTHHINS SRERHRLSID PSRLDPDAFG ETRFLNNFAN
     TRSFGDVAGK PYGISSEPDI FSFLVGNTLH LPRSERSKLP FNGDECFLAL VTDGITNKLA
     DQEVVDLITS TVNSWGLKKA TPQFVAEETI KFIQAIATKH SDNATCVVVR LSNWGNWPNV
     DRTGPQRETK LMNAQSNETK LN
//