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   27-MAR-2024, entry version 160.
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}, PPP2
GN   {ECO:0000303|PubMed:18180296};
GN   OrderedLocusNames=YCR079W {ECO:0000312|SGD:S000002133};
GN   ORFNames=YCR79C {ECO:0000312|SGD:S000002133}, YCR79W
GN   {ECO:0000312|SGD:S000002133};
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   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., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., 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., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   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., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Dephoure N.,
RA   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 the
RT   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 for
RT   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 activity
RT   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 subunit
CC       (PDA1) of the pyruvate dehydrogenase complex (PubMed:18180296).
CC       Required for efficient mitophagy in stationary phase cells
CC       (PubMed:17166847). {ECO:0000269|PubMed:17002782,
CC       ECO:0000269|PubMed:17166847, ECO:0000269|PubMed:18180296}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha
CC         subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] +
CC         phosphate; Xref=Rhea:RHEA:12669, Rhea:RHEA-COMP:13689, Rhea:RHEA-
CC         COMP:13690, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.43;
CC         Evidence={ECO:0000269|PubMed:18180296};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000269|PubMed:17002782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={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 medium.
CC       {ECO:0000269|PubMed:14562106}.
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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   AlphaFoldDB; P25646; -.
DR   BioGRID; 31053; 221.
DR   DIP; DIP-2963N; -.
DR   IntAct; P25646; 30.
DR   MINT; P25646; -.
DR   STRING; 4932.YCR079W; -.
DR   iPTMnet; P25646; -.
DR   PaxDb; 4932-YCR079W; -.
DR   PeptideAtlas; P25646; -.
DR   EnsemblFungi; YCR079W_mRNA; YCR079W; YCR079W.
DR   GeneID; 850441; -.
DR   KEGG; sce:YCR079W; -.
DR   AGR; SGD:S000002133; -.
DR   SGD; S000002133; PTC6.
DR   VEuPathDB; FungiDB:YCR079W; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   GeneTree; ENSGT00940000156633; -.
DR   HOGENOM; CLU_021251_0_0_1; -.
DR   InParanoid; P25646; -.
DR   OMA; LPNWGNW; -.
DR   OrthoDB; 202023at2759; -.
DR   BioCyc; YEAST:G3O-29400-MONOMER; -.
DR   BioGRID-ORCS; 850441; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P25646; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25646; Protein.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0004741; F:[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity; IMP:SGD.
DR   GO; GO:0019909; F:[pyruvate dehydrogenase (lipoamide)] phosphatase regulator activity; IEA:UniProtKB-EC.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR   GO; GO:0016236; P:macroautophagy; IGI:SGD.
DR   GO; GO:1901524; P:regulation of mitophagy; IMP:SGD.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF828; [PYRUVATE DEHYDROGENASE [ACETYL-TRANSFERRING]]-PHOSPHATASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Hydrolase; Magnesium; Manganese; Mitochondrion;
KW   Protein phosphatase; Reference proteome; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..442
FT                   /note="[Pyruvate dehydrogenase [acetyl-transferring]]-
FT                   phosphatase 2, mitochondrial"
FT                   /id="PRO_0000057788"
FT   DOMAIN          35..411
FT                   /note="PPM-type phosphatase"
FT                   /evidence="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
//