PDP2_YEAST
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 03-AUG-2022, entry version 152.
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; 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; 219.
DR DIP; DIP-2963N; -.
DR IntAct; P25646; 30.
DR MINT; P25646; -.
DR STRING; 4932.YCR079W; -.
DR iPTMnet; P25646; -.
DR PaxDb; P25646; -.
DR PRIDE; P25646; -.
DR EnsemblFungi; YCR079W_mRNA; YCR079W; YCR079W.
DR GeneID; 850441; -.
DR KEGG; sce:YCR079W; -.
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 BioCyc; YEAST:G3O-29400-MON; -.
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 (lipoamide)] phosphatase activity; IMP:SGD.
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:0070262; P:peptidyl-serine dephosphorylation; IMP:SGD.
DR GO; GO:1904184; P:positive regulation of pyruvate dehydrogenase activity; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:SGD.
DR GO; GO:1901524; P:regulation of mitophagy; IMP:SGD.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 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
