PP2C2_YEAST
ID PP2C2_YEAST Reviewed; 464 AA.
AC P39966; D3DLZ6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Protein phosphatase 2C homolog 2;
DE Short=PP2C-2;
DE EC=3.1.3.16;
GN Name=PTC2; OrderedLocusNames=YER089C;
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 [GENOMIC DNA].
RA Maeda T., Tsai A.Y.M., Saito H.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 FUNCTION.
RX PubMed=10580002; DOI=10.1101/gad.13.22.2946;
RA Cheng A., Ross K.E., Kaldis P., Solomon M.J.;
RT "Dephosphorylation of cyclin-dependent kinases by type 2C protein
RT phosphatases.";
RL Genes Dev. 13:2946-2957(1999).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-376 AND THR-380, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Responsible, together with PTC3, for the dephosphorylation of
CC the cyclin-dependent protein kinase CDC28.
CC {ECO:0000269|PubMed:10580002}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC P39966; Q12447: PAA1; NbExp=8; IntAct=EBI-12795, EBI-33397;
CC -!- MISCELLANEOUS: Present with 12600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; U18839; AAB64644.1; -; Genomic_DNA.
DR EMBL; U72498; AAB17392.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07750.1; -; Genomic_DNA.
DR PIR; S50592; S50592.
DR RefSeq; NP_011013.1; NM_001178980.1.
DR AlphaFoldDB; P39966; -.
DR SMR; P39966; -.
DR BioGRID; 36834; 210.
DR DIP; DIP-1539N; -.
DR IntAct; P39966; 14.
DR MINT; P39966; -.
DR STRING; 4932.YER089C; -.
DR iPTMnet; P39966; -.
DR MaxQB; P39966; -.
DR PaxDb; P39966; -.
DR PRIDE; P39966; -.
DR EnsemblFungi; YER089C_mRNA; YER089C; YER089C.
DR GeneID; 856823; -.
DR KEGG; sce:YER089C; -.
DR SGD; S000000891; PTC2.
DR VEuPathDB; FungiDB:YER089C; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000172210; -.
DR HOGENOM; CLU_013173_4_2_1; -.
DR InParanoid; P39966; -.
DR OMA; HKPNNEA; -.
DR BioCyc; YEAST:G3O-30258-MON; -.
DR PRO; PR:P39966; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39966; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990439; F:MAP kinase serine/threonine phosphatase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:SGD.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
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; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..464
FT /note="Protein phosphatase 2C homolog 2"
FT /id="PRO_0000057775"
FT DOMAIN 23..292
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 361..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 464 AA; 50388 MW; 61D82D2CA4ED3FED CRC64;
MGQILSNPVI DKESHSGADS LTAFGLCAMQ GWRMSMEDSH ILEPNVLTKS DKDHIAFYGI
FDGHGGAKVA EYCGNKIVEI LQEQKSFHEG NLPRALIDTF INTDVKLLQD PVMKEDHSGC
TATSILVSKS QNLLVCGNAG DSRTVLATDG NAKALSYDHK PTLASEKSRI VAADGFVEMD
RVNGNLALSR AIGDFEFKSN PKLGPEEQIV TCVPDILEHS LDYDRDEFVI LACDGIWDCL
TSQDCVDLVH LGLREGKTLN EISSRIIDVC CAPTTEGTGI GCDNMSIVVV ALLKEGEDVA
QWSDRMKSKA HRTSVRSFAD KRRRVFSYYD FSKCNDEQVF AITTKKPQDK FTRDHEAAVA
SVTAADNDDP MDIDDTDADT DAENLDPSSQ SKSKTSGPID LASLEALLGA TGGVKTDSNG
NKVTYTLPQS ALAQLLQTMG HDPASSHPEN DSNTDHKAGR SHLQ
