ID   PP2C1_YEAST             Reviewed;         281 AA.
AC   P35182; D6VRY2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Protein phosphatase 2C homolog 1;
DE            Short=PP2C-1;
DE            EC=3.1.3.16;
GN   Name=PTC1; Synonyms=TPD1; OrderedLocusNames=YDL006W; ORFNames=D2925;
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].
RX   PubMed=8395005; DOI=10.1128/mcb.13.9.5408-5417.1993;
RA   Maeda T., Tsai A.Y.M., Saito H.;
RT   "Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein
RT   serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in
RT   Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 13:5408-5417(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8196609; DOI=10.1128/mcb.14.6.3634-3645.1994;
RA   Robinson M.K., van Zyl W.H., Phizicky E.M., Broach J.R.;
RT   "TPD1 of Saccharomyces cerevisiae encodes a protein phosphatase 2C-like
RT   activity implicated in tRNA splicing and cell separation.";
RL   Mol. Cell. Biol. 14:3634-3645(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
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   [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   INTERACTION WITH NBP2 AND PBS2.
RX   PubMed=14685261; DOI=10.1038/sj.emboj.7600036;
RA   Mapes J., Ota I.M.;
RT   "Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK
RT   pathway.";
RL   EMBO J. 23:302-311(2004).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=35563734; DOI=10.3390/cells11091426;
RA   David Y., Castro I.G., Yifrach E., Bibi C., Katawi E., Yahav Har-Shai D.,
RA   Brodsky S., Barkai N., Ravid T., Eisenstein M., Pietrokovski S.,
RA   Schuldiner M., Zalckvar E.;
RT   "Pls1 Is a Peroxisomal Matrix Protein with a Role in Regulating Lysine
RT   Biosynthesis.";
RL   Cells 11:1426-1426(2022).
CC   -!- FUNCTION: It has a serine and a weak tyrosine phosphatase activity with
CC       ratios of serine to tyrosine phosphatase activity as high as 200:1. It
CC       is essential for growth or germination at 37 degrees Celsius. May have
CC       a role in the heat shock response. Involved in tRNA splicing and cell
CC       separation.
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;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 magnesium or manganese ions per subunit. Manganese is
CC       about 20 times more efficient than magnesium.;
CC   -!- SUBUNIT: Interacts with NBP2 and PBS2. {ECO:0000269|PubMed:14685261}.
CC   -!- INTERACTION:
CC       P35182; Q12163: NBP2; NbExp=4; IntAct=EBI-12784, EBI-34713;
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:35563734}.
CC       Note=Peroxisomal localization is dependent on PEX5.
CC       {ECO:0000269|PubMed:35563734}.
CC   -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; L14593; AAA34920.1; -; Genomic_DNA.
DR   EMBL; Z48432; CAA88353.1; -; Genomic_DNA.
DR   EMBL; Z74054; CAA98562.1; -; Genomic_DNA.
DR   EMBL; Z48008; CAA88055.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11842.1; -; Genomic_DNA.
DR   PIR; S41854; S41854.
DR   RefSeq; NP_010278.3; NM_001180065.3.
DR   AlphaFoldDB; P35182; -.
DR   SMR; P35182; -.
DR   BioGRID; 32048; 839.
DR   DIP; DIP-1537N; -.
DR   IntAct; P35182; 13.
DR   MINT; P35182; -.
DR   STRING; 4932.YDL006W; -.
DR   iPTMnet; P35182; -.
DR   MaxQB; P35182; -.
DR   PaxDb; 4932-YDL006W; -.
DR   PeptideAtlas; P35182; -.
DR   EnsemblFungi; YDL006W_mRNA; YDL006W; YDL006W.
DR   GeneID; 851558; -.
DR   KEGG; sce:YDL006W; -.
DR   AGR; SGD:S000002164; -.
DR   SGD; S000002164; PTC1.
DR   VEuPathDB; FungiDB:YDL006W; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   GeneTree; ENSGT00940000158427; -.
DR   HOGENOM; CLU_013173_1_1_1; -.
DR   InParanoid; P35182; -.
DR   OMA; IDDQEAC; -.
DR   OrthoDB; 11028at2759; -.
DR   BioCyc; YEAST:G3O-29437-MONOMER; -.
DR   BioGRID-ORCS; 851558; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P35182; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P35182; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:0000001; P:mitochondrion inheritance; IMP:SGD.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:SGD.
DR   GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IMP:SGD.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 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; Peroxisome;
KW   Protein phosphatase; Reference proteome; Stress response.
FT   CHAIN           1..281
FT                   /note="Protein phosphatase 2C homolog 1"
FT                   /id="PRO_0000057774"
FT   DOMAIN          20..281
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         58
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        53
FT                   /note="Y -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124
FT                   /note="E -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  31550 MW;  FA384D2541B20D50 CRC64;
     MSNHSEILER PETPYDITYR VGVAENKNSK FRRTMEDVHT YVKNFASRLD WGYFAVFDGH
     AGIQASKWCG KHLHTIIEQN ILADETRDVR DVLNDSFLAI DEEINTKLVG NSGCTAAVCV
     LRWELPDSVS DDSMDLAQHQ RKLYTANVGD SRIVLFRNGN SIRLTYDHKA SDTLEMQRVE
     QAGGLIMKSR VNGMLAVTRS LGDKFFDSLV VGSPFTTSVE ITSEDKFLIL ACDGLWDVID
     DQDACELIKD ITEPNEAAKV LVRYALENGT TDNVTVMVVF L
//