ID   PPT1_YEAST              Reviewed;         513 AA.
AC   P53043; D6VUQ5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Serine/threonine-protein phosphatase T;
DE            Short=PPT;
DE            EC=3.1.3.16;
GN   Name=PPT1; OrderedLocusNames=YGR123C; ORFNames=G6347;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7925273; DOI=10.1002/j.1460-2075.1994.tb06748.x;
RA   Chen M.X., McPartlin A.E., Brown L., Chen Y.H., Barker H.M., Cohen P.T.W.;
RT   "A novel human protein serine/threonine phosphatase, which possesses four
RT   tetratricopeptide repeat motifs and localizes to the nucleus.";
RL   EMBO J. 13:4278-4290(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9046098;
RX   DOI=10.1002/(sici)1097-0061(199702)13:2<171::aid-yea57>3.0.co;2-v;
RA   van Dyck L., Tettelin H., Purnelle B., Goffeau A.;
RT   "An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown
RT   open reading frames, the gene for an Asn synthase, remnants of Ty and three
RT   tRNA genes.";
RL   Yeast 13:171-176(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-277.
RX   PubMed=1321058; DOI=10.1016/0014-5793(92)80836-6;
RA   Chen M.X., Chen Y.H., Cohen P.T.W.;
RT   "Polymerase chain reactions using Saccharomyces, Drosophila and human DNA
RT   predict a large family of protein serine/threonine phosphatases.";
RL   FEBS Lett. 306:54-58(1992).
RN   [7]
RP   CHARACTERIZATION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=12694636; DOI=10.1186/1471-2121-4-3;
RA   Jeong J.-Y., Johns J., Sinclair C., Park J.-M., Rossie S.;
RT   "Characterization of Saccharomyces cerevisiae protein Ser/Thr phosphatase
RT   T1 and comparison to its mammalian homolog PP5.";
RL   BMC Cell Biol. 4:3-3(2003).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [9]
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   [10]
RP   FUNCTION, INTERACTION WITH HSP82, AND MUTAGENESIS OF HIS-311.
RX   PubMed=16407978; DOI=10.1038/sj.emboj.7600930;
RA   Wandinger S.K., Suhre M.H., Wegele H., Buchner J.;
RT   "The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone
RT   Hsp90.";
RL   EMBO J. 25:367-376(2006).
RN   [11]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16442612; DOI=10.1016/j.ijbiomac.2005.12.019;
RA   Suhre M.H., Wegele H., Wandinger S.K.;
RT   "Expression, purification and refolding of the phosphatase domain of
RT   protein phosphatase 1 (Ppt1) from Saccharomyces cerevisiae.";
RL   Int. J. Biol. Macromol. 39:23-28(2006).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 179-513.
RG   Midwest center for structural genomics (MCSG);
RT   "Structure of protein serine/threonine phosphatase from Saccharomyces
RT   cerevisiae with similarity to human phosphatase PP5.";
RL   Submitted (JUL-2011) to the PDB data bank.
CC   -!- FUNCTION: Protein phosphatase that specifically binds to and
CC       dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82).
CC       Dephosphorylation positively regulates the Hsp90 chaperone machinery.
CC       {ECO:0000269|PubMed:16407978}.
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Stimulated by arachidonic acid and other
CC       unsaturated fatty acids, and by arachidoyl coenzyme A.
CC       {ECO:0000269|PubMed:12694636}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=34 mM for p-nitrophenylphosphate {ECO:0000269|PubMed:16442612};
CC       pH dependence:
CC         Optimum pH is 7.8. {ECO:0000269|PubMed:16442612};
CC   -!- SUBUNIT: Interacts (via TPR repeats) with HSP82 (via C-terminal MEEVD
CC       pentapeptide). {ECO:0000269|PubMed:16407978}.
CC   -!- INTERACTION:
CC       P53043; P15108: HSC82; NbExp=2; IntAct=EBI-13796, EBI-8666;
CC       P53043; P02829: HSP82; NbExp=8; IntAct=EBI-13796, EBI-8659;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12694636,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Expression peaks in early log phase and decreases
CC       dramatically during the stationary phase (at protein level).
CC       {ECO:0000269|PubMed:12694636}.
CC   -!- DOMAIN: The TPR repeats mediate protein-protein interactions with
CC       substrate proteins, but also autoinhibit PPT1 phosphatase activity.
CC   -!- MISCELLANEOUS: Present with 6990 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA61596.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X89417; CAA61596.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X83099; CAA58158.1; -; Genomic_DNA.
DR   EMBL; Z72908; CAA97134.1; -; Genomic_DNA.
DR   EMBL; AY558095; AAS56421.1; -; Genomic_DNA.
DR   EMBL; S39959; AAB22462.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08216.1; -; Genomic_DNA.
DR   PIR; S52571; S52571.
DR   RefSeq; NP_011639.3; NM_001181252.3.
DR   PDB; 3ICF; X-ray; 2.30 A; A/B=179-513.
DR   PDBsum; 3ICF; -.
DR   AlphaFoldDB; P53043; -.
DR   SMR; P53043; -.
DR   BioGRID; 33370; 104.
DR   DIP; DIP-1525N; -.
DR   IntAct; P53043; 15.
DR   MINT; P53043; -.
DR   STRING; 4932.YGR123C; -.
DR   MaxQB; P53043; -.
DR   PaxDb; 4932-YGR123C; -.
DR   PeptideAtlas; P53043; -.
DR   EnsemblFungi; YGR123C_mRNA; YGR123C; YGR123C.
DR   GeneID; 853023; -.
DR   KEGG; sce:YGR123C; -.
DR   AGR; SGD:S000003355; -.
DR   SGD; S000003355; PPT1.
DR   VEuPathDB; FungiDB:YGR123C; -.
DR   eggNOG; KOG0376; Eukaryota.
DR   GeneTree; ENSGT00940000158785; -.
DR   HOGENOM; CLU_004962_5_2_1; -.
DR   InParanoid; P53043; -.
DR   OMA; NHFFMSR; -.
DR   OrthoDB; 1107740at2759; -.
DR   BioCyc; YEAST:G3O-30830-MONOMER; -.
DR   Reactome; R-SCE-8939211; ESR-mediated signaling.
DR   BioGRID-ORCS; 853023; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P53043; -.
DR   PRO; PR:P53043; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53043; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; 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:0006470; P:protein dephosphorylation; IDA:SGD.
DR   CDD; cd07417; MPP_PP5_C; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041753; PP5_C.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..513
FT                   /note="Serine/threonine-protein phosphatase T"
FT                   /id="PRO_0000058898"
FT   REPEAT          12..45
FT                   /note="TPR 1"
FT   REPEAT          46..79
FT                   /note="TPR 2"
FT   REPEAT          80..113
FT                   /note="TPR 3"
FT   REGION          188..513
FT                   /note="Catalytic"
FT   ACT_SITE        311
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         434
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         311
FT                   /note="H->A: Loss of phosphatase activity."
FT                   /evidence="ECO:0000269|PubMed:16407978"
FT   HELIX           192..201
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           211..226
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          243..247
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           254..264
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          271..275
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          280..283
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           286..299
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   TURN            301..303
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          304..306
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           314..320
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           322..329
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           332..342
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          347..351
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   TURN            352..354
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          355..357
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           370..374
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          384..386
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           387..393
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          398..404
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          411..413
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           415..424
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          428..432
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          439..444
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           445..447
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          449..452
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   HELIX           458..460
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          465..471
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   TURN            480..482
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   STRAND          488..493
FT                   /evidence="ECO:0007829|PDB:3ICF"
FT   TURN            503..506
FT                   /evidence="ECO:0007829|PDB:3ICF"
SQ   SEQUENCE   513 AA;  57995 MW;  6966DA22340A5793 CRC64;
     MSTPTAADRA KALERKNEGN VFVKEKHFLK AIEKYTEAID LDSTQSIYFS NRAFAHFKVD
     NFQSALNDCD EAIKLDPKNI KAYHRRALSC MALLEFKKAR KDLNVLLKAK PNDPAATKAL
     LTCDRFIREE RFRKAIGGAE NEAKISLCQT LNLSSFDANA DLANYEGPKL EFEQLYDDKN
     AFKGAKIKNM SQEFISKMVN DLFLKGKYLP KKYVAAIISH ADTLFRQEPS MVELENNSTP
     DVKISVCGDT HGQFYDVLNL FRKFGKVGPK HTYLFNGDFV DRGSWSCEVA LLFYCLKILH
     PNNFFLNRGN HESDNMNKIY GFEDECKYKY SQRIFNMFAQ SFESLPLATL INNDYLVMHG
     GLPSDPSATL SDFKNIDRFA QPPRDGAFME LLWADPQEAN GMGPSQRGLG HAFGPDITDR
     FLRNNKLRKI FRSHELRMGG VQFEQKGKLM TVFSAPNYCD SQGNLGGVIH VVPGHGILQA
     GRNDDQNLII ETFEAVEHPD IKPMAYSNGG FGL
//