PPT1_YEAST
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 03-AUG-2022, entry version 197.
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; 100.
DR DIP; DIP-1525N; -.
DR IntAct; P53043; 15.
DR MINT; P53043; -.
DR STRING; 4932.YGR123C; -.
DR MaxQB; P53043; -.
DR PaxDb; P53043; -.
DR PRIDE; P53043; -.
DR EnsemblFungi; YGR123C_mRNA; YGR123C; YGR123C.
DR GeneID; 853023; -.
DR KEGG; sce:YGR123C; -.
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 BioCyc; YEAST:G3O-30830-MON; -.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
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; 1.25.40.10; -; 1.
DR Gene3D; 3.60.21.10; -; 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; IPR011236; Ser/Thr_PPase_5.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45668:SF5; PTHR45668:SF5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56300; SSF56300; 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
