ID   PPZ1_YEAST              Reviewed;         692 AA.
AC   P26570; D6VZF8; Q00979;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 5.
DT   27-MAR-2024, entry version 212.
DE   RecName: Full=Serine/threonine-protein phosphatase PP-Z1;
DE            EC=3.1.3.16;
GN   Name=PPZ1; OrderedLocusNames=YML016C; ORFNames=YM9571.02C;
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=M5;
RX   PubMed=1318299; DOI=10.1016/s0021-9258(19)49759-7;
RA   Posas F., Casamayor A., Morral N., Arino J.;
RT   "Molecular cloning and analysis of a yeast protein phosphatase with an
RT   unusual amino-terminal region.";
RL   J. Biol. Chem. 267:11734-11740(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AY926;
RX   PubMed=8396031; DOI=10.1111/j.1432-1033.1993.tb18142.x;
RA   Hughes V., Mueller A., Stark M.J.R., Cohen P.T.W.;
RT   "Both isoforms of protein phosphatase Z are essential for the maintenance
RT   of cell size and integrity in Saccharomyces cerevisiae in response to
RT   osmotic stress.";
RL   Eur. J. Biochem. 216:269-279(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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] OF 345-692.
RX   PubMed=2166691; DOI=10.1016/0014-5793(90)81285-v;
RA   Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J.;
RT   "Protein serine/threonine phosphatases; an expanding family.";
RL   FEBS Lett. 268:355-359(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 389-610.
RX   PubMed=1647215; DOI=10.1016/0167-4781(91)90023-f;
RA   Da Cruz e Silva E.F., Hughes V., McDonald P., Stark M.J.R., Cohen P.T.W.;
RT   "Protein phosphatase 2Bw and protein phosphatase Z are Saccharomyces
RT   cerevisiae enzymes.";
RL   Biochim. Biophys. Acta 1089:269-272(1991).
RN   [7]
RP   INTERACTION WITH SIS2.
RX   PubMed=9636153; DOI=10.1073/pnas.95.13.7357;
RA   de Nadal E., Clotet J., Posas F., Serrano R., Gomez N., Arino J.;
RT   "The yeast halotolerance determinant Hal3p is an inhibitory subunit of the
RT   Ppz1p Ser/Thr protein phosphatase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:7357-7362(1998).
RN   [8]
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   [9]
RP   INTERACTION WITH VHS3.
RX   PubMed=15192104; DOI=10.1074/jbc.m400572200;
RA   Ruiz A., Munoz I., Serrano R., Gonzalez A., Simon E., Arino J.;
RT   "Functional characterization of the Saccharomyces cerevisiae VHS3 gene. A
RT   regulatory subunit of the Ppz1 protein phosphatase with novel, phosphatase-
RT   unrelated functions.";
RL   J. Biol. Chem. 279:34421-34430(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-171; THR-261 AND
RP   SER-265, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222 AND SER-690, 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: Essential for the maintenance of cell size and integrity in
CC       response to osmotic stress.
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: Inhibited by the regulatory subunits VHS3 and
CC       SIS2.
CC   -!- SUBUNIT: Interacts with SIS2 and VHS3, which regulate its activity.
CC       {ECO:0000269|PubMed:15192104, ECO:0000269|PubMed:9636153}.
CC   -!- INTERACTION:
CC       P26570; P36076: CAB3; NbExp=6; IntAct=EBI-13807, EBI-26778;
CC       P26570; P33329: PPZ2; NbExp=3; IntAct=EBI-13807, EBI-13815;
CC       P26570; P36024: SIS2; NbExp=7; IntAct=EBI-13807, EBI-17250;
CC       P26570; Q08438: VHS3; NbExp=4; IntAct=EBI-13807, EBI-30482;
CC   -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from a rabbit cDNA library
CC       and was known as protein phosphatase Z (PP-Z).
CC       {ECO:0000305|PubMed:2166691}.
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DR   EMBL; M86242; AAA34898.1; -; Genomic_DNA.
DR   EMBL; X74135; CAA52232.1; -; Genomic_DNA.
DR   EMBL; Z49810; CAA89936.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09882.1; -; Genomic_DNA.
DR   PIR; S55103; PABY12.
DR   RefSeq; NP_013696.1; NM_001182374.1.
DR   AlphaFoldDB; P26570; -.
DR   SMR; P26570; -.
DR   BioGRID; 35153; 346.
DR   DIP; DIP-557N; -.
DR   IntAct; P26570; 60.
DR   MINT; P26570; -.
DR   STRING; 4932.YML016C; -.
DR   iPTMnet; P26570; -.
DR   MaxQB; P26570; -.
DR   PaxDb; 4932-YML016C; -.
DR   PeptideAtlas; P26570; -.
DR   EnsemblFungi; YML016C_mRNA; YML016C; YML016C.
DR   GeneID; 854992; -.
DR   KEGG; sce:YML016C; -.
DR   AGR; SGD:S000004478; -.
DR   SGD; S000004478; PPZ1.
DR   VEuPathDB; FungiDB:YML016C; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   GeneTree; ENSGT00940000153472; -.
DR   HOGENOM; CLU_004962_3_0_1; -.
DR   InParanoid; P26570; -.
DR   OMA; IHASMEN; -.
DR   OrthoDB; 19833at2759; -.
DR   BioCyc; YEAST:G3O-32620-MONOMER; -.
DR   BioGRID-ORCS; 854992; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P26570; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P26570; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
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:0006883; P:intracellular sodium ion homeostasis; IMP:SGD.
DR   GO; GO:0008104; P:protein localization; IMP:SGD.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011159; PPPtase_PPZ/Ppq1.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF484; SERINE_THREONINE-PROTEIN PHOSPHATASE PP-Z1-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PIRSF; PIRSF000909; PPPtase_PPZ; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Lipoprotein; Manganese; Metal-binding; Myristate;
KW   Phosphoprotein; Protein phosphatase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..692
FT                   /note="Serine/threonine-protein phosphatase PP-Z1"
FT                   /id="PRO_0000058891"
FT   REGION          1..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        480
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         421
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         479
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         528
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         603
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         171
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P33329"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         261
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         690
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        340
FT                   /note="E -> G (in Ref. 1; AAA34898)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440
FT                   /note="S -> A (in Ref. 5; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        649
FT                   /note="E -> K (in Ref. 5; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   692 AA;  77491 MW;  8B7F009521F72C15 CRC64;
     MGNSSSKSSK KDSHSNSSSR NPRPQVSRTE TSHSVKSAKS NKSSRSRRSL PSSSTTNTNS
     NVPDPSTPSK PNLEVNHQRH SSHTNRYHFP SSSHSHSNSQ NELLTTPSSS STKRPSTSRR
     SSYNTKAAAD LPPSMIQMEP KSPILKTNNS STHVSKHKSS YSSTYYENAL TDDDNDDKDN
     DISHTKRFSR SSNSRPSSIR SGSVSRRKSD VTHEEPNNGS YSSNNQENYL VQALTRSNSH
     ASSLHSRKSS FGSDGNTAYS TPLNSPGLSK LTDHSGEYFT SNSTSSLNHH SSRDIYPSKH
     ISNDDDIENS SQLSNIHASM ENVNDKNNNI TDSKKDPNEE FNDIMQSSGN KNAPKKFKKP
     IDIDETIQKL LDAGYAAKRT KNVCLKNNEI LQICIKAREI FLSQPSLLEL SPPVKIVGDV
     HGQYGDLLRL FTKCGFPPSS NYLFLGDYVD RGKQSLETIL LLFCYKIKYP ENFFLLRGNH
     ECANVTRVYG FYDECKRRCN IKIWKTFIDT FNTLPLAAIV AGKIFCVHGG LSPVLNSMDE
     IRHVVRPTDV PDFGLINDLL WSDPTDSPNE WEDNERGVSY CYNKVAINKF LNKFGFDLVC
     RAHMVVEDGY EFFNDRSLVT VFSAPNYCGE FDNWGAVMSV SEGLLCSFEL LDPLDSAALK
     QVMKKGRQER KLANQQQQMM ETSITNDNES QQ
//