PPZ1_YEAST
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 03-AUG-2022, entry version 205.
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; 333.
DR DIP; DIP-557N; -.
DR IntAct; P26570; 60.
DR MINT; P26570; -.
DR STRING; 4932.YML016C; -.
DR iPTMnet; P26570; -.
DR MaxQB; P26570; -.
DR PaxDb; P26570; -.
DR PRIDE; P26570; -.
DR EnsemblFungi; YML016C_mRNA; YML016C; YML016C.
DR GeneID; 854992; -.
DR KEGG; sce:YML016C; -.
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 BioCyc; YEAST:G3O-32620-MON; -.
DR PRO; PR:P26570; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P26570; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA: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:cellular sodium ion homeostasis; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
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 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; SSF56300; 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
