PPQ1_YEAST
ID PPQ1_YEAST Reviewed; 549 AA.
AC P32945; D6W3I9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Serine/threonine-protein phosphatase PPQ;
DE EC=3.1.3.16;
GN Name=PPQ1; Synonyms=SAL6; OrderedLocusNames=YPL179W;
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=8269960; DOI=10.1111/j.1432-1033.1993.tb18423.x;
RA Chen M.X., Chen Y.H., Cohen P.T.W.;
RT "PPQ, a novel protein phosphatase containing a Ser + Asn-rich amino-
RT terminal domain, is involved in the regulation of protein synthesis.";
RL Eur. J. Biochem. 218:689-699(1993).
RN [2]
RP ERRATUM OF PUBMED:8269960.
RA Chen M.X., Chen Y.H., Cohen P.T.W.;
RL Eur. J. Biochem. 221:1133-1133(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=7851758; DOI=10.1093/genetics/138.3.597;
RA Vincent A., Newnam G.P., Liebman S.W.;
RT "The yeast translational allosuppressor, SAL6: a new member of the PP1-like
RT phosphatase family with a long serine-rich N-terminal extension.";
RL Genetics 138:597-607(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-328.
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 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
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: Phosphatase involved in the regulation of protein synthesis.
CC Affects translational accuracy.
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 -!- INTERACTION:
CC P32945; P36047: SDS22; NbExp=3; IntAct=EBI-13787, EBI-16783;
CC -!- MISCELLANEOUS: Present with 319 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X75485; CAA53214.1; -; Genomic_DNA.
DR EMBL; U00795; AAC48924.1; -; Genomic_DNA.
DR EMBL; Z73535; CAA97886.1; -; Genomic_DNA.
DR EMBL; S39958; AAB22461.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11255.1; -; Genomic_DNA.
DR PIR; S39533; S39533.
DR RefSeq; NP_015146.1; NM_001183993.1.
DR AlphaFoldDB; P32945; -.
DR SMR; P32945; -.
DR BioGRID; 36003; 170.
DR DIP; DIP-5504N; -.
DR IntAct; P32945; 4.
DR MINT; P32945; -.
DR STRING; 4932.YPL179W; -.
DR iPTMnet; P32945; -.
DR MaxQB; P32945; -.
DR PaxDb; P32945; -.
DR PRIDE; P32945; -.
DR EnsemblFungi; YPL179W_mRNA; YPL179W; YPL179W.
DR GeneID; 855923; -.
DR KEGG; sce:YPL179W; -.
DR SGD; S000006100; PPQ1.
DR VEuPathDB; FungiDB:YPL179W; -.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_4_1_1; -.
DR InParanoid; P32945; -.
DR OMA; DRFFMLR; -.
DR BioCyc; YEAST:G3O-34074-MON; -.
DR PRO; PR:P32945; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32945; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0090029; P:negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; 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; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..549
FT /note="Serine/threonine-protein phosphatase PPQ"
FT /id="PRO_0000058893"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 362
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 549 AA; 61420 MW; 1E26D05E2865A8C1 CRC64;
MRRSPSRSNN NFAVPNCSTN SNSSQQQLTT PSDDLNSNEP NDPDDSRSLP TIKKFNNKHS
INNYNTLASA GKNNNNKRAS NDNLLIPGEN AHKQKIYTKD ENLKSLYLDI DVSVAKALSS
SATAPKLINT ARTSSTTTAT TSNNILTSPS YRESNYSSPS SYSFSSYYSS ATSASSSTSS
FLKSSGLSSR VKSPSSSVKA GSFGAPSSPT SGIPNPKSSK KPIFLRRYSH DTSSNEGLDI
DVAIEKLLQV GESREITKTS KKKNFPFHSW EIQLICYHAR EIFLNQPTLL RLQAPIKVVG
DVHGQFNDLL RILKLSGVPS DTNYLFLGDY VDRGKNSLET ILLLLCYKIK YKDNFFMLRG
NHESANVTKM YGFYDECKRR LSSKVWKMFV DVFNTLPLAA IIQDKIFCVH GGISPDLHDM
KQIEKVARPT DIPESGLVTD LLWSDPDPQV TDWSENDRGV SYTFSKRNVL DFCAKFKFDL
ILRGHMVVED GYEFFARKKF VTIFSAPNYC GEFHNWGAVM SVTTGMMCSF ELLKPRALKN
KKKLYKTKV
