PP2A4_YEAST
ID PP2A4_YEAST Reviewed; 368 AA.
AC P32838; D6W1K6; E9P8U5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-like PPG1;
DE EC=3.1.3.16;
GN Name=PPG1; Synonyms=PPG; OrderedLocusNames=YNR032W; ORFNames=N3281;
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].
RX PubMed=7678255; DOI=10.1016/s0021-9258(18)54082-5;
RA Posas F., Clotet J., Muns M.T., Corominas J., Casamayor A., Arino J.;
RT "The gene PPG encodes a novel yeast protein phosphatase involved in
RT glycogen accumulation.";
RL J. Biol. Chem. 268:1349-1354(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH TAP42.
RX PubMed=14551259; DOI=10.1091/mbc.e03-02-0072;
RA Wang H., Wang X., Jiang Y.;
RT "Interaction with Tap42 is required for the essential function of Sit4 and
RT type 2A phosphatases.";
RL Mol. Biol. Cell 14:4342-4351(2003).
RN [6]
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 [7]
RP INTERACTION WITH PPE1 AND RRD1.
RX PubMed=15447631; DOI=10.1042/bj20040887;
RA Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V.,
RA Goris J.;
RT "Specific interactions of PP2A and PP2A-like phosphatases with the yeast
RT PTPA homologues, Ypa1 and Ypa2.";
RL Biochem. J. 386:93-102(2005).
CC -!- FUNCTION: Involved in glycogen accumulation.
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 -!- SUBUNIT: Inactivated in a complex with phosphatase methylesterase PPE1
CC (PP2Ai). Interacts with phosphatase 2A activator RRD1, which can
CC reactivate PP2Ai by dissociating the catalytic subunit from the
CC complex. Interacts with TAP42. {ECO:0000269|PubMed:14551259,
CC ECO:0000269|PubMed:15447631}.
CC -!- PTM: Reversibly methyl esterified on Leu-368 by leucine carboxyl
CC methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1
CC (PPE1). Carboxyl methylation influences the affinity of the catalytic
CC subunit for the different regulatory subunits, thereby modulating the
CC PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC localization.
CC -!- MISCELLANEOUS: Present with 1960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC {ECO:0000305}.
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DR EMBL; M94269; AAA34895.1; -; Genomic_DNA.
DR EMBL; Z71647; CAA96312.1; -; Genomic_DNA.
DR EMBL; AY558021; AAS56347.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10572.1; -; Genomic_DNA.
DR PIR; S63363; S63363.
DR RefSeq; NP_014429.3; NM_001183209.3.
DR AlphaFoldDB; P32838; -.
DR SMR; P32838; -.
DR BioGRID; 35856; 219.
DR DIP; DIP-1523N; -.
DR IntAct; P32838; 9.
DR MINT; P32838; -.
DR STRING; 4932.YNR032W; -.
DR MaxQB; P32838; -.
DR PaxDb; P32838; -.
DR PRIDE; P32838; -.
DR TopDownProteomics; P32838; -.
DR EnsemblFungi; YNR032W_mRNA; YNR032W; YNR032W.
DR GeneID; 855766; -.
DR KEGG; sce:YNR032W; -.
DR SGD; S000005315; PPG1.
DR VEuPathDB; FungiDB:YNR032W; -.
DR eggNOG; KOG0372; Eukaryota.
DR GeneTree; ENSGT00960000189235; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; P32838; -.
DR OMA; EVNNMSH; -.
DR BioCyc; YEAST:G3O-33343-MON; -.
DR PRO; PR:P32838; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P32838; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA: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; ISS:SGD.
DR GO; GO:0061509; P:asymmetric protein localization to old mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0005977; P:glycogen metabolic process; 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; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 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; Methylation; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..368
FT /note="Serine/threonine-protein phosphatase PP2A-like PPG1"
FT /id="PRO_0000058876"
FT ACT_SITE 111
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 126
FT /note="C -> S (in Ref. 1; AAA34895)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="D -> G (in Ref. 4; AAS56347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 42433 MW; 1B326BBC41A67481 CRC64;
MELDECLERL YKAQLLPEVT VRALCFKLKE MLVKESNVIH IQTPVTVVGD MHGQFHDMLE
IFQIGGPVPD TNYLFLGDYV DRGLYSVETI MLLIVLKLRY PSRIHLLRGN HESRQITQSY
GFYTECLNKY GGNSRVWQYL TDIFDYLVLC CIIDDEIFCV HGGLSPNVQT IDQIKIIDRF
REIPHDGAMA DLVWSDPEEN NNPTLDHPDN SGQHFQVSPR GAGYTFGRSV VEKFLRMNDM
NRIYRAHQLC NEGYQIYFDG LVTTVWSAPN YCYRCGNKAS ILELYSKDQF YFNVFEEAPE
NKLLKENSMN DNALEDSISN PVANRKLIAD YFEDDSASAD GSTDPEMYIF SDVYQARSAS
NRHVDYFL
