PP2A1_YEAST
ID PP2A1_YEAST Reviewed; 369 AA.
AC P23594; D6VRL4;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-1 catalytic subunit;
DE EC=3.1.3.16;
GN Name=PPH21; OrderedLocusNames=YDL134C; ORFNames=D2180;
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=LL20;
RX PubMed=2176150; DOI=10.1002/j.1460-2075.1990.tb07883.x;
RA Sneddon A.A., Cohen P.T.W., Stark M.J.R.;
RT "Saccharomyces cerevisiae protein phosphatase 2A performs an essential
RT cellular function and is encoded by two genes.";
RL EMBO J. 9:4339-4346(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=1656215; DOI=10.1128/mcb.11.10.4876-4884.1991;
RA Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.;
RT "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth
RT and bud morphogenesis.";
RL Mol. Cell. Biol. 11:4876-4884(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972577;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1549::aid-yea42>3.0.co;2-s;
RA Woelfl S., Haneman V., Saluz H.P.;
RT "Analysis of a 26,756 bp segment from the left arm of yeast chromosome
RT IV.";
RL Yeast 12:1549-1554(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 METHYLATION AT LEU-369 BY PPM1, AND DEMETHYLATION AT LEU-369 BY PPE1.
RX PubMed=11060018; DOI=10.1093/emboj/19.21.5672;
RA Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.;
RT "Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic
RT subunit promotes its functional association with regulatory subunits in
RT vivo.";
RL EMBO J. 19:5672-5681(2000).
RN [7]
RP METHYLATION BY PPM1.
RX PubMed=11697862; DOI=10.1006/abbi.2001.2558;
RA Kalhor H.R., Luk K., Ramos A., Zobel-Thropp P., Clarke S.;
RT "Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity
RT responsible for modification of the major forms of protein phosphatase 2A
RT in yeast.";
RL Arch. Biochem. Biophys. 395:239-245(2001).
RN [8]
RP INTERACTION WITH TAP42, AND MUTAGENESIS OF LEU-99; GLU-102 AND GLU-103.
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 [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 INTERACTION WITH PPE1 AND RRD2.
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).
RN [11]
RP INTERACTION WITH RRD2 AND TAP42.
RX PubMed=15689491; DOI=10.1091/mbc.e04-09-0797;
RA Zheng Y., Jiang Y.;
RT "The yeast phosphotyrosyl phosphatase activator is part of the Tap42-
RT phosphatase complexes.";
RL Mol. Biol. Cell 16:2119-2127(2005).
CC -!- FUNCTION: Exact function not known, phosphatase 2A performs an
CC essential cellular function.
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 RRD2, which can
CC reactivate PP2Ai by dissociating the catalytic subunit from the
CC complex. Forms a ternary complex with RRD2-TAP42.
CC {ECO:0000269|PubMed:14551259, ECO:0000269|PubMed:15447631,
CC ECO:0000269|PubMed:15689491}.
CC -!- INTERACTION:
CC P23594; P38796: PPE1; NbExp=5; IntAct=EBI-12745, EBI-13775;
CC P23594; Q12461: RRD2; NbExp=7; IntAct=EBI-12745, EBI-32784;
CC P23594; Q04372: TAP42; NbExp=10; IntAct=EBI-12745, EBI-18926;
CC -!- PTM: Reversibly methyl esterified on Leu-369 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. {ECO:0000269|PubMed:11060018,
CC ECO:0000269|PubMed:11697862}.
CC -!- MISCELLANEOUS: Present with 5620 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; X56261; CAA39702.1; -; Genomic_DNA.
DR EMBL; X58856; CAA41656.1; -; Genomic_DNA.
DR EMBL; X96876; CAA65625.1; -; Genomic_DNA.
DR EMBL; Z74182; CAA98707.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11724.1; -; Genomic_DNA.
DR PIR; A41525; PABY21.
DR RefSeq; NP_010147.1; NM_001180193.1.
DR AlphaFoldDB; P23594; -.
DR SMR; P23594; -.
DR BioGRID; 31927; 242.
DR ComplexPortal; CPX-1380; TAP42-RRD2-PPH21 phosphatase complex.
DR ComplexPortal; CPX-1856; Serine/threonine-protein phosphatase PP2A variant 1.
DR ComplexPortal; CPX-1857; Serine/threonine-protein phosphatase PP2A variant 2.
DR DIP; DIP-2282N; -.
DR IntAct; P23594; 27.
DR MINT; P23594; -.
DR STRING; 4932.YDL134C; -.
DR iPTMnet; P23594; -.
DR MaxQB; P23594; -.
DR PaxDb; P23594; -.
DR PRIDE; P23594; -.
DR EnsemblFungi; YDL134C_mRNA; YDL134C; YDL134C.
DR GeneID; 851421; -.
DR KEGG; sce:YDL134C; -.
DR SGD; S000002292; PPH21.
DR VEuPathDB; FungiDB:YDL134C; -.
DR eggNOG; KOG0371; Eukaryota.
DR GeneTree; ENSGT00940000176641; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; P23594; -.
DR OMA; DHINYAF; -.
DR BioCyc; YEAST:G3O-29532-MON; -.
DR PRO; PR:P23594; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P23594; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; 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; IMP:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IGI:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:ComplexPortal.
DR GO; GO:0006417; P:regulation of translation; IPI:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:ComplexPortal.
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..369
FT /note="Serine/threonine-protein phosphatase PP2A-1
FT catalytic subunit"
FT /id="PRO_0000058873"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 369
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000269|PubMed:11060018"
FT MUTAGEN 99
FT /note="L->A: Reduced interaction with TAP42."
FT /evidence="ECO:0000269|PubMed:14551259"
FT MUTAGEN 102
FT /note="E->A: Reduced interaction with TAP42."
FT /evidence="ECO:0000269|PubMed:14551259"
FT MUTAGEN 103
FT /note="E->A: Reduced interaction with TAP42."
FT /evidence="ECO:0000269|PubMed:14551259"
SQ SEQUENCE 369 AA; 41938 MW; D8D5757283C9BBD6 CRC64;
MDTDLDVPMQ DAVTEQLTPT VSEDMDLNNN SSDNNAEEFS VDDLKPGSSG IADHKSSKPL
ELNNTNINQL DQWIEHLSKC EPLSEDDVAR LCKMAVDVLQ FEENVKPINV PVTICGDVHG
QFHDLLELFK IGGPCPDTNY LFMGDYVDRG YYSVETVSYL VAMKVRYPHR ITILRGNHES
RQITQVYGFY DECLRKYGSA NVWKMFTDLF DYFPITALVD NKIFCLHGGL SPMIETIDQV
RELNRIQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGFTF GQDVSEQFNH TNDLSLIARA
HQLVMEGYAW SHQQNVVTIF SAPNYCYRCG NQAAIMEVDE NHNRQFLQYD PSVRPGEPSV
SRKTPDYFL
