ID   PP2A1_ARATH             Reviewed;         306 AA.
AC   Q07099; Q3ECM1;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Serine/threonine-protein phosphatase PP2A-1 catalytic subunit;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase 2A isoform 1;
GN   Name=PP2A1 {ECO:0000303|PubMed:17368080}; Synonyms=PP2A2;
GN   OrderedLocusNames=At1g59830; ORFNames=F23H11.15;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia GL1;
RX   PubMed=8382968; DOI=10.1007/bf00028805;
RA   Arino J., Perez-Callejon E., Cunillera N., Camps M., Posas F., Ferrer A.;
RT   "Protein phosphatases in higher plants: multiplicity of type 2A
RT   phosphatases in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 21:475-485(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17368080; DOI=10.1016/j.tplants.2007.03.003;
RA   Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.;
RT   "Arabidopsis PPP family of serine/threonine phosphatases.";
RL   Trends Plant Sci. 12:169-176(2007).
RN   [6]
RP   INTERACTION WITH TAF12B.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=17526916; DOI=10.1093/jxb/erm080;
RA   Robles L.M., Wampole J.S., Christians M.J., Larsen P.B.;
RT   "Arabidopsis enhanced ethylene response 4 encodes an EIN3-interacting TFIID
RT   transcription factor required for proper ethylene response, including ERF1
RT   induction.";
RL   J. Exp. Bot. 58:2627-2639(2007).
RN   [7]
RP   INTERACTION WITH TAP46.
RX   PubMed=24357600; DOI=10.1104/pp.113.233684;
RA   Hu R., Zhu Y., Shen G., Zhang H.;
RT   "TAP46 plays a positive role in the ABSCISIC ACID INSENSITIVE5-regulated
RT   gene expression in Arabidopsis.";
RL   Plant Physiol. 164:721-734(2014).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SRK2E/OST1.
RX   PubMed=26175513; DOI=10.1104/pp.15.00575;
RA   Waadt R., Manalansan B., Rauniyar N., Munemasa S., Booker M.A., Brandt B.,
RA   Waadt C., Nusinow D.A., Kay S.A., Kunz H.H., Schumacher K., DeLong A.,
RA   Yates J.R. III, Schroeder J.I.;
RT   "Identification of Open Stomata1-interacting proteins reveals interactions
RT   with sucrose non-fermenting1-related protein kinases2 and with type 2a
RT   protein phosphatases that function in abscisic acid responses.";
RL   Plant Physiol. 169:760-779(2015).
RN   [9]
RP   METHYLATION AT LEU-306.
RX   PubMed=28741704; DOI=10.1111/pce.13038;
RA   Creighton M.T., Kolton A., Kataya A.R.A., Maple-Groedem J., Averkina I.O.,
RA   Heidari B., Lillo C.;
RT   "Methylation of protein phosphatase 2A-influence of regulators and
RT   environmental stress factors.";
RL   Plant Cell Environ. 40:2347-2358(2017).
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: PP2A consists of a common heterodimeric core enzyme, composed
CC       of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC       regulatory subunit (subunit A), that associates with a variety of
CC       regulatory subunits such as subunits B (the R2/B/PR55/B55,
CC       R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) (By similarity).
CC       Interacts with TAF12B (By similarity) (PubMed:17526916). Interacts with
CC       SRK2E/OST1 (PubMed:26175513). Interacts with TAP46. {ECO:0000250,
CC       ECO:0000250|UniProtKB:P62714, ECO:0000269|PubMed:17526916,
CC       ECO:0000269|PubMed:24357600, ECO:0000269|PubMed:26175513}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q07099-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q07099-2; Sequence=VSP_028727, VSP_028728;
CC   -!- PTM: Reversibly methyl esterified on Leu-306 by leucine carboxyl
CC       methyltransferase 1 (LCMT1) and pectin methylesterase 1 (PME1).
CC       Carboxyl methylation influences the affinity of the catalytic subunit
CC       for the different regulatory subunits, thereby modulating the PP2A
CC       holoenzyme's substrate specificity, enzyme activity and cellular
CC       localization. {ECO:0000305|PubMed:28741704}.
CC   -!- PTM: Phosphorylation of either threonine (by autophosphorylation-
CC       activated protein kinase) or tyrosine results in inactivation of the
CC       phosphatase. Auto-dephosphorylation has been suggested as a mechanism
CC       for reactivation. {ECO:0000250|UniProtKB:P67774}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M96732; AAA32847.1; -; mRNA.
DR   EMBL; AC007258; AAD39326.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33622.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33623.1; -; Genomic_DNA.
DR   EMBL; AY063942; AAL36298.1; -; mRNA.
DR   EMBL; AY096543; AAM20193.1; -; mRNA.
DR   PIR; S31161; S31161.
DR   RefSeq; NP_176192.1; NM_104676.5. [Q07099-1]
DR   RefSeq; NP_974050.1; NM_202321.2. [Q07099-2]
DR   AlphaFoldDB; Q07099; -.
DR   SMR; Q07099; -.
DR   BioGRID; 27501; 16.
DR   IntAct; Q07099; 1.
DR   STRING; 3702.Q07099; -.
DR   PaxDb; 3702-AT1G59830-1; -.
DR   ProteomicsDB; 248967; -. [Q07099-1]
DR   EnsemblPlants; AT1G59830.1; AT1G59830.1; AT1G59830. [Q07099-1]
DR   EnsemblPlants; AT1G59830.2; AT1G59830.2; AT1G59830. [Q07099-2]
DR   GeneID; 842276; -.
DR   Gramene; AT1G59830.1; AT1G59830.1; AT1G59830. [Q07099-1]
DR   Gramene; AT1G59830.2; AT1G59830.2; AT1G59830. [Q07099-2]
DR   KEGG; ath:AT1G59830; -.
DR   Araport; AT1G59830; -.
DR   TAIR; AT1G59830; PP2A-1.
DR   eggNOG; KOG0371; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; Q07099; -.
DR   OMA; CEAGYLW; -.
DR   OrthoDB; 19833at2759; -.
DR   PhylomeDB; Q07099; -.
DR   PRO; PR:Q07099; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q07099; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
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:TAIR.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF16; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A-1 CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   Genevisible; Q07099; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW   Methylation; Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..306
FT                   /note="Serine/threonine-protein phosphatase PP2A-1
FT                   catalytic subunit"
FT                   /id="PRO_0000058853"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P67775"
FT   BINDING         56
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P67775"
FT   BINDING         82
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P67775"
FT   BINDING         82
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P67775"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P67775"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P67775"
FT   BINDING         238
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P67775"
FT   MOD_RES         306
FT                   /note="Leucine methyl ester"
FT                   /evidence="ECO:0000305|PubMed:28741704"
FT   VAR_SEQ         250..262
FT                   /note="EKNVVTVFSAPNY -> VYNMCITIDWHMC (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_028727"
FT   VAR_SEQ         263..306
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_028728"
SQ   SEQUENCE   306 AA;  34961 MW;  579427029D41A1C1 CRC64;
     MPLNGDLDRQ IEQLMECKPL GEADVKILCD QAKAILVEEY NVQPVKCPVT VCGDIHGQFY
     DLIELFRIGG NAPDTNYLFM GDYVDRGYYS VETVSLLVAL KVRYRDRLTI LRGNHESRQI
     TQVYGFYDEC LRKYGNANVW KYFTDLFDYL PLTALIESQV FCLHGGLSPS LDTLDNIRSL
     DRIQEVPHEG PMCDLLWSDP DDRCGWGISP RGAGYTFGQD IATQFNHNNG LSLISRAHQL
     VMEGYNWCQE KNVVTVFSAP NYCYRCGNMA AILEIGEKME QNFLQFDPAP RQVEPDTTRK
     TPDYFL
//