PP2A2_ARATH
ID PP2A2_ARATH Reviewed; 306 AA.
AC Q07098;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-2 catalytic subunit;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2A isoform 2;
GN Name=PP2A2 {ECO:0000303|PubMed:17368080}; Synonyms=PP2A1;
GN OrderedLocusNames=At1g10430; ORFNames=T10O24.4;
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].
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].
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 INTERACTION WITH PP2AA1.
RX PubMed=10091592; DOI=10.1046/j.1432-1327.1999.00154.x;
RA Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S.,
RA Rundle S.J.;
RT "Molecular characterization of the B' regulatory subunit gene family of
RT Arabidopsis protein phosphatase 2A.";
RL Eur. J. Biochem. 260:127-136(1999).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY ABSCISIC ACID.
RX PubMed=17617176; DOI=10.1111/j.1365-313x.2007.03179.x;
RA Pernas M., Garcia-Casado G., Rojo E., Solano R., Sanchez-Serrano J.J.;
RT "A protein phosphatase 2A catalytic subunit is a negative regulator of
RT abscisic acid signalling.";
RL Plant J. 51:763-778(2007).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=22642987; DOI=10.1093/pcp/pcs081;
RA Wen F., Wang J., Xing D.;
RT "A protein phosphatase 2A catalytic subunit modulates blue light-induced
RT chloroplast avoidance movements through regulating actin cytoskeleton in
RT Arabidopsis.";
RL Plant Cell Physiol. 53:1366-1379(2012).
RN [9]
RP INTERACTION WITH HDA14, AND SUBCELLULAR LOCATION.
RX PubMed=22404109; DOI=10.1111/j.1365-313x.2012.04984.x;
RA Tran H.T., Nimick M., Uhrig R.G., Templeton G., Morrice N., Gourlay R.,
RA DeLong A., Moorhead G.B.;
RT "Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-tubulin
RT deacetylase that associates with PP2A and enriches in the microtubule
RT fraction with the putative histone acetyltransferase ELP3.";
RL Plant J. 71:263-272(2012).
RN [10]
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 [11]
RP FUNCTION, INTERACTION WITH B'THETA, AND SUBCELLULAR LOCATION.
RX PubMed=25489022; DOI=10.1104/pp.114.254409;
RA Kataya A.R., Heidari B., Hagen L., Kommedal R., Slupphaug G., Lillo C.;
RT "Protein phosphatase 2A holoenzyme is targeted to peroxisomes by
RT piggybacking and positively affects peroxisomal beta-oxidation.";
RL Plant Physiol. 167:493-506(2015).
RN [12]
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 [13]
RP FUNCTION.
RX PubMed=28656346; DOI=10.1007/s00425-017-2726-4;
RA Creighton M.T., Sanmartin M., Kataya A.R.A., Averkina I.O., Heidari B.,
RA Nemie-Feyissa D., Sanchez-Serrano J.J., Lillo C.;
RT "Light regulation of nitrate reductase by catalytic subunits of protein
RT phosphatase 2A.";
RL Planta 246:701-710(2017).
RN [14]
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 -!- FUNCTION: Dephosphorylates and activates the actin-depolymerizing
CC factor ADF1, which, in turn, regulates actin cytoskeleton remodeling
CC and is involved in the blue light photoreceptor PHOT2-mediated
CC chloroplast avoidance movements (PubMed:22642987). Associates with the
CC serine/threonine-protein phosphatase PP2A regulatory subunits A and B'
CC to positively regulates beta-oxidation of fatty acids and protoauxins
CC in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related
CC proteins (PubMed:25489022). Acts as negative regulator of abscisic acid
CC (ABA) signaling. May regulate ABA-dependent gene expression
CC (PubMed:17617176). Involved in the light-dependent activation of
CC nitrate reductase (PubMed:28656346). {ECO:0000269|PubMed:17617176,
CC ECO:0000269|PubMed:22642987, ECO:0000269|PubMed:25489022,
CC ECO:0000269|PubMed:28656346}.
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;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P67775};
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) (Probable). Interacts
CC with B'THETA (PubMed:25489022). Interacts with HDA14 (PubMed:22404109).
CC Interacts with SRK2E/OST1 (PubMed:26175513). Interacts with TAP46.
CC {ECO:0000269|PubMed:22404109, ECO:0000269|PubMed:24357600,
CC ECO:0000269|PubMed:25489022, ECO:0000269|PubMed:26175513,
CC ECO:0000305|PubMed:10091592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22404109,
CC ECO:0000269|PubMed:25489022}. Nucleus {ECO:0000269|PubMed:22404109}.
CC Peroxisome {ECO:0000269|PubMed:25489022}. Note=Interacts with B'THETA
CC in the cytosol and peroxisomal import occurs by a piggybacking
CC transport. {ECO:0000269|PubMed:25489022}.
CC -!- TISSUE SPECIFICITY: Expressed in root meristem, emerging lateral roots,
CC leaf vasculature, stipules, guard cells, anthers and pollen grains.
CC {ECO:0000269|PubMed:17617176}.
CC -!- INDUCTION: Induced by abscisic acid (ABA).
CC {ECO:0000269|PubMed:17617176}.
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; M96733; AAA32848.1; -; mRNA.
DR EMBL; AC007067; AAD39564.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28579.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59883.1; -; Genomic_DNA.
DR EMBL; AY059847; AAL24329.1; -; mRNA.
DR EMBL; AY093267; AAM13266.1; -; mRNA.
DR PIR; S31162; S31162.
DR RefSeq; NP_001322206.1; NM_001331905.1.
DR RefSeq; NP_172514.1; NM_100918.3.
DR AlphaFoldDB; Q07098; -.
DR SMR; Q07098; -.
DR BioGRID; 22823; 16.
DR IntAct; Q07098; 2.
DR STRING; 3702.AT1G10430.1; -.
DR PaxDb; Q07098; -.
DR PRIDE; Q07098; -.
DR ProteomicsDB; 248968; -.
DR EnsemblPlants; AT1G10430.1; AT1G10430.1; AT1G10430.
DR EnsemblPlants; AT1G10430.2; AT1G10430.2; AT1G10430.
DR GeneID; 837583; -.
DR Gramene; AT1G10430.1; AT1G10430.1; AT1G10430.
DR Gramene; AT1G10430.2; AT1G10430.2; AT1G10430.
DR KEGG; ath:AT1G10430; -.
DR Araport; AT1G10430; -.
DR TAIR; locus:2194626; AT1G10430.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q07098; -.
DR OMA; INCPLET; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q07098; -.
DR PRO; PR:Q07098; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q07098; baseline and differential.
DR Genevisible; Q07098; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA: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; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009903; P:chloroplast avoidance movement; IMP:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:TAIR.
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 Abscisic acid signaling pathway; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Methylation; Nucleus; Peroxisome; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..306
FT /note="Serine/threonine-protein phosphatase PP2A-2
FT catalytic subunit"
FT /id="PRO_0000058852"
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"
SQ SEQUENCE 306 AA; 34934 MW; B2DCB1B3C2CDD54F CRC64;
MPSNGDLDRQ IEQLMECKPL SEADVRTLCD QARAILVEEY NVQPVKCPVT VCGDIHGQFY
DLIELFRIGG NAPDTNYLFM GDYVDRGYYS VETVSLLVAL KVRYRDRLTI LRGNHESRQI
TQVYGFYDEC LRKYGNANVW KYFTDLFDYL PLTALIESQV FCLHGGLSPS LDTLDNIRSL
DRIQEVPHEG PMCDLLWSDP DDRCGWGISP RGAGYTFGQD IAAQFNHNNG LSLISRAHQL
VMEGFNWCQD KNVVTVFSAP NYCYRCGNMA AILEIGENME QNFLQFDPAP RQVEPDTTRK
TPDYFL
