PP2A3_ARATH
ID PP2A3_ARATH Reviewed; 313 AA.
AC Q07100; Q7G9R3; Q9ZRF6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-3 catalytic subunit;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2A isoform 3;
GN Name=PP2A3 {ECO:0000303|PubMed:9524239};
GN Synonyms=PP2A4 {ECO:0000303|PubMed:17368080}; OrderedLocusNames=At2g42500;
GN ORFNames=MHK10.22;
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; TISSUE=Leaf;
RX PubMed=7948902; DOI=10.1007/bf00039564;
RA Casamayor A., Perez-Callejon E., Pujol G., Arino J., Ferrer A.;
RT "Molecular characterization of a fourth isoform of the catalytic subunit of
RT protein phosphatase 2A from Arabidopsis thaliana.";
RL Plant Mol. Biol. 26:523-528(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9524239; DOI=10.1016/s0378-1119(98)00013-4;
RA Perez-Callejon E., Casamayor A., Pujol G., Camps M., Ferrer A., Arino J.;
RT "Molecular cloning and characterization of two phosphatase 2A catalytic
RT subunit genes from Arabidopsis thaliana.";
RL Gene 209:105-112(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-313.
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 [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 INTERACTION WITH TAP46.
RX PubMed=21216945; DOI=10.1105/tpc.110.074005;
RA Ahn C.S., Han J.-A., Lee H.-S., Lee S., Pai H.-S.;
RT "The PP2A regulatory subunit Tap46, a component of the TOR signaling
RT pathway, modulates growth and metabolism in plants.";
RL Plant Cell 23:185-209(2011).
RN [9]
RP FUNCTION.
RX PubMed=23167545; DOI=10.1111/tpj.12078;
RA Ballesteros I., Dominguez T., Sauer M., Paredes P., Duprat A., Rojo E.,
RA Sanmartin M., Sanchez-Serrano J.J.;
RT "Specialized functions of the PP2A subfamily II catalytic subunits PP2A-C3
RT and PP2A-C4 in the distribution of auxin fluxes and development in
RT Arabidopsis.";
RL Plant J. 73:862-872(2013).
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, AND INTERACTION WITH ACR4.
RX PubMed=26792519; DOI=10.1073/pnas.1525122113;
RA Yue K., Sandal P., Williams E.L., Murphy E., Stes E., Nikonorova N.,
RA Ramakrishna P., Czyzewicz N., Montero-Morales L., Kumpf R., Lin Z.,
RA van de Cotte B., Iqbal M., Van Bel M., Van De Slijke E., Meyer M.R.,
RA Gadeyne A., Zipfel C., De Jaeger G., Van Montagu M., Van Damme D.,
RA Gevaert K., Rao A.G., Beeckman T., De Smet I.;
RT "PP2A-3 interacts with ACR4 and regulates formative cell division in the
RT Arabidopsis root.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:1447-1452(2016).
RN [12]
RP INTERACTION WITH SIC/RON3.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=26888284; DOI=10.1073/pnas.1501343112;
RA Karampelias M., Neyt P., De Groeve S., Aesaert S., Coussens G., Rolcik J.,
RA Bruno L., De Winne N., Van Minnebruggen A., Van Montagu M., Ponce M.R.,
RA Micol J.L., Friml J., De Jaeger G., Van Lijsebettens M.;
RT "ROTUNDA3 function in plant development by phosphatase 2A-mediated
RT regulation of auxin transporter recycling.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:2768-2773(2016).
RN [13]
RP METHYLATION AT LEU-313.
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: Functions redundantly with PP2A4, and is involved in
CC establishing auxin gradients, apical-basal axis of polarity and root
CC and shoot apical meristem during embryogenesis. May dephosphorylate
CC PIN1 and regulate its subcellular distribution for polar auxin
CC transport (PubMed:23167545). Involved in the regulation of formative
CC cell division in roots by dephosphorylating ACR4 protein kinase
CC (PubMed:26792519). {ECO:0000269|PubMed:23167545,
CC ECO:0000269|PubMed:26792519}.
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 ACR4 (PubMed:26792519). Interacts with TAP46
CC (PubMed:21216945, PubMed:24357600). Interacts with SIC/RON3
CC (PubMed:26888284). {ECO:0000250|UniProtKB:P62714,
CC ECO:0000269|PubMed:21216945, ECO:0000269|PubMed:24357600,
CC ECO:0000269|PubMed:26792519, ECO:0000269|PubMed:26888284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q07100-1; Sequence=Displayed;
CC -!- PTM: Reversibly methyl esterified on Leu-313 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10854.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M96841; AAA64742.1; -; mRNA.
DR EMBL; U60135; AAD10854.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005956; AAD23731.1; -; Genomic_DNA.
DR EMBL; AC007087; AAM15383.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10127.1; -; Genomic_DNA.
DR EMBL; BT010166; AAQ22635.1; -; mRNA.
DR PIR; S31163; S31163.
DR PIR; S52659; S52659.
DR RefSeq; NP_565974.1; NM_129811.4. [Q07100-1]
DR AlphaFoldDB; Q07100; -.
DR SMR; Q07100; -.
DR BioGRID; 4187; 18.
DR IntAct; Q07100; 1.
DR STRING; 3702.AT2G42500.1; -.
DR PaxDb; Q07100; -.
DR PRIDE; Q07100; -.
DR ProteomicsDB; 249207; -. [Q07100-1]
DR EnsemblPlants; AT2G42500.1; AT2G42500.1; AT2G42500. [Q07100-1]
DR GeneID; 818850; -.
DR Gramene; AT2G42500.1; AT2G42500.1; AT2G42500. [Q07100-1]
DR KEGG; ath:AT2G42500; -.
DR Araport; AT2G42500; -.
DR TAIR; locus:2041579; AT2G42500.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q07100; -.
DR OMA; DHINYAF; -.
DR PhylomeDB; Q07100; -.
DR PRO; PR:Q07100; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q07100; baseline and differential.
DR Genevisible; Q07100; 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: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:TAIR.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:0048364; P:root development; IGI:TAIR.
DR GO; GO:0048863; P:stem cell differentiation; 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 Alternative splicing; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Methylation; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..313
FT /note="Serine/threonine-protein phosphatase PP2A-3
FT catalytic subunit"
FT /id="PRO_0000058854"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT MOD_RES 313
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000305|PubMed:28741704"
FT CONFLICT 15
FT /note="D -> N (in Ref. 2; AAD10854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 35833 MW; 2EF8542AD8A89C64 CRC64;
MGANSIPTDA TIDLDEQISQ LMQCKPLSEQ QVRALCEKAK EILMDESNVQ PVKSPVTICG
DIHGQFHDLA ELFRIGGMCP DTNYLFMGDY VDRGYYSVET VTLLVALKMR YPQRITILRG
NHESRQITQV YGFYDECLRK YGNANVWKIF TDLFDYFPLT ALVESEIFCL HGGLSPSIET
LDNIRNFDRV QEVPHEGPMC DLLWSDPDDR CGWGISPRGA GYTFGQDISE QFNHTNNLKL
IARAHQLVMD GYNWAHEQKV VTIFSAPNYC YRCGNMASIL EVDDCRNHTF IQFEPAPRRG
EPDVTRRTPD YFL
