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 27-MAR-2024, entry version 174. 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}; GN OrderedLocusNames=At2g42500; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 19. DR IntAct; Q07100; 1. DR STRING; 3702.Q07100; -. DR PaxDb; 3702-AT2G42500-1; -. 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; AT2G42500; PP2A-3. DR eggNOG; KOG0371; Eukaryota. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; Q07100; -. DR OMA; EGYNWGQ; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; Q07100; -. DR PRO; PR:Q07100; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q07100; baseline and differential. 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: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 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:SF12; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A; 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; Q07100; 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..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 //