PP2A4_ARATH
ID PP2A4_ARATH Reviewed; 313 AA.
AC P48578; Q9M2G6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-4 catalytic subunit;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2A isoform 4;
GN Name=PP2A4 {ECO:0000303|PubMed:9524239};
GN Synonyms=EP7, PP2A3 {ECO:0000303|PubMed:17368080};
GN OrderedLocusNames=At3g58500; ORFNames=F14P22.90;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [7]
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 [8]
RP FUNCTION.
RX PubMed=25085430; DOI=10.15252/embj.201488698;
RA Segonzac C., Macho A.P., Sanmartin M., Ntoukakis V., Sanchez-Serrano J.J.,
RA Zipfel C.;
RT "Negative control of BAK1 by protein phosphatase 2A during plant innate
RT immunity.";
RL EMBO J. 33:2069-2079(2014).
RN [9]
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 [10]
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 PP2A3, 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). The holoenzyme composed of PP2AA1, PP2A4
CC and B'ZETA or B'ETA acts as negative regulator of plant innate immunity
CC by controlling BAK1 phosphorylation state and activation in surface-
CC localized immune receptor complexes (PubMed:25085430).
CC {ECO:0000269|PubMed:23167545, ECO:0000269|PubMed:25085430}.
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 SIC/RON3 (PubMed:26888284).
CC {ECO:0000250|UniProtKB:P62714, ECO:0000269|PubMed:26888284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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=CAB68188.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U08047; AAA64941.1; -; mRNA.
DR EMBL; U60136; AAD10855.1; -; Genomic_DNA.
DR EMBL; AL137082; CAB68188.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79790.1; -; Genomic_DNA.
DR EMBL; AY057604; AAL14399.1; -; mRNA.
DR EMBL; AY056222; AAL07071.1; -; mRNA.
DR EMBL; AY113023; AAM47331.1; -; mRNA.
DR PIR; S52660; S52660.
DR RefSeq; NP_567066.1; NM_115712.4.
DR AlphaFoldDB; P48578; -.
DR SMR; P48578; -.
DR BioGRID; 10334; 10.
DR IntAct; P48578; 2.
DR STRING; 3702.AT3G58500.1; -.
DR PaxDb; P48578; -.
DR PRIDE; P48578; -.
DR ProteomicsDB; 249208; -.
DR EnsemblPlants; AT3G58500.1; AT3G58500.1; AT3G58500.
DR GeneID; 825019; -.
DR Gramene; AT3G58500.1; AT3G58500.1; AT3G58500.
DR KEGG; ath:AT3G58500; -.
DR Araport; AT3G58500; -.
DR TAIR; locus:2076451; AT3G58500.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR OMA; EGYNWGQ; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; P48578; -.
DR PRO; PR:P48578; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P48578; baseline and differential.
DR Genevisible; P48578; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS: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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; TAS: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 Cytoplasm; Hydrolase; Manganese; Metal-binding; Methylation;
KW Phosphoprotein; Plant defense; Protein phosphatase; Reference proteome.
FT CHAIN 1..313
FT /note="Serine/threonine-protein phosphatase PP2A-4
FT catalytic subunit"
FT /id="PRO_0000058855"
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"
SQ SEQUENCE 313 AA; 35767 MW; 0636FF10832B1B00 CRC64;
MGANSLPTDA TLDLDEQISQ LMQCKPLSEQ QVRALCEKAK EILMDESNVQ PVKSPVTICG
DIHGQFHDLA ELFRIGGKCP DTNYLFMGDY VDRGYYSVET VTLLVGLKVR YPQRITILRG
NHESRQITQV YGFYDECLRK YGNANVWKIF TDLFDYFPLT ALVESEIFCL HGGLSPSIET
LDNIRNFDRV QEVPHEGPMC DLLWSDPDDR CGWGISPRGA GYTFGQDISE QFNHTNNLKL
IARAHQLVMD GFNWAHEQKV VTIFSAPNYC YRCGNMASIL EVDDCRNHTF IQFEPAPRRG
EPDVTRRTPD YFL
