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Serine/threonine-protein phosphatase PP2A-4 catalytic subunit (EC 3.1.3.16) (Protein phosphatase 2A isoform 4)

 PP2A4_ARATH             Reviewed;         313 AA.
P48578; Q9M2G6;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
05-DEC-2018, entry version 136.
RecName: Full=Serine/threonine-protein phosphatase PP2A-4 catalytic subunit;
EC=3.1.3.16;
AltName: Full=Protein phosphatase 2A isoform 4;
Name=PP2A4 {ECO:0000303|PubMed:9524239};
Synonyms=EP7, PP2A3 {ECO:0000303|PubMed:17368080};
OrderedLocusNames=At3g58500; ORFNames=F14P22.90;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia GL1; TISSUE=Leaf;
PubMed=7948902; DOI=10.1007/BF00039564;
Casamayor A., Perez-Callejon E., Pujol G., Arino J., Ferrer A.;
"Molecular characterization of a fourth isoform of the catalytic
subunit of protein phosphatase 2A from Arabidopsis thaliana.";
Plant Mol. Biol. 26:523-528(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9524239; DOI=10.1016/S0378-1119(98)00013-4;
Perez-Callejon E., Casamayor A., Pujol G., Camps M., Ferrer A.,
Arino J.;
"Molecular cloning and characterization of two phosphatase 2A
catalytic subunit genes from Arabidopsis thaliana.";
Gene 209:105-112(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=17368080; DOI=10.1016/j.tplants.2007.03.003;
Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.;
"Arabidopsis PPP family of serine/threonine phosphatases.";
Trends Plant Sci. 12:169-176(2007).
[7]
FUNCTION.
PubMed=23167545; DOI=10.1111/tpj.12078;
Ballesteros I., Dominguez T., Sauer M., Paredes P., Duprat A.,
Rojo E., Sanmartin M., Sanchez-Serrano J.J.;
"Specialized functions of the PP2A subfamily II catalytic subunits
PP2A-C3 and PP2A-C4 in the distribution of auxin fluxes and
development in Arabidopsis.";
Plant J. 73:862-872(2013).
[8]
FUNCTION.
PubMed=25085430; DOI=10.15252/embj.201488698;
Segonzac C., Macho A.P., Sanmartin M., Ntoukakis V.,
Sanchez-Serrano J.J., Zipfel C.;
"Negative control of BAK1 by protein phosphatase 2A during plant
innate immunity.";
EMBO J. 33:2069-2079(2014).
[9]
INTERACTION WITH SIC/RON3.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=26888284; DOI=10.1073/pnas.1501343112;
Karampelias M., Neyt P., De Groeve S., Aesaert S., Coussens G.,
Rolcik J., Bruno L., De Winne N., Van Minnebruggen A., Van Montagu M.,
Ponce M.R., Micol J.L., Friml J., De Jaeger G., Van Lijsebettens M.;
"ROTUNDA3 function in plant development by phosphatase 2A-mediated
regulation of auxin transporter recycling.";
Proc. Natl. Acad. Sci. U.S.A. 113:2768-2773(2016).
[10]
METHYLATION AT LEU-313.
PubMed=28741704; DOI=10.1111/pce.13038;
Creighton M.T., Kolton A., Kataya A.R.A., Maple-Groedem J.,
Averkina I.O., Heidari B., Lillo C.;
"Methylation of protein phosphatase 2A-influence of regulators and
environmental stress factors.";
Plant Cell Environ. 40:2347-2358(2017).
-!- FUNCTION: Functions redundantly with PP2A3, and is involved in
establishing auxin gradients, apical-basal axis of polarity and
root and shoot apical meristem during embryogenesis. May
dephosphorylate PIN1 and regulate its subcellular distribution for
polar auxin transport (PubMed:23167545). The holoenzyme composed
of PP2AA1, PP2A4 and B'ZETA or B'ETA acts as negative regulator of
plant innate immunity by controlling BAK1 phosphorylation state
and activation in surface-localized immune receptor complexes
(PubMed:25085430). {ECO:0000269|PubMed:23167545,
ECO:0000269|PubMed:25085430}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
EC=3.1.3.16;
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
constant regulatory subunit (subunit A), that associates with a
variety of regulatory subunits such as subunits B (the
R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) (By
similarity). Interacts with SIC/RON3 (PubMed:26888284).
{ECO:0000250|UniProtKB:P62714, ECO:0000269|PubMed:26888284}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: Reversibly methyl esterified on Leu-313 by leucine carboxyl
methyltransferase 1 (LCMT1) and pectin methylesterase 1 (PME1).
Carboxyl methylation influences the affinity of the catalytic
subunit for the different regulatory subunits, thereby modulating
the PP2A holoenzyme's substrate specificity, enzyme activity and
cellular localization. {ECO:0000305|PubMed:28741704}.
-!- PTM: Phosphorylation of either threonine (by autophosphorylation-
activated protein kinase) or tyrosine results in inactivation of
the phosphatase. Auto-dephosphorylation has been suggested as a
mechanism for reactivation. {ECO:0000250|UniProtKB:P67774}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB68188.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U08047; AAA64941.1; -; mRNA.
EMBL; U60136; AAD10855.1; -; Genomic_DNA.
EMBL; AL137082; CAB68188.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE79790.1; -; Genomic_DNA.
EMBL; AY057604; AAL14399.1; -; mRNA.
EMBL; AY056222; AAL07071.1; -; mRNA.
EMBL; AY113023; AAM47331.1; -; mRNA.
PIR; S52660; S52660.
RefSeq; NP_567066.1; NM_115712.4.
UniGene; At.25267; -.
ProteinModelPortal; P48578; -.
SMR; P48578; -.
BioGrid; 10334; 2.
IntAct; P48578; 1.
STRING; 3702.AT3G58500.1; -.
PaxDb; P48578; -.
PRIDE; P48578; -.
EnsemblPlants; AT3G58500.1; AT3G58500.1; AT3G58500.
GeneID; 825019; -.
Gramene; AT3G58500.1; AT3G58500.1; AT3G58500.
KEGG; ath:AT3G58500; -.
Araport; AT3G58500; -.
TAIR; locus:2076451; AT3G58500.
eggNOG; KOG0371; Eukaryota.
eggNOG; COG0639; LUCA.
HOGENOM; HOG000172696; -.
KO; K04382; -.
OMA; QILWNDP; -.
OrthoDB; EOG09360EXD; -.
PhylomeDB; P48578; -.
Reactome; R-ATH-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-ATH-198753; ERK/MAPK targets.
Reactome; R-ATH-202670; ERKs are inactivated.
Reactome; R-ATH-69231; Cyclin D associated events in G1.
Reactome; R-ATH-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-ATH-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
PRO; PR:P48578; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P48578; baseline and differential.
Genevisible; P48578; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0006470; P:protein dephosphorylation; TAS:TAIR.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Manganese; Metal-binding;
Methylation; Phosphoprotein; Plant defense; Protein phosphatase;
Reference proteome.
CHAIN 1 313 Serine/threonine-protein phosphatase
PP2A-4 catalytic subunit.
/FTId=PRO_0000058855.
ACT_SITE 122 122 Proton donor. {ECO:0000250}.
METAL 61 61 Manganese 1.
{ECO:0000250|UniProtKB:P67775}.
METAL 63 63 Manganese 1.
{ECO:0000250|UniProtKB:P67775}.
METAL 89 89 Manganese 1.
{ECO:0000250|UniProtKB:P67775}.
METAL 89 89 Manganese 2.
{ECO:0000250|UniProtKB:P67775}.
METAL 121 121 Manganese 2.
{ECO:0000250|UniProtKB:P67775}.
METAL 171 171 Manganese 2.
{ECO:0000250|UniProtKB:P67775}.
METAL 245 245 Manganese 2.
{ECO:0000250|UniProtKB:P67775}.
MOD_RES 313 313 Leucine methyl ester.
{ECO:0000305|PubMed:28741704}.
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


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