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

 PP2A2_ARATH             Reviewed;         306 AA.
Q07098;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
27-SEP-2017, entry version 130.
RecName: Full=Serine/threonine-protein phosphatase PP2A-2 catalytic subunit;
EC=3.1.3.16;
AltName: Full=Protein phosphatase 2A isoform 2;
Name=PP2A2 {ECO:0000303|PubMed:17368080}; Synonyms=PP2A1;
OrderedLocusNames=At1g10430; ORFNames=T10O24.4;
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;
PubMed=8382968; DOI=10.1007/BF00028805;
Arino J., Perez-Callejon E., Cunillera N., Camps M., Posas F.,
Ferrer A.;
"Protein phosphatases in higher plants: multiplicity of type 2A
phosphatases in Arabidopsis thaliana.";
Plant Mol. Biol. 21:475-485(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
INTERACTION WITH PP2AA1.
PubMed=10091592; DOI=10.1046/j.1432-1327.1999.00154.x;
Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S.,
Rundle S.J.;
"Molecular characterization of the B' regulatory subunit gene family
of Arabidopsis protein phosphatase 2A.";
Eur. J. Biochem. 260:127-136(1999).
[6]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY ABSCISIC ACID.
PubMed=17617176; DOI=10.1111/j.1365-313X.2007.03179.x;
Pernas M., Garcia-Casado G., Rojo E., Solano R., Sanchez-Serrano J.J.;
"A protein phosphatase 2A catalytic subunit is a negative regulator of
abscisic acid signalling.";
Plant J. 51:763-778(2007).
[7]
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).
[8]
FUNCTION.
PubMed=22642987; DOI=10.1093/pcp/pcs081;
Wen F., Wang J., Xing D.;
"A protein phosphatase 2A catalytic subunit modulates blue light-
induced chloroplast avoidance movements through regulating actin
cytoskeleton in Arabidopsis.";
Plant Cell Physiol. 53:1366-1379(2012).
[9]
INTERACTION WITH HDA14, AND SUBCELLULAR LOCATION.
PubMed=22404109; DOI=10.1111/j.1365-313X.2012.04984.x;
Tran H.T., Nimick M., Uhrig R.G., Templeton G., Morrice N.,
Gourlay R., DeLong A., Moorhead G.B.;
"Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-
tubulin deacetylase that associates with PP2A and enriches in the
microtubule fraction with the putative histone acetyltransferase
ELP3.";
Plant J. 71:263-272(2012).
[10]
INTERACTION WITH TAP46.
PubMed=24357600; DOI=10.1104/pp.113.233684;
Hu R., Zhu Y., Shen G., Zhang H.;
"TAP46 plays a positive role in the ABSCISIC ACID INSENSITIVE5-
regulated gene expression in Arabidopsis.";
Plant Physiol. 164:721-734(2014).
[11]
FUNCTION, INTERACTION WITH B'THETA, AND SUBCELLULAR LOCATION.
PubMed=25489022; DOI=10.1104/pp.114.254409;
Kataya A.R., Heidari B., Hagen L., Kommedal R., Slupphaug G.,
Lillo C.;
"Protein phosphatase 2A holoenzyme is targeted to peroxisomes by
piggybacking and positively affects peroxisomal beta-oxidation.";
Plant Physiol. 167:493-506(2015).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SRK2E/OST1.
PubMed=26175513; DOI=10.1104/pp.15.00575;
Waadt R., Manalansan B., Rauniyar N., Munemasa S., Booker M.A.,
Brandt B., Waadt C., Nusinow D.A., Kay S.A., Kunz H.H., Schumacher K.,
DeLong A., Yates J.R. III, Schroeder J.I.;
"Identification of Open Stomata1-interacting proteins reveals
interactions with sucrose non-fermenting1-related protein kinases2 and
with type 2a protein phosphatases that function in abscisic acid
responses.";
Plant Physiol. 169:760-779(2015).
-!- FUNCTION: Dephosphorylates and activates the actin-depolymerizing
factor ADF1, which, in turn, regulates actin cytoskeleton
remodeling and is involved in the blue light photoreceptor PHOT2-
mediated chloroplast avoidance movements (PubMed:22642987).
Associates with the serine/threonine-protein phosphatase PP2A
regulatory subunits A and B' to positively regulates beta-
oxidation of fatty acids and protoauxins in peroxisomes by
dephosphorylating peroxisomal beta-oxidation-related proteins
(PubMed:25489022). Acts as negative regulator of abscisic acid
(ABA) signaling. May regulate ABA-dependent gene expression
(PubMed:17617176). {ECO:0000269|PubMed:17617176,
ECO:0000269|PubMed:22642987, ECO:0000269|PubMed:25489022}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- 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)
(Probable). Interacts with B'THETA (PubMed:25489022). Interacts
with HDA14 (PubMed:22404109). Interacts with SRK2E/OST1
(PubMed:26175513). Interacts with TAP46.
{ECO:0000269|PubMed:22404109, ECO:0000269|PubMed:24357600,
ECO:0000269|PubMed:25489022, ECO:0000269|PubMed:26175513,
ECO:0000305|PubMed:10091592}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:22404109, ECO:0000269|PubMed:25489022}.
Nucleus {ECO:0000269|PubMed:22404109}. Peroxisome
{ECO:0000269|PubMed:25489022}. Note=Interacts with B'THETA in the
cytosol and peroxisomal import occurs by a piggybacking transport.
{ECO:0000269|PubMed:25489022}.
-!- TISSUE SPECIFICITY: Expressed in root meristem, emerging lateral
roots, leaf vasculature, stipules, guard cells, anthers and pollen
grains. {ECO:0000269|PubMed:17617176}.
-!- INDUCTION: Induced by abscisic acid (ABA).
{ECO:0000269|PubMed:17617176}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M96733; AAA32848.1; -; mRNA.
EMBL; AC007067; AAD39564.1; -; Genomic_DNA.
EMBL; CP002684; AEE28579.1; -; Genomic_DNA.
EMBL; CP002684; ANM59883.1; -; Genomic_DNA.
EMBL; AY059847; AAL24329.1; -; mRNA.
EMBL; AY093267; AAM13266.1; -; mRNA.
PIR; S31162; S31162.
RefSeq; NP_001322206.1; NM_001331905.1.
RefSeq; NP_172514.1; NM_100918.3.
UniGene; At.21842; -.
ProteinModelPortal; Q07098; -.
SMR; Q07098; -.
BioGrid; 22823; 4.
IntAct; Q07098; 1.
STRING; 3702.AT1G10430.1; -.
PaxDb; Q07098; -.
EnsemblPlants; AT1G10430.1; AT1G10430.1; AT1G10430.
EnsemblPlants; AT1G10430.2; AT1G10430.2; AT1G10430.
GeneID; 837583; -.
Gramene; AT1G10430.1; AT1G10430.1; AT1G10430.
Gramene; AT1G10430.2; AT1G10430.2; AT1G10430.
KEGG; ath:AT1G10430; -.
Araport; AT1G10430; -.
TAIR; locus:2194626; AT1G10430.
eggNOG; KOG0371; Eukaryota.
eggNOG; COG0639; LUCA.
HOGENOM; HOG000172696; -.
InParanoid; Q07098; -.
KO; K04382; -.
OMA; IARAHQI; -.
OrthoDB; EOG09360EXD; -.
PhylomeDB; Q07098; -.
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-5673000; RAF activation.
Reactome; R-ATH-5675221; Negative regulation of MAPK pathway.
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:Q07098; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q07098; baseline and differential.
Genevisible; Q07098; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0034613; P:cellular protein localization; IMP:TAIR.
GO; GO:0009903; P:chloroplast avoidance movement; IMP:TAIR.
GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; IMP: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.
SUPFAM; SSF56300; SSF56300; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
Abscisic acid signaling pathway; Complete proteome; Cytoplasm;
Hydrolase; Manganese; Metal-binding; Nucleus; Peroxisome;
Protein phosphatase; Reference proteome.
CHAIN 1 306 Serine/threonine-protein phosphatase
PP2A-2 catalytic subunit.
/FTId=PRO_0000058852.
ACT_SITE 115 115 Proton donor. {ECO:0000250}.
METAL 54 54 Manganese 1. {ECO:0000250}.
METAL 56 56 Manganese 1. {ECO:0000250}.
METAL 82 82 Manganese 1. {ECO:0000250}.
METAL 82 82 Manganese 2. {ECO:0000250}.
METAL 114 114 Manganese 2. {ECO:0000250}.
METAL 164 164 Manganese 2. {ECO:0000250}.
METAL 238 238 Manganese 2. {ECO:0000250}.
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


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