PP2A1_ARATH
ID PP2A1_ARATH Reviewed; 306 AA.
AC Q07099; Q3ECM1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-1 catalytic subunit;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2A isoform 1;
GN Name=PP2A1 {ECO:0000303|PubMed:17368080}; Synonyms=PP2A2;
GN OrderedLocusNames=At1g59830; ORFNames=F23H11.15;
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] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
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 [6]
RP INTERACTION WITH TAF12B.
RC STRAIN=cv. Wassilewskija;
RX PubMed=17526916; DOI=10.1093/jxb/erm080;
RA Robles L.M., Wampole J.S., Christians M.J., Larsen P.B.;
RT "Arabidopsis enhanced ethylene response 4 encodes an EIN3-interacting TFIID
RT transcription factor required for proper ethylene response, including ERF1
RT induction.";
RL J. Exp. Bot. 58:2627-2639(2007).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SRK2E/OST1.
RX PubMed=26175513; DOI=10.1104/pp.15.00575;
RA Waadt R., Manalansan B., Rauniyar N., Munemasa S., Booker M.A., Brandt B.,
RA Waadt C., Nusinow D.A., Kay S.A., Kunz H.H., Schumacher K., DeLong A.,
RA Yates J.R. III, Schroeder J.I.;
RT "Identification of Open Stomata1-interacting proteins reveals interactions
RT with sucrose non-fermenting1-related protein kinases2 and with type 2a
RT protein phosphatases that function in abscisic acid responses.";
RL Plant Physiol. 169:760-779(2015).
RN [9]
RP METHYLATION AT LEU-306.
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 -!- 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 TAF12B (By similarity) (PubMed:17526916). Interacts with
CC SRK2E/OST1 (PubMed:26175513). Interacts with TAP46. {ECO:0000250,
CC ECO:0000250|UniProtKB:P62714, ECO:0000269|PubMed:17526916,
CC ECO:0000269|PubMed:24357600, ECO:0000269|PubMed:26175513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q07099-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q07099-2; Sequence=VSP_028727, VSP_028728;
CC -!- PTM: Reversibly methyl esterified on Leu-306 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}.
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DR EMBL; M96732; AAA32847.1; -; mRNA.
DR EMBL; AC007258; AAD39326.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33622.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33623.1; -; Genomic_DNA.
DR EMBL; AY063942; AAL36298.1; -; mRNA.
DR EMBL; AY096543; AAM20193.1; -; mRNA.
DR PIR; S31161; S31161.
DR RefSeq; NP_176192.1; NM_104676.5. [Q07099-1]
DR RefSeq; NP_974050.1; NM_202321.2. [Q07099-2]
DR AlphaFoldDB; Q07099; -.
DR SMR; Q07099; -.
DR BioGRID; 27501; 16.
DR IntAct; Q07099; 1.
DR STRING; 3702.AT1G59830.1; -.
DR PaxDb; Q07099; -.
DR PRIDE; Q07099; -.
DR ProteomicsDB; 248967; -. [Q07099-1]
DR EnsemblPlants; AT1G59830.1; AT1G59830.1; AT1G59830. [Q07099-1]
DR EnsemblPlants; AT1G59830.2; AT1G59830.2; AT1G59830. [Q07099-2]
DR GeneID; 842276; -.
DR Gramene; AT1G59830.1; AT1G59830.1; AT1G59830. [Q07099-1]
DR Gramene; AT1G59830.2; AT1G59830.2; AT1G59830. [Q07099-2]
DR KEGG; ath:AT1G59830; -.
DR Araport; AT1G59830; -.
DR TAIR; locus:2025976; AT1G59830.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q07099; -.
DR OMA; YSLECAT; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q07099; -.
DR PRO; PR:Q07099; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q07099; baseline and differential.
DR Genevisible; Q07099; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004722; F:protein serine/threonine phosphatase activity; ISS:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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..306
FT /note="Serine/threonine-protein phosphatase PP2A-1
FT catalytic subunit"
FT /id="PRO_0000058853"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT MOD_RES 306
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000305|PubMed:28741704"
FT VAR_SEQ 250..262
FT /note="EKNVVTVFSAPNY -> VYNMCITIDWHMC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028727"
FT VAR_SEQ 263..306
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028728"
SQ SEQUENCE 306 AA; 34961 MW; 579427029D41A1C1 CRC64;
MPLNGDLDRQ IEQLMECKPL GEADVKILCD QAKAILVEEY NVQPVKCPVT VCGDIHGQFY
DLIELFRIGG NAPDTNYLFM GDYVDRGYYS VETVSLLVAL KVRYRDRLTI LRGNHESRQI
TQVYGFYDEC LRKYGNANVW KYFTDLFDYL PLTALIESQV FCLHGGLSPS LDTLDNIRSL
DRIQEVPHEG PMCDLLWSDP DDRCGWGISP RGAGYTFGQD IATQFNHNNG LSLISRAHQL
VMEGYNWCQE KNVVTVFSAP NYCYRCGNMA AILEIGEKME QNFLQFDPAP RQVEPDTTRK
TPDYFL
