PP12_ARATH
ID PP12_ARATH Reviewed; 312 AA.
AC P48482; Q24JM8; Q94B57;
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 PP1 isozyme 2 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:21222654};
DE AltName: Full=Type one protein phosphatase 2 {ECO:0000303|PubMed:17368080};
GN Name=TOPP2 {ECO:0000303|PubMed:17368080};
GN OrderedLocusNames=At5g59160 {ECO:0000312|Araport:AT5G59160};
GN ORFNames=MNC17.7 {ECO:0000312|EMBL:BAB09762.1};
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].
RX PubMed=7678768; DOI=10.1007/bf00019946;
RA Smith R.D., Walker J.C.;
RT "Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 21:307-316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8220477; DOI=10.1046/j.1365-313x.1993.04010081.x;
RA Ferreira P.C.G., Hemerly A.S., van Montagu M., Inze D.;
RT "A protein phosphatase 1 from Arabidopsis thaliana restores temperature
RT sensitivity of a Schizosaccharomyces pombe cdc25ts/wee1-double mutant.";
RL Plant J. 4:81-87(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 SUBCELLULAR LOCATION.
RX PubMed=19329567; DOI=10.1104/pp.109.135335;
RA Takemiya A., Ariyoshi C., Shimazaki K.;
RT "Identification and functional characterization of inhibitor-3, a
RT regulatory subunit of protein phosphatase 1 in plants.";
RL Plant Physiol. 150:144-156(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=21222654; DOI=10.1042/bj20101035;
RA Templeton G.W., Nimick M., Morrice N., Campbell D., Goudreault M.,
RA Gingras A.C., Takemiya A., Shimazaki K., Moorhead G.B.;
RT "Identification and characterization of AtI-2, an Arabidopsis homologue of
RT an ancient protein phosphatase 1 (PP1) regulatory subunit.";
RL Biochem. J. 435:73-83(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP INTERACTION WITH SRK2D/SNRK2.2 AND SRK2E/SNRK2.6.
RX PubMed=26943172; DOI=10.1371/journal.pgen.1005835;
RA Hou Y.J., Zhu Y., Wang P., Zhao Y., Xie S., Batelli G., Wang B., Duan C.G.,
RA Wang X., Xing L., Lei M., Yan J., Zhu X., Zhu J.K.;
RT "Type one protein phosphatase 1 and its regulatory protein inhibitor 2
RT negatively regulate ABA signaling.";
RL PLoS Genet. 12:E1005835-E1005835(2016).
CC -!- FUNCTION: Serine/threonine-protein phosphatase that possesses
CC phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro.
CC {ECO:0000269|PubMed:21222654}.
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 Evidence={ECO:0000269|PubMed:21222654};
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 Evidence={ECO:0000269|PubMed:21222654};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Phosphatase activity is strongly reduced by the
CC protein phosphatase inhibitor 2 (I-2). {ECO:0000269|PubMed:21222654}.
CC -!- SUBUNIT: Interacts with SRK2D/SNRK2.2 and SRK2E/SNRK2.6.
CC {ECO:0000269|PubMed:26943172}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567,
CC ECO:0000269|PubMed:21222654}. Cytoplasm {ECO:0000269|PubMed:19329567,
CC ECO:0000269|PubMed:21222654}. Note=Predominantly localizes in the
CC nucleus. {ECO:0000269|PubMed:21222654}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; M93409; AAA32837.1; -; mRNA.
DR EMBL; Z12163; CAA78153.1; -; mRNA.
DR EMBL; AB016890; BAB09762.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97150.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97151.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97152.1; -; Genomic_DNA.
DR EMBL; AY042840; AAK68780.1; -; mRNA.
DR EMBL; BT002401; AAO00761.1; -; mRNA.
DR EMBL; BT024861; ABD65592.1; -; mRNA.
DR PIR; S24264; S24264.
DR PIR; S31086; S31086.
DR RefSeq; NP_001032103.1; NM_001037026.1.
DR RefSeq; NP_200724.1; NM_125306.2.
DR RefSeq; NP_851218.1; NM_180887.5.
DR AlphaFoldDB; P48482; -.
DR SMR; P48482; -.
DR BioGRID; 21278; 1.
DR STRING; 3702.AT5G59160.2; -.
DR iPTMnet; P48482; -.
DR PaxDb; P48482; -.
DR PRIDE; P48482; -.
DR ProteomicsDB; 249065; -.
DR EnsemblPlants; AT5G59160.1; AT5G59160.1; AT5G59160.
DR EnsemblPlants; AT5G59160.2; AT5G59160.2; AT5G59160.
DR EnsemblPlants; AT5G59160.3; AT5G59160.3; AT5G59160.
DR GeneID; 836034; -.
DR Gramene; AT5G59160.1; AT5G59160.1; AT5G59160.
DR Gramene; AT5G59160.2; AT5G59160.2; AT5G59160.
DR Gramene; AT5G59160.3; AT5G59160.3; AT5G59160.
DR KEGG; ath:AT5G59160; -.
DR Araport; AT5G59160; -.
DR TAIR; locus:2168484; AT5G59160.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P48482; -.
DR OMA; PDLITIQ; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P48482; -.
DR PRO; PR:P48482; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P48482; baseline and differential.
DR Genevisible; P48482; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISS: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; IDA:TAIR.
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 InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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 Acetylation; Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..312
FT /note="Serine/threonine-protein phosphatase PP1 isozyme 2"
FT /id="PRO_0000058798"
FT ACT_SITE 131
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 181..182
FT /note="GL -> AI (in Ref. 2; CAA78153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 35532 MW; DF71C23B5CB53CC2 CRC64;
MAQQGQGSMD PAALDDIIRR LLDYRNPKPG TKQAMLNESE IRQLCIVSRE IFLQQPNLLE
LEAPIKICGD IHGQYSDLLR LFEYGGFPPT ANYLFLGDYV DRGKQSLETI CLLLAYKIKY
PENFFLLRGN HECASINRIY GFYDECKRRF SVRLWKVFTD SFNCLPVAAV IDDKILCMHG
GLSPDLTNVE QIKNIKRPTD VPDSGLLCDL LWSDPSKDVK GWGMNDRGVS YTFGPDKVAE
FLIKNDMDLI CRAHQVVEDG YEFFADRQLV TIFSAPNYCG EFDNAGAMMS VDESLMCSFQ
ILKPADRKPR FL
