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 27-MAR-2024, entry version 159. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.P48482; -. DR iPTMnet; P48482; -. DR PaxDb; 3702-AT5G59160-2; -. 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; AT5G59160; TOPP2. DR eggNOG; KOG0374; Eukaryota. DR HOGENOM; CLU_004962_0_0_1; -. DR InParanoid; P48482; -. DR OMA; KQSVECI; -. DR OrthoDB; 5484004at2759; -. DR PhylomeDB; P48482; -. DR PRO; PR:P48482; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; P48482; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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 CDD; cd07414; MPP_PP1_PPKL; 1. 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 PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF459; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 2-RELATED; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF16891; STPPase_N; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. DR Genevisible; P48482; AT. 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 //