ID PP16_ARATH Reviewed; 322 AA. AC P48486; Q8RX64; Q9SUT7; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 02-SEP-2026, entry version 168. DE RecName: Full=Serine/threonine-protein phosphatase PP1 isozyme 6 {ECO:0000305}; DE EC=3.1.3.16 {ECO:0000269|PubMed:21222654}; DE AltName: Full=Type one protein phosphatase 6 {ECO:0000303|PubMed:17368080}; GN Name=TOPP6 {ECO:0000303|PubMed:17368080}; GN Synonyms=PP1BG {ECO:0000312|EMBL:CAA86339.1}, TOPP7 GN {ECO:0000303|PubMed:21222654}; GN OrderedLocusNames=At4g11240 {ECO:0000312|Araport:AT4G11240}; GN ORFNames=F8L21.30 {ECO:0000312|EMBL:CAB51408.1}; 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=7773310; DOI=10.1046/j.1365-313x.1995.07050823.x; RA Arundhati A., Feiler H., Traas J., Zhang H., Lunness P.A., Doonan J.H.; RT "A novel Arabidopsis type 1 protein phosphatase is highly expressed in male RT and female tissues and functionally complements a conditional cell cycle RT mutant of Aspergillus."; RL Plant J. 7:823-834(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9617814; DOI=10.1023/a:1005912413555; RA Lin Q., Li J., Smith R.D., Walker J.C.; RT "Molecular cloning and chromosomal mapping of type one serine/threonine RT protein phosphatases in Arabidopsis thaliana."; RL Plant Mol. Biol. 37:471-481(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). 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 GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [8] 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 [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND RP ACTIVITY REGULATION. 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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). 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=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm CC {ECO:0000269|PubMed:19329567}. CC -!- TISSUE SPECIFICITY: Strongly up-regulated within developing flowers, CC especially in the tapetum, the developing and mature pollen and in the CC ovaries. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB51408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB81225.1; Type=Erroneous gene model prediction; Evidence={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; Z46253; CAA86339.1; -; mRNA. DR EMBL; U80921; AAC39460.1; -; Genomic_DNA. DR EMBL; AL096882; CAB51408.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161531; CAB81225.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE82988.1; -; Genomic_DNA. DR EMBL; OZ408686; CAO7046713.1; -; Genomic_DNA. DR EMBL; AY090365; AAL91268.1; -; mRNA. DR EMBL; AY122904; AAM67437.1; -; mRNA. DR EMBL; AY086060; AAM63269.1; -; mRNA. DR PIR; T13015; T13015. DR RefSeq; NP_567375.1; NM_117195.5. DR AlphaFoldDB; P48486; -. DR SMR; P48486; -. DR BioGRID; 12025; 4. DR FunCoup; P48486; 2498. DR IntAct; P48486; 2. DR STRING; 3702.P48486; -. DR iPTMnet; P48486; -. DR PaxDb; 3702-P48486; -. DR ProteomicsDB; 249140; -. DR GeneID; 826726; -. DR KEGG; ath:AT4G11240; -. DR Araport; AT4G11240; -. DR TAIR; AT4G11240; TOPP7. DR eggNOG; KOG0374; Eukaryota. DR HOGENOM; CLU_004962_0_0_1; -. DR InParanoid; P48486; -. DR OMA; VKYKFNF; -. DR OrthoDB; 1930084at2759; -. DR PhylomeDB; P48486; -. DR PRO; PR:P48486; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; P48486; baseline and differential. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISM:TAIR. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:TAIR. DR CDD; cd07414; MPP_PP1_PPKL; 1. DR FunFam; 3.60.21.10:FF:000026; Serine/threonine-protein phosphatase; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR050341; PP1_catalytic_subunit. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR InterPro; IPR031675; STPPase_N. DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF504; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 6; 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. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleus; KW Protein phosphatase; Reference proteome. FT CHAIN 1..322 FT /note="Serine/threonine-protein phosphatase PP1 isozyme 6" FT /id="PRO_0000058802" FT REGION 303..322 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 122 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 61 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 63 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 89 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 89 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 121 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 170 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895" FT CONFLICT 248 FT /note="V -> D (in Ref. 1; CAA86339 and 2; AAC39460)" FT /evidence="ECO:0000305" SQ SEQUENCE 322 AA; 36567 MW; B2320EB8E472AEDF CRC64; MDETLLDDII RRLLATNNGR TVKQAQITET EIRQLCLASK EVFLSQPNLL ELEAPIKICG DVHGQFPDLL RLFEYGGYPP AANYLFLGDY VDRGKQSIET ICLLLAYKVK YKFNFFLLRG NHECASINRV YGFYDECKRR YNVRLWKTFT ECFNCLPVSA LIDDKILCMH GGLSPDIKSL DDIRRIPRPI DVPDQGILCD LLWADPDREI QGWGENDRGV SYTFGADKVA EFLQTHDLDL ICRAHQVVED GYEFFAKRQL VTIFSAPNYC GEFDNAGALM SVDDSLTCSF QILKASEKKG RFGFNNNVPR PGTPPHKGGK GR //