ID   PP19_ARATH              Reviewed;         318 AA.
AC   Q9M9W3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1 isozyme 9 {ECO:0000305};
DE            EC=3.1.3.16 {ECO:0000269|PubMed:21222654};
DE   AltName: Full=Type one protein phosphatase 9 {ECO:0000303|PubMed:17368080};
GN   Name=TOPP9 {ECO:0000303|PubMed:17368080}; OrderedLocusNames=At3g05580;
GN   ORFNames=F18C1.15;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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   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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND 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).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm
CC       {ECO:0000269|PubMed:19329567}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC011620; AAF26139.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74262.1; -; Genomic_DNA.
DR   EMBL; BT010532; AAQ65155.1; -; mRNA.
DR   EMBL; AK175443; BAD43206.1; -; mRNA.
DR   RefSeq; NP_187209.1; NM_111431.4.
DR   AlphaFoldDB; Q9M9W3; -.
DR   SMR; Q9M9W3; -.
DR   BioGRID; 5059; 3.
DR   IntAct; Q9M9W3; 2.
DR   STRING; 3702.Q9M9W3; -.
DR   PaxDb; 3702-AT3G05580-1; -.
DR   ProteomicsDB; 250507; -.
DR   EnsemblPlants; AT3G05580.1; AT3G05580.1; AT3G05580.
DR   GeneID; 819724; -.
DR   Gramene; AT3G05580.1; AT3G05580.1; AT3G05580.
DR   KEGG; ath:AT3G05580; -.
DR   Araport; AT3G05580; -.
DR   TAIR; AT3G05580; TOPP9.
DR   eggNOG; KOG0374; Eukaryota.
DR   HOGENOM; CLU_004962_0_0_1; -.
DR   InParanoid; Q9M9W3; -.
DR   OMA; HESESIC; -.
DR   OrthoDB; 5484004at2759; -.
DR   PhylomeDB; Q9M9W3; -.
DR   PRO; PR:Q9M9W3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M9W3; baseline and differential.
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; IDA:TAIR.
DR   GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR   GO; GO:0048768; P:root hair cell tip growth; IGI: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:SF429; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 9; 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; Q9M9W3; AT.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..318
FT                   /note="Serine/threonine-protein phosphatase PP1 isozyme 9"
FT                   /id="PRO_0000308987"
FT   ACT_SITE        127
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  36001 MW;  548C712D728C099D CRC64;
     MMTSMEGMME MGVLDDIIRR LLEGKGGKQV QLSEVEIRQL CVNARQIFLS QPNLLELHAP
     IRICGDIHGQ YQDLLRLFEY GGYPPSANYL FLGDYVDRGK QSLETICLLL AYKIRYPSKI
     FLLRGNHEDA KINRIYGFYD ECKRRFNVRL WKIFTDCFNC LPVAALIDEK ILCMHGGLSP
     ELENLGQIRE IQRPTEIPDN GLLCDLLWSD PDQKNEGWTD SDRGISCTFG ADVVADFLDK
     NDLDLICRGH QVVEDGYEFF AKRRLVTIFS APNYGGEFDN AGALLSVDQS LVCSFEILKP
     APASSTNPLK KVPKMGKS
//