ID   PPX1_ARATH              Reviewed;         305 AA.
AC   P48529;
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 PP-X isozyme 1;
DE            EC=3.1.3.16;
GN   Name=PPX1; Synonyms=EP124, EP129; OrderedLocusNames=At4g26720;
GN   ORFNames=F10M23.60;
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].
RC   TISSUE=Leaf;
RX   PubMed=8292782; DOI=10.1007/bf00042351;
RA   Perez-Callejon E., Casamayor A., Pujol G., Clua E., Ferrer A., Arino J.;
RT   "Identification and molecular cloning of two homologues of protein
RT   phosphatase X from Arabidopsis thaliana.";
RL   Plant Mol. Biol. 23:1177-1185(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11197325; DOI=10.1023/a:1026587405656;
RA   Pujol G., Baskin T.I., Casamayor A., Cortadellas N., Ferrer A., Arino J.;
RT   "The Arabidopsis thaliana PPX/PP4 phosphatases: molecular cloning and
RT   structural organization of the genes and immunolocalization of the proteins
RT   to plastids.";
RL   Plant Mol. Biol. 44:499-511(2000).
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   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 TAP46.
RX   PubMed=21216945; DOI=10.1105/tpc.110.074005;
RA   Ahn C.S., Han J.-A., Lee H.-S., Lee S., Pai H.-S.;
RT   "The PP2A regulatory subunit Tap46, a component of the TOR signaling
RT   pathway, modulates growth and metabolism in plants.";
RL   Plant Cell 23:185-209(2011).
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).
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: Interacts with TAP46. {ECO:0000269|PubMed:21216945,
CC       ECO:0000269|PubMed:24357600}.
CC   -!- SUBCELLULAR LOCATION: Plastid stroma {ECO:0000269|PubMed:11197325}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous, mostly expressed in root mersitems,
CC       flowers, and vascular tissues. {ECO:0000269|PubMed:11197325}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC       subfamily. {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; Z22587; CAA80302.1; -; mRNA.
DR   EMBL; AF030289; AAB86418.1; -; Genomic_DNA.
DR   EMBL; AL035440; CAB36518.1; -; Genomic_DNA.
DR   EMBL; AL161565; CAB79527.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85245.1; -; Genomic_DNA.
DR   PIR; S42558; S42558.
DR   RefSeq; NP_194402.1; NM_118806.6.
DR   AlphaFoldDB; P48529; -.
DR   SMR; P48529; -.
DR   BioGRID; 14066; 2.
DR   IntAct; P48529; 1.
DR   STRING; 3702.P48529; -.
DR   PaxDb; 3702-AT4G26720-1; -.
DR   ProteomicsDB; 226332; -.
DR   EnsemblPlants; AT4G26720.1; AT4G26720.1; AT4G26720.
DR   GeneID; 828779; -.
DR   Gramene; AT4G26720.1; AT4G26720.1; AT4G26720.
DR   KEGG; ath:AT4G26720; -.
DR   Araport; AT4G26720; -.
DR   TAIR; AT4G26720; PPX1.
DR   eggNOG; KOG0372; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; P48529; -.
DR   OMA; CELITEQ; -.
DR   OrthoDB; 19833at2759; -.
DR   PhylomeDB; P48529; -.
DR   PRO; PR:P48529; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P48529; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0009532; C:plastid stroma; IEA:UniProtKB-SubCell.
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:0007131; P:reciprocal meiotic recombination; IMP:TAIR.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF29; SERINE_THREONINE-PROTEIN PHOSPHATASE PP-X ISOZYME 1; 1.
DR   Pfam; PF00149; Metallophos; 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; P48529; AT.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Metal-binding; Plastid; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..305
FT                   /note="Serine/threonine-protein phosphatase PP-X isozyme 1"
FT                   /id="PRO_0000058886"
FT   ACT_SITE        112
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  34738 MW;  3FBBEADB2DA5B650 CRC64;
     MSDLDRQIGQ LKRCEPLSES EVKALCLKAM EILVEESNVQ RVDAPVTLCG DIHGQFYDMM
     ELFKVGGDCP KTNYLFMGDF VDRGYYSVET FLLLLALKVR YPDRITLIRG NHESRQITQV
     YGFYDECLRK YGSSNVWRYC TDIFDYMSLS AVVENKIFCV HGGLSPAIMT LDQIRTIDRK
     QEVPHDGAMC DLLWSDPEDI VDGWGLSPRG AGFLFGGSVV TSFNHSNNID YIARAHQLVM
     EGYKWMFDSQ IVTVWSAPNY CYRCGNVASI LELDENLNKE FRVFDAAQQD SRGPPAKKPA
     PDYFL
//