PPX1_ARATH
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 03-AUG-2022, entry version 152.
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}.
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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.AT4G26720.1; -.
DR PaxDb; P48529; -.
DR PRIDE; P48529; -.
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; locus:2116402; AT4G26720.
DR eggNOG; KOG0372; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; P48529; -.
DR OMA; FKCFGPS; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; P48529; -.
DR PRO; PR:P48529; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P48529; baseline and differential.
DR Genevisible; P48529; AT.
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:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP: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 Pfam; PF00149; Metallophos; 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 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
