ID   PPX2_ARATH              Reviewed;         305 AA.
AC   P48528; O22626; Q29Q40;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Serine/threonine-protein phosphatase PP-X isozyme 2;
DE            EC=3.1.3.16;
GN   Name=PPX2; OrderedLocusNames=At5g55260; ORFNames=MCO15.21;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(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;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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).
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   -!- 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; Z22596; CAA80312.1; -; mRNA.
DR   EMBL; AF030290; AAB86419.1; -; Genomic_DNA.
DR   EMBL; AB010071; BAB08595.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96607.1; -; Genomic_DNA.
DR   EMBL; BT024716; ABD59054.1; -; mRNA.
DR   PIR; S42559; S42559.
DR   RefSeq; NP_200337.1; NM_124908.4.
DR   AlphaFoldDB; P48528; -.
DR   SMR; P48528; -.
DR   STRING; 3702.P48528; -.
DR   iPTMnet; P48528; -.
DR   PaxDb; 3702-AT5G55260-1; -.
DR   ProteomicsDB; 236589; -.
DR   EnsemblPlants; AT5G55260.1; AT5G55260.1; AT5G55260.
DR   GeneID; 835619; -.
DR   Gramene; AT5G55260.1; AT5G55260.1; AT5G55260.
DR   KEGG; ath:AT5G55260; -.
DR   Araport; AT5G55260; -.
DR   TAIR; AT5G55260; PPX2.
DR   eggNOG; KOG0372; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; P48528; -.
DR   PhylomeDB; P48528; -.
DR   PRO; PR:P48528; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P48528; baseline and differential.
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; ISS:TAIR.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IGI: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:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC SUBUNIT; 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; P48528; AT.
PE   2: Evidence at transcript 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 2"
FT                   /id="PRO_0000058887"
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"
FT   CONFLICT        73
FT                   /note="N -> H (in Ref. 1; CAA80312)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="S -> L (in Ref. 1; CAA80312)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   305 AA;  34726 MW;  77DF2B662F3B1FB1 CRC64;
     MSDLDKQIEQ LKRCEALKES EVKALCLKAM EILVEESNVQ RVDAPVTICG DIHGQFYDMK
     ELFKVGGDCP KTNYLFLGDF VDRGFYSVET FLLLLALKVR YPDRITLIRG NHESRQITQV
     YGFYDECLRK YGSVNVWRYC TDIFDYLSLS ALVENKIFCV HGGLSPAIMT LDQIRAIDRK
     QEVPHDGAMC DLLWSDPEDI VDGWGLSPRG AGFLFGGSVV TSFNHSNNID YICRAHQLVM
     EGYKWMFNSQ IVTVWSAPNY CYRCGNVAAI LELDENLNKE FRVFDAAPQE SRGALAKKPA
     PDYFL
//