PPX2_ARATH
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 03-AUG-2022, entry version 149.
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.AT5G55260.1; -.
DR PaxDb; P48528; -.
DR PRIDE; P48528; -.
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; locus:2161700; AT5G55260.
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 Genevisible; P48528; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IGI: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 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
