ID   P2C25_ARATH             Reviewed;         396 AA.
AC   O80871;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Probable protein phosphatase 2C 25;
DE            Short=AtPP2C25;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase AP2C1;
GN   OrderedLocusNames=At2g30020; ORFNames=F23F1.6;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH MAPK4 AND
RP   MAPK6, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-98; ARG-99 AND GLY-178.
RX   PubMed=17630279; DOI=10.1105/tpc.106.049585;
RA   Schweighofer A., Kazanaviciute V., Scheikl E., Teige M., Doczi R., Hirt H.,
RA   Schwanninger M., Kant M., Schuurink R., Mauch F., Buchala A., Cardinale F.,
RA   Meskiene I.;
RT   "The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and MPK6,
RT   modulates innate immunity, jasmonic acid, and ethylene levels in
RT   Arabidopsis.";
RL   Plant Cell 19:2213-2224(2007).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA   Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT   "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT   Arabidopsis.";
RL   BMC Genomics 9:550-550(2008).
CC   -!- FUNCTION: Protein phosphatase that negatively regulates defense
CC       respones. Inactivates MPK4 and MPK6 MAP kinases involved in stress and
CC       defense signaling. {ECO:0000269|PubMed:17630279}.
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=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with MPK4 and MPK6. {ECO:0000269|PubMed:17630279}.
CC   -!- INTERACTION:
CC       O80871; Q39024: MPK4; NbExp=3; IntAct=EBI-16897073, EBI-994375;
CC       O80871; Q39026: MPK6; NbExp=3; IntAct=EBI-16897073, EBI-349548;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17630279}. Nucleus
CC       {ECO:0000269|PubMed:17630279}.
CC   -!- INDUCTION: By wounding. {ECO:0000269|PubMed:17630279}.
CC   -!- DISRUPTION PHENOTYPE: High jasmonate production and PDF1.2 expression
CC       upon wounding. Slight reduction of lesion size caused by fungal
CC       pathogen. Slight decrease of spider mite reproductive performance.
CC       {ECO:0000269|PubMed:17630279}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AC004680; AAC31850.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08336.1; -; Genomic_DNA.
DR   EMBL; AF370594; AAK43913.1; -; mRNA.
DR   PIR; T02483; T02483.
DR   RefSeq; NP_180563.1; NM_128557.4.
DR   AlphaFoldDB; O80871; -.
DR   SMR; O80871; -.
DR   BioGRID; 2903; 15.
DR   IntAct; O80871; 13.
DR   STRING; 3702.O80871; -.
DR   PaxDb; 3702-AT2G30020-1; -.
DR   ProteomicsDB; 248708; -.
DR   EnsemblPlants; AT2G30020.1; AT2G30020.1; AT2G30020.
DR   GeneID; 817553; -.
DR   Gramene; AT2G30020.1; AT2G30020.1; AT2G30020.
DR   KEGG; ath:AT2G30020; -.
DR   Araport; AT2G30020; -.
DR   TAIR; AT2G30020; AP2C1.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_5_1_1; -.
DR   InParanoid; O80871; -.
DR   OMA; IQLGQFC; -.
DR   OrthoDB; 1215619at2759; -.
DR   PhylomeDB; O80871; -.
DR   PRO; PR:O80871; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80871; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; 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:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR47992:SF86; PROTEIN-SERINE_THREONINE PHOSPHATASE; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; O80871; AT.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..396
FT                   /note="Probable protein phosphatase 2C 25"
FT                   /id="PRO_0000367954"
FT   DOMAIN          139..392
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          32..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
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         176
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         383
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         98
FT                   /note="K->A: Abolishes interaction with MPK4 and MPK6; when
FT                   associated with Q-99."
FT                   /evidence="ECO:0000269|PubMed:17630279"
FT   MUTAGEN         99
FT                   /note="R->Q: Abolishes interaction with MPK4 and MPK6; when
FT                   associated with A-98."
FT                   /evidence="ECO:0000269|PubMed:17630279"
FT   MUTAGEN         178
FT                   /note="G->D: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17630279"
SQ   SEQUENCE   396 AA;  42420 MW;  EB1ACBD10113022F CRC64;
     MSCSVAVCNS PVFSPSSSLF CNKSSILSSP QESLSLTLSH RKPQTSSPSS PSTTVSSPKS
     PFRLRFQKPP SGFAPGPLSF GSESVSASSP PGGVLKRKRP TRLDIPIGVA GFVAPISSSA
     AVAATPREEC REVEREGDGY SVYCKRGRRE AMEDRFSAIT NLHGDRKQAI FGVYDGHGGV
     KAAEFAAKNL DKNIVEEVVG KRDESEIAEA VKHGYLATDA SFLKEEDVKG GSCCVTALVN
     EGNLVVSNAG DCRAVMSVGG VAKALSSDHR PSRDDERKRI ETTGGYVDTF HGVWRIQGSL
     AVSRGIGDAQ LKKWVIAEPE TKISRIEHDH EFLILASDGL WDKVSNQEAV DIARPLCLGT
     EKPLLLAACK KLVDLSASRG SSDDISVMLI PLRQFI
//