P2C25_ARATH
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 03-AUG-2022, entry version 137.
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.AT2G30020.1; -.
DR PaxDb; O80871; -.
DR PRIDE; O80871; -.
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; locus:2045678; AT2G30020.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_5_1_1; -.
DR InParanoid; O80871; -.
DR OMA; TFHGVWR; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; O80871; -.
DR PRO; PR:O80871; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80871; baseline and differential.
DR Genevisible; O80871; AT.
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:0006470; P:protein dephosphorylation; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
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
