P2C22_ARATH
ID P2C22_ARATH Reviewed; 392 AA.
AC Q9SLA1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable protein phosphatase 2C 22;
DE Short=AtPP2C22;
DE EC=3.1.3.16;
GN OrderedLocusNames=At2g25620; ORFNames=F3N11.7;
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 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 -!- 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 -!- INTERACTION:
CC Q9SLA1; Q9FTA2: TCP21; NbExp=3; IntAct=EBI-15193303, EBI-4426168;
CC Q9SLA1; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15193303, EBI-15192325;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006053; AAD31375.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07725.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61961.1; -; Genomic_DNA.
DR EMBL; AF326901; AAG41483.1; -; mRNA.
DR EMBL; AF339719; AAK00401.1; -; mRNA.
DR EMBL; AF436827; AAL32009.1; -; mRNA.
DR EMBL; AY039595; AAK62650.1; -; mRNA.
DR EMBL; AY057740; AAL15370.1; -; mRNA.
DR EMBL; BT002487; AAO00847.1; -; mRNA.
DR PIR; F84650; F84650.
DR RefSeq; NP_001324148.1; NM_001336005.1.
DR RefSeq; NP_180133.1; NM_128120.2.
DR AlphaFoldDB; Q9SLA1; -.
DR SMR; Q9SLA1; -.
DR BioGRID; 2454; 48.
DR IntAct; Q9SLA1; 46.
DR STRING; 3702.AT2G25620.1; -.
DR iPTMnet; Q9SLA1; -.
DR PaxDb; Q9SLA1; -.
DR PRIDE; Q9SLA1; -.
DR ProteomicsDB; 248874; -.
DR EnsemblPlants; AT2G25620.1; AT2G25620.1; AT2G25620.
DR EnsemblPlants; AT2G25620.2; AT2G25620.2; AT2G25620.
DR GeneID; 817102; -.
DR Gramene; AT2G25620.1; AT2G25620.1; AT2G25620.
DR Gramene; AT2G25620.2; AT2G25620.2; AT2G25620.
DR KEGG; ath:AT2G25620; -.
DR Araport; AT2G25620; -.
DR TAIR; locus:2050296; AT2G25620.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_21_2_1; -.
DR InParanoid; Q9SLA1; -.
DR OMA; RDHKPIC; -.
DR OrthoDB; 957254at2759; -.
DR PhylomeDB; Q9SLA1; -.
DR PRO; PR:Q9SLA1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLA1; baseline and differential.
DR Genevisible; Q9SLA1; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0050688; P:regulation of defense response to virus; IMP: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 Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..392
FT /note="Probable protein phosphatase 2C 22"
FT /id="PRO_0000367952"
FT DOMAIN 89..356
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 392 AA; 42674 MW; AC09DC922197BE53 CRC64;
MEETRGISDP ENGSSSYGGK PPNPLSFSSS SAAAAVYRQT FDGERSLAPC NKRSLVRHSS
LVKTMVSDIS VENEFTIEKN KSEFVPATRS GAWSDIGSRS SMEDAYLCVD NFMDSFGLLN
SEAGPSAFYG VFDGHGGKHA AEFACHHIPR YIVEDQEFPS EINKVLSSAF LQTDTAFLEA
CSLDGSLASG TTALAAILFG RSLVVANAGD CRAVLSRQGK AIEMSRDHKP MSSKERRRIE
ASGGHVFDGY LNGQLNVARA LGDFHMEGMK KKKDGSDCGP LIAEPELMTT KLTEEDEFLI
IGCDGVWDVF MSQNAVDFAR RRLQEHNDPV MCSKELVEEA LKRKSADNVT AVVVCLQPQP
PPNLVAPRLR VHRSFSAEGL KDLQSYLDGL GN
