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 24-JAN-2024, entry version 145. 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.Q9SLA1; -. DR iPTMnet; Q9SLA1; -. DR PaxDb; 3702-AT2G25620-1; -. 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; AT2G25620; DBP1. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_21_2_1; -. DR InParanoid; Q9SLA1; -. DR OMA; RDHKPIC; -. DR OrthoDB; 91820at2759; -. DR PhylomeDB; Q9SLA1; -. DR PRO; PR:Q9SLA1; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q9SLA1; baseline and differential. 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:0050688; P:regulation of defense response to virus; IMP: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; PTHR13832; PROTEIN PHOSPHATASE 2C; 1. DR PANTHER; PTHR13832:SF790; PROTEIN PHOSPHATASE 2C 22-RELATED; 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; Q9SLA1; AT. 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 //