ID P2C40_ARATH Reviewed; 493 AA. AC Q9LUS8; Q8LCU0; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=Probable protein phosphatase 2C 40; DE Short=AtPP2C40; DE EC=3.1.3.16; DE AltName: Full=Protein phosphatase 2C homolog 1; GN OrderedLocusNames=At3g16560; ORFNames=MDC8.3; 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=10819329; DOI=10.1093/dnares/7.2.131; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. 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 -!- 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 Q9LUS8; Q17TI5: BRX; NbExp=3; IntAct=EBI-25519200, EBI-4426649; 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; AB022217; BAB02747.1; -; Genomic_DNA. DR EMBL; CP002686; AEE75836.1; -; Genomic_DNA. DR EMBL; CP002686; ANM63918.1; -; Genomic_DNA. DR EMBL; CP002686; ANM63920.1; -; Genomic_DNA. DR EMBL; AY136458; AAM97123.1; -; mRNA. DR EMBL; BT008864; AAP68303.1; -; mRNA. DR EMBL; AY086406; AAM64473.1; -; mRNA. DR RefSeq; NP_001325978.1; NM_001338238.1. DR RefSeq; NP_001325980.1; NM_001338240.1. DR RefSeq; NP_566554.1; NM_112529.3. DR AlphaFoldDB; Q9LUS8; -. DR SMR; Q9LUS8; -. DR BioGRID; 6239; 1. DR IntAct; Q9LUS8; 2. DR STRING; 3702.Q9LUS8; -. DR iPTMnet; Q9LUS8; -. DR PaxDb; 3702-AT3G16560-1; -. DR ProteomicsDB; 248798; -. DR EnsemblPlants; AT3G16560.1; AT3G16560.1; AT3G16560. DR EnsemblPlants; AT3G16560.2; AT3G16560.2; AT3G16560. DR EnsemblPlants; AT3G16560.4; AT3G16560.4; AT3G16560. DR GeneID; 820905; -. DR Gramene; AT3G16560.1; AT3G16560.1; AT3G16560. DR Gramene; AT3G16560.2; AT3G16560.2; AT3G16560. DR Gramene; AT3G16560.4; AT3G16560.4; AT3G16560. DR KEGG; ath:AT3G16560; -. DR Araport; AT3G16560; -. DR TAIR; AT3G16560; -. DR eggNOG; KOG0700; Eukaryota. DR HOGENOM; CLU_013173_12_3_1; -. DR InParanoid; Q9LUS8; -. DR OMA; GIDNCHG; -. DR OrthoDB; 999128at2759; -. DR PhylomeDB; Q9LUS8; -. DR PRO; PR:Q9LUS8; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9LUS8; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR13832:SF550; PROTEIN PHOSPHATASE 1L; 1. DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; Q9LUS8; AT. PE 1: Evidence at protein level; KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..493 FT /note="Probable protein phosphatase 2C 40" FT /id="PRO_0000301257" FT DOMAIN 145..480 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT BINDING 180 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 180 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 408 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 471 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT CONFLICT 372 FT /note="G -> E (in Ref. 4; AAM64473)" FT /evidence="ECO:0000305" SQ SEQUENCE 493 AA; 53614 MW; 613ED80B06B8C844 CRC64; MQEGTDPYGE IEISFGYQCN NKKIGIPEDK IADGREVLGG FRLQKTSSFS CLSGAALSGN PTLANTNICN GVIGSEILPS LDSPKSFRKV PSSPALSKLD ILSPSLHGSM VSLSCSSSTS PSPPEPESCY LTSMSSPSSV NEGFLLSAME VQVAGGAAGE DRVQAVCSEE NGWLFCAIYD GFNGRDAADF LACTLYESIV FHLQLLDRQM KQTKSDDDGE KLELLSNISN VDYSSTDLFR QGVLDCLNRA LFQAETDFLR MVEQEMEERP DLVSVGSCVL VTLLVGKDLY VLNLGDSRAV LATYNGNKKL QAVQLTEDHT VDNEVEEARL LSEHLDDPKI VIGGKIKGKL KVTRALGVGY LKKEKLNDAL MGILRVRNLL SPPYVSVEPS MRVHKITESD HFVIVASDGL FDFFSNEEAI GLVHSFVSSN PSGDPAKFLL ERLVAKAAAR AGFTLEELTN VPAGRRRRYH DDVTIMVITL GTDQRTSKAS TFV //