P2C40_ARATH
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 03-AUG-2022, entry version 123.
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}.
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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; 1.
DR STRING; 3702.AT3G16560.1; -.
DR iPTMnet; Q9LUS8; -.
DR PaxDb; Q9LUS8; -.
DR PRIDE; Q9LUS8; -.
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; locus:2089293; AT3G16560.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_12_3_1; -.
DR InParanoid; Q9LUS8; -.
DR OMA; NLLDWEM; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q9LUS8; -.
DR PRO; PR:Q9LUS8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUS8; baseline and differential.
DR Genevisible; Q9LUS8; AT.
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 CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
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; PS51746; PPM_2; 1.
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
