P2C39_ARATH
ID P2C39_ARATH Reviewed; 289 AA.
AC Q9LDA7; Q8L834;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable protein phosphatase 2C 39;
DE Short=AtPP2C39;
DE EC=3.1.3.16;
GN OrderedLocusNames=At3g15260; ORFNames=K7L4.6;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [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 -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AP000413; BAB02155.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75637.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75638.1; -; Genomic_DNA.
DR EMBL; AK117480; BAC42144.1; -; mRNA.
DR EMBL; AY120770; AAM53328.1; -; mRNA.
DR EMBL; BT008532; AAP40359.1; -; mRNA.
DR RefSeq; NP_188144.1; NM_112389.4.
DR RefSeq; NP_974318.1; NM_202589.2.
DR AlphaFoldDB; Q9LDA7; -.
DR SMR; Q9LDA7; -.
DR BioGRID; 6091; 1.
DR IntAct; Q9LDA7; 1.
DR MINT; Q9LDA7; -.
DR STRING; 3702.AT3G15260.2; -.
DR iPTMnet; Q9LDA7; -.
DR PaxDb; Q9LDA7; -.
DR PRIDE; Q9LDA7; -.
DR ProteomicsDB; 248877; -.
DR EnsemblPlants; AT3G15260.1; AT3G15260.1; AT3G15260.
DR EnsemblPlants; AT3G15260.2; AT3G15260.2; AT3G15260.
DR GeneID; 820757; -.
DR Gramene; AT3G15260.1; AT3G15260.1; AT3G15260.
DR Gramene; AT3G15260.2; AT3G15260.2; AT3G15260.
DR KEGG; ath:AT3G15260; -.
DR Araport; AT3G15260; -.
DR TAIR; locus:2087095; AT3G15260.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_0_1_1; -.
DR InParanoid; Q9LDA7; -.
DR OMA; NMERQTI; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9LDA7; -.
DR PRO; PR:Q9LDA7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LDA7; baseline and differential.
DR Genevisible; Q9LDA7; AT.
DR GO; GO:0005829; C:cytosol; HDA: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 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 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..289
FT /note="Probable protein phosphatase 2C 39"
FT /id="PRO_0000367964"
FT DOMAIN 41..288
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 55
FT /note="M -> I (in Ref. 4; AAM53328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 31630 MW; D37C3DE3BF2F481B CRC64;
MTGREILHKM KESVKEKVGL GASASSADSG KGKSKMLKQI THGFHLVKGK AFHEMEDYVV
AKFKEVDDNE LGLFAIFDGH LSHEIPDYLC SHLFENILKE PNFWQEPEKA IKKAYYITDT
TILDKADDLG KGGSTAVTAI LINCQKLVVA NVGDSRAVIC QNGVAKPLSV DHEPNMEKDE
IENRGGFVSN FPGDVPRVDG QLAVARAFGD KSLKMHLSSE PYVTVEIIDD DAEFLILASD
GLWKVMSNQE AVDSIKGIKD AKAAAKHLAE EAVARKSSDD ISVVVVKFQ
