P2C20_ARATH
ID P2C20_ARATH Reviewed; 290 AA.
AC Q9SIU8; Q680F4; Q945Q0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable protein phosphatase 2C 20;
DE Short=AtPP2C20;
DE EC=3.1.3.16;
DE AltName: Full=AtPPC3;1.2;
GN Name=PPC3-1.2; OrderedLocusNames=At2g20630; ORFNames=F23N11.5;
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 [MRNA] (ISOFORM 2).
RA Izumi S., Yamada M., Ohsato H., Miyazaki S., Bohnert H.J., Fukuhara T.;
RT "Substrate specificity of type 2C protein phosphatases (PP2C) in
RT Arabidopsis thaliana.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 56-69 AND 103-116.
RX PubMed=10036779; DOI=10.1046/j.1365-313x.1998.00335.x;
RA Santoni V., Rouquie D., Doumas P., Mansion M., Boutry M., Degand H.,
RA Dupree P., Packman L., Sherrier J., Prime T., Bauw G., Posada E., Rouze P.,
RA Dehais P., Sahnoun I., Barlier I., Rossignol M.;
RT "Use of a proteome strategy for tagging proteins present at the plasma
RT membrane.";
RL Plant J. 16:633-641(1998).
RN [8]
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).
RN [9]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19053141; DOI=10.1002/pmic.200800293;
RA Widjaja I., Naumann K., Roth U., Wolf N., Mackey D., Dangl J.L., Scheel D.,
RA Lee J.;
RT "Combining subproteome enrichment and Rubisco depletion enables
RT identification of low abundance proteins differentially regulated during
RT plant defense.";
RL Proteomics 9:138-147(2009).
CC -!- FUNCTION: May be involved in defense signaling.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SIU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SIU8-2; Sequence=VSP_036763, VSP_036764;
CC -!- INDUCTION: By the avirulence factor AvrRpm1 (at protein level).
CC {ECO:0000269|PubMed:19053141}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX842471; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB079672; BAB84701.1; -; mRNA.
DR EMBL; AC007048; AAD21710.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07049.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07050.1; -; Genomic_DNA.
DR EMBL; AF411787; AAL06477.1; -; mRNA.
DR EMBL; AY093793; AAM10409.1; -; mRNA.
DR EMBL; BX842471; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK175113; BAD42876.1; -; mRNA.
DR EMBL; AK175149; BAD42912.1; -; mRNA.
DR EMBL; AK175260; BAD43023.1; -; mRNA.
DR EMBL; AK175913; BAD43676.1; -; mRNA.
DR EMBL; AK175927; BAD43690.1; -; mRNA.
DR EMBL; AK176179; BAD43942.1; -; mRNA.
DR EMBL; AK176199; BAD43962.1; -; mRNA.
DR EMBL; AK176314; BAD44077.1; -; mRNA.
DR EMBL; AK220638; BAD95097.1; -; mRNA.
DR PIR; E84591; E84591.
DR RefSeq; NP_565480.1; NM_127627.3. [Q9SIU8-2]
DR RefSeq; NP_973490.1; NM_201761.1. [Q9SIU8-1]
DR AlphaFoldDB; Q9SIU8; -.
DR SMR; Q9SIU8; -.
DR BioGRID; 1943; 1.
DR IntAct; Q9SIU8; 1.
DR STRING; 3702.AT2G20630.2; -.
DR iPTMnet; Q9SIU8; -.
DR PaxDb; Q9SIU8; -.
DR PRIDE; Q9SIU8; -.
DR ProteomicsDB; 248704; -. [Q9SIU8-1]
DR EnsemblPlants; AT2G20630.1; AT2G20630.1; AT2G20630. [Q9SIU8-2]
DR EnsemblPlants; AT2G20630.2; AT2G20630.2; AT2G20630. [Q9SIU8-1]
DR GeneID; 816590; -.
DR Gramene; AT2G20630.1; AT2G20630.1; AT2G20630. [Q9SIU8-2]
DR Gramene; AT2G20630.2; AT2G20630.2; AT2G20630. [Q9SIU8-1]
DR KEGG; ath:AT2G20630; -.
DR Araport; AT2G20630; -.
DR TAIR; locus:2046046; AT2G20630.
DR eggNOG; KOG0698; Eukaryota.
DR InParanoid; Q9SIU8; -.
DR OMA; KMWKNIA; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9SIU8; -.
DR PRO; PR:Q9SIU8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIU8; baseline and differential.
DR Genevisible; Q9SIU8; AT.
DR GO; GO:0005739; C:mitochondrion; 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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
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 Alternative splicing; Direct protein sequencing; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Protein phosphatase; Reference proteome.
FT CHAIN 1..290
FT /note="Probable protein phosphatase 2C 20"
FT /id="PRO_0000367950"
FT DOMAIN 31..278
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 68
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 276..279
FT /note="PCFL -> VRFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.6"
FT /id="VSP_036763"
FT VAR_SEQ 280..290
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.6"
FT /id="VSP_036764"
FT CONFLICT 39
FT /note="G -> D (in Ref. 5; BAD43676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31847 MW; 622AB1EEC1D739CB CRC64;
MAGREILHKM KVGLCGSDTG RGKTKVWKNI AHGYDFVKGK AGHPMEDYVV SEFKKVDGHD
LGLFAIFDGH LGHDVAKYLQ TNLFDNILKE KDFWTDTKNA IRNAYISTDA VILEQSLKLG
KGGSTAVTGI LIDGKTLVIA NVGDSRAVMS KNGVASQLSV DHEPSKEQKE IESRGGFVSN
IPGDVPRVDG QLAVARAFGD KSLKIHLSSD PDIRDENIDH ETEFILFASD GVWKVMSNQE
AVDLIKSIKD PQAAAKELIE EAVSKQSTDD ISCIVPCFLR REALSERYCR
