P2C01_ARATH
ID P2C01_ARATH Reviewed; 462 AA.
AC Q9LR65; Q8SBC2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable protein phosphatase 2C 1;
DE Short=AtPP2C01;
DE EC=3.1.3.16;
DE AltName: Full=AtPPC6;6;
GN Name=PPC6-6; OrderedLocusNames=At1g03590; ORFNames=F21B7.20;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 [MRNA] OF 43-462.
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 [4]
RP FUNCTION, AND INTERACTION WITH GCN5.
RX PubMed=18498779; DOI=10.1016/j.bbagrm.2008.04.007;
RA Servet C., Benhamed M., Latrasse D., Kim W., Delarue M., Zhou D.-X.;
RT "Characterization of a phosphatase 2C protein as an interacting partner of
RT the histone acetyltransferase GCN5 in Arabidopsis.";
RL Biochim. Biophys. Acta 1779:376-382(2008).
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 -!- FUNCTION: May act as negative regulator of GCN5.
CC {ECO:0000269|PubMed:18498779}.
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 -!- SUBUNIT: Interacts with GCN5. {ECO:0000269|PubMed:18498779}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC002560; AAF86530.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27587.1; -; Genomic_DNA.
DR EMBL; AB079670; BAB84699.1; -; mRNA.
DR PIR; T00901; T00901.
DR RefSeq; NP_171856.4; NM_100239.8.
DR AlphaFoldDB; Q9LR65; -.
DR SMR; Q9LR65; -.
DR BioGRID; 24682; 1.
DR STRING; 3702.AT1G03590.1; -.
DR iPTMnet; Q9LR65; -.
DR PaxDb; Q9LR65; -.
DR PRIDE; Q9LR65; -.
DR ProteomicsDB; 248788; -.
DR EnsemblPlants; AT1G03590.1; AT1G03590.1; AT1G03590.
DR GeneID; 839447; -.
DR Gramene; AT1G03590.1; AT1G03590.1; AT1G03590.
DR KEGG; ath:AT1G03590; -.
DR Araport; AT1G03590; -.
DR TAIR; locus:2020863; AT1G03590.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_6_0_1; -.
DR InParanoid; Q9LR65; -.
DR OMA; DNEEQCF; -.
DR OrthoDB; 1344250at2759; -.
DR PhylomeDB; Q9LR65; -.
DR PRO; PR:Q9LR65; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LR65; baseline and differential.
DR Genevisible; Q9LR65; 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: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 Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..462
FT /note="Probable protein phosphatase 2C 1"
FT /id="PRO_0000367935"
FT DOMAIN 60..362
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 369..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 462 AA; 50975 MW; F264E7DA32C7E472 CRC64;
MGGCISKTSW SNEEPMHRPC LGMGCCGSKM GKRGFSDRMV SLHNLVSIPN RIIGNGKSRS
SCIFTQQGRK GINQDAMIVW EDFMSKDVTF CGVFDGHGPH GHLVARKVRD SLPVKLLSLL
NSIKSKQNGP IGTRASKSDS LEAEKEESTE EDKLNFLWEE AFLKSFNAMD KELRSHPNLE
CFCSGCTAVT IIKQGSNLYM GNIGDSRAIL GSKDSNDSMI AVQLTVDLKP DLPREAERIK
QCKGRVFALQ DEPEVSRVWL PFDNAPGLAM ARAFGDFCLK DYGVISIPEF SHRVLTDRDQ
FIVLASDGVW DVLSNEEVVE VVASATSRAS AARLVVDSAV REWKLKYPTS KMDDCAVVCL
FLDGRMDSET SDNEEQCFSS ATNAVESDES QGAEPCLQRN VTVRSLSTDQ ENNSYGKVIA
EADNAEKEKT REGEQNWSGL EGVTRVNSLV QLPRFPGEEP KT
