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   24-JAN-2024, entry version 126.
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.Q9LR65; -.
DR   iPTMnet; Q9LR65; -.
DR   PaxDb; 3702-AT1G03590-1; -.
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; AT1G03590; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_6_0_1; -.
DR   InParanoid; Q9LR65; -.
DR   OMA; PCLQRNV; -.
DR   OrthoDB; 1450097at2759; -.
DR   PhylomeDB; Q9LR65; -.
DR   PRO; PR:Q9LR65; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LR65; 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; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR47992:SF34; PROTEIN PHOSPHATASE 2C 1-RELATED; 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; Q9LR65; AT.
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
//