ID   P2C14_ARATH             Reviewed;         445 AA.
AC   Q9FXE4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Probable protein phosphatase 2C 14;
DE            Short=AtPP2C14;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase AP2C4;
GN   OrderedLocusNames=At1g67820; ORFNames=F12A21.5;
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 [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 [LARGE SCALE MRNA].
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   [4]
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG28911.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BX813565; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AC008113; AAG28911.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34702.1; -; Genomic_DNA.
DR   EMBL; BX813565; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; H96700; H96700.
DR   RefSeq; NP_176948.2; NM_105450.4.
DR   AlphaFoldDB; Q9FXE4; -.
DR   SMR; Q9FXE4; -.
DR   BioGRID; 28329; 2.
DR   STRING; 3702.Q9FXE4; -.
DR   iPTMnet; Q9FXE4; -.
DR   PaxDb; 3702-AT1G67820-1; -.
DR   ProteomicsDB; 248793; -.
DR   EnsemblPlants; AT1G67820.1; AT1G67820.1; AT1G67820.
DR   GeneID; 843108; -.
DR   Gramene; AT1G67820.1; AT1G67820.1; AT1G67820.
DR   KEGG; ath:AT1G67820; -.
DR   Araport; AT1G67820; -.
DR   TAIR; AT1G67820; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_5_1_1; -.
DR   InParanoid; Q9FXE4; -.
DR   OrthoDB; 1112856at2759; -.
DR   PhylomeDB; Q9FXE4; -.
DR   PRO; PR:Q9FXE4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FXE4; 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; IPR000222; PP2C_BS.
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:SF86; PROTEIN-SERINE_THREONINE PHOSPHATASE; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; Q9FXE4; AT.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..445
FT                   /note="Probable protein phosphatase 2C 14"
FT                   /id="PRO_0000367945"
FT   DOMAIN          120..440
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          384..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         431
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  49353 MW;  C0E01A328F2F4CFF CRC64;
     MTNKLRSEET ITSLSSFMAS TLSIASPSPC SIPLSVTKVS PLKRKRPTHL NIPDLNPQQP
     ISTDYFRFRE GDAKVSPLKR KRPAHLNIPD LNPQQPIRTD YFSFTDFAHQ NGTVSFGGNG
     FGVVSRNGKK KFMEDTHRIV PCLVGNSKKS FFGVYDGHGG AKAAEFVAEN LHKYVVEMME
     NCKGKEEKVE AFKAAFLRTD RDFLEKGVVS GACCVTAVIQ DQEMIVSNLG DCRAVLCRAG
     VAEALTDDHK PGRDDEKERI ESQGGYVDNH QGAWRVQGIL AVSRSIGDAH LKKWVVAEPE
     TRVLELEQDM EFLVLASDGL WDVVSNQEAV YTVLHVLAQR KTPKESEEEN LVQGFVNMSP
     SSKLRRASLV KSPRCAKSQS YYYNSENESP SLNREIGSSP SKSPITPWKS LWAKAACKEL
     ANLAAKRGSM DDITVVIIDL NHYKG
//