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P2C28_ARATH
ID   P2C28_ARATH             Reviewed;         339 AA.
AC   O64583; F4IIV1; F4IIV2; Q681L4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Probable protein phosphatase 2C 28;
DE            Short=AtPP2C28;
DE            EC=3.1.3.16;
GN   OrderedLocusNames=At2g34740; ORFNames=T29F13.5;
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=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   [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] OF 170-339 (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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O64583-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O64583-2; Sequence=VSP_041311;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC16260.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AEC09017.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC003096; AAC16260.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09016.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09017.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK175603; BAD43366.1; -; mRNA.
DR   PIR; T01361; T01361.
DR   RefSeq; NP_001189678.1; NM_001202749.1.
DR   RefSeq; NP_181021.4; NM_129028.4. [O64583-1]
DR   AlphaFoldDB; O64583; -.
DR   SMR; O64583; -.
DR   STRING; 3702.AT2G34740.1; -.
DR   PaxDb; O64583; -.
DR   PRIDE; O64583; -.
DR   ProteomicsDB; 248710; -. [O64583-1]
DR   EnsemblPlants; AT2G34740.1; AT2G34740.1; AT2G34740. [O64583-1]
DR   GeneID; 818039; -.
DR   Gramene; AT2G34740.1; AT2G34740.1; AT2G34740. [O64583-1]
DR   KEGG; ath:AT2G34740; -.
DR   Araport; AT2G34740; -.
DR   TAIR; locus:2061579; AT2G34740.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_0_1_1; -.
DR   InParanoid; O64583; -.
DR   OMA; MSNDEVW; -.
DR   PRO; PR:O64583; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O64583; baseline and differential.
DR   Genevisible; O64583; 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; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..339
FT                   /note="Probable protein phosphatase 2C 28"
FT                   /id="PRO_0000367957"
FT   DOMAIN          87..334
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         124
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         292..339
FT                   /note="MSNDEVWDQIKKRGNAEEAAKMLIDKALARGSKDDISCVVVSFLQWID ->
FT                   STYECHGTLLIGAPKDRTKS (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_041311"
SQ   SEQUENCE   339 AA;  37881 MW;  3A7310A6CBF3AC47 CRC64;
     MKKTIKNSTH RPEDILVHAI KKRRSASGDV KNAVKLKEGE DYLRVEEEIP HDDNVVVIDD
     GCDHDHDVDD NDDDEEENGR YCRREFDHGY HLVKGQMGHG MEDFIVADTK TVKGHNLGLY
     AIFDGHSGSD VADYLQNHLF DNILSQPDFW RNPKKAIKRA YKSTDDYILQ NVVGPRGGST
     AVTAIVIDGK KIVVANVGDS RAILCRESDV VKQITVDHEP DKERDLVKSK GGFVSQKPGN
     VPRVDGQLAM TRAFGDGGLK EHISVIPNIE IAEIHDDTKF LILASDGLWK VMSNDEVWDQ
     IKKRGNAEEA AKMLIDKALA RGSKDDISCV VVSFLQWID
 
 
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