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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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