P2C43_ARATH
ID P2C43_ARATH Reviewed; 422 AA.
AC Q9LUU7; Q56ZV0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable protein phosphatase 2C 43;
DE Short=AtPP2C43;
DE EC=3.1.3.16;
GN OrderedLocusNames=At3g17250; ORFNames=MGD8.13, MGD8.8;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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;
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 (JUL-2006) 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 -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AB022216; BAB02728.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75928.1; -; Genomic_DNA.
DR EMBL; AK220861; BAD94223.1; -; mRNA.
DR EMBL; AK228860; BAF00754.1; -; mRNA.
DR RefSeq; NP_188351.2; NM_112603.3.
DR AlphaFoldDB; Q9LUU7; -.
DR SMR; Q9LUU7; -.
DR BioGRID; 6319; 1.
DR IntAct; Q9LUU7; 1.
DR MINT; Q9LUU7; -.
DR STRING; 3702.AT3G17250.1; -.
DR PaxDb; Q9LUU7; -.
DR PRIDE; Q9LUU7; -.
DR ProteomicsDB; 248713; -.
DR EnsemblPlants; AT3G17250.1; AT3G17250.1; AT3G17250.
DR GeneID; 820986; -.
DR Gramene; AT3G17250.1; AT3G17250.1; AT3G17250.
DR KEGG; ath:AT3G17250; -.
DR Araport; AT3G17250; -.
DR TAIR; locus:2089035; AT3G17250.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_21_0_1; -.
DR InParanoid; Q9LUU7; -.
DR OMA; IAEIRIH; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9LUU7; -.
DR PRO; PR:Q9LUU7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUU7; baseline and differential.
DR Genevisible; Q9LUU7; AT.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..422
FT /note="Probable protein phosphatase 2C 43"
FT /id="PRO_0000367967"
FT DOMAIN 117..393
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 303
FT /note="W -> S (in Ref. 3; BAD94223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 47599 MW; 63B7B3E7DD69FCE4 CRC64;
MRTSKASVTQ TWLLYTQLCL WKDLIIRYVR QIIRRAKSML FSQNMVADSA EISVIDVKSH
LSVAKDPSNF QIAEIRIHDS ICIDIPSSEE TPLLESIKSC SATTIEEHVT EFVPNISSGS
YADKGDYREY MEDEHICIDD LSDHLGSSFY RFPVPMAFYG VFDGHGGSDA SQYIKENAMS
LFFEDAVFRQ SPSVVDSLFL KELETSHREA YRLADLAMED ERIVSSSCGT TALTALVIGR
HLMVANVGDC RAVLCRKGKA VDMSFDHKST FEPERRRVED LGGYFEGEYL YGDLAVTRAL
GDWSIKRFSP LGESLSPLIS DPDIQQMILT EEDEFLIMGC DGVWDVMTSQ YAVTFVRQGL
RRHGDPRRCA MELGREALRL DSSDNVTVVV ICFSSSPAPQ RRRIRFCVSD EARARLQTML
EG
