P2C76_ARATH
ID P2C76_ARATH Reviewed; 420 AA.
AC Q94AT1; Q8VZD9; Q9FGM3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable protein phosphatase 2C 76;
DE Short=AtPP2C76;
DE EC=3.1.3.16;
GN OrderedLocusNames=At5g53140; ORFNames=MFH8.8;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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=BAB08417.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025622; BAB08417.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96312.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68199.1; -; Genomic_DNA.
DR EMBL; AY045819; AAK76493.1; -; mRNA.
DR EMBL; AY065026; AAL57666.1; -; mRNA.
DR EMBL; AY091360; AAM14299.1; -; mRNA.
DR EMBL; AY133656; AAM91486.1; -; mRNA.
DR RefSeq; NP_001329972.1; NM_001345034.1.
DR RefSeq; NP_568786.1; NM_124693.4.
DR AlphaFoldDB; Q94AT1; -.
DR SMR; Q94AT1; -.
DR BioGRID; 20640; 4.
DR IntAct; Q94AT1; 1.
DR MINT; Q94AT1; -.
DR STRING; 3702.AT5G53140.1; -.
DR iPTMnet; Q94AT1; -.
DR MetOSite; Q94AT1; -.
DR PaxDb; Q94AT1; -.
DR PRIDE; Q94AT1; -.
DR ProteomicsDB; 250974; -.
DR EnsemblPlants; AT5G53140.1; AT5G53140.1; AT5G53140.
DR EnsemblPlants; AT5G53140.2; AT5G53140.2; AT5G53140.
DR GeneID; 835395; -.
DR Gramene; AT5G53140.1; AT5G53140.1; AT5G53140.
DR Gramene; AT5G53140.2; AT5G53140.2; AT5G53140.
DR KEGG; ath:AT5G53140; -.
DR Araport; AT5G53140; -.
DR TAIR; locus:2163781; AT5G53140.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_0_6_1; -.
DR InParanoid; Q94AT1; -.
DR OMA; IFDGHSN; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q94AT1; -.
DR PRO; PR:Q94AT1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94AT1; baseline and differential.
DR Genevisible; Q94AT1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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; IPR000222; PP2C_BS.
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; 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..420
FT /note="Probable protein phosphatase 2C 76"
FT /id="PRO_0000367996"
FT DOMAIN 101..347
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 353..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 267
FT /note="F -> L (in Ref. 3; AAM91486/AAL57666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 45786 MW; C312D84D35159052 CRC64;
MVCSSFIRSF IVQAGCRIGV LAQGRHQFIH IKKTLSVGFG FRTSVIGFRT TSGIGFRTSA
KMMVDTSAGE KRISLVDMPP EKVDDGGYIG GGWKNDDGSL SCGYCSFRGK RSTMEDFYDI
KASTIEGQAV CMFGIFDGHG GSRAAEYLKE HLFNNLMKHP QFLTDTKLAL NETYKQTDVA
FLESEKDTYR DDGSTASAAV LVGNHLYVAN VGDSRTIVSK AGKAIALSDD HKPNRSDERK
RIESAGGVIM WAGTWRVGGV LAMSRAFGNR MLKQFVVAEP EIQDLEIDHE AELLVLASDG
LWDVVPNEDA VALAQSEEEP EAAARKLTDT AFSRGSADNI TCIVVKFRHD KTESPKIETN
AMAESEPELN PTTELEPESN PSTALETESI PKAELESEPD AIPDPKPETE PETKGEKAGE
