P2C27_ARATH
ID P2C27_ARATH Reviewed; 380 AA.
AC P93006;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable protein phosphatase 2C 27 {ECO:0000303|PubMed:19021904};
DE Short=AtPP2C27 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000255|PROSITE-ProRule:PRU01082};
DE AltName: Full=Probable protein phosphatase 2C G group 1 {ECO:0000303|PubMed:22627139};
DE Short=AtPP2CG1 {ECO:0000303|PubMed:22627139};
GN Name=PP2C27 {ECO:0000303|PubMed:19021904};
GN Synonyms=PP2CG1 {ECO:0000303|PubMed:22627139};
GN OrderedLocusNames=At2g33700 {ECO:0000312|Araport:AT2G33700};
GN ORFNames=T1B8.2 {ECO:0000312|EMBL:AAC69126.1};
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].
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.
RC STRAIN=cv. Columbia;
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).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALT STRESS; DROUGHT AND
RP ABSCISIC ACID, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22627139; DOI=10.1016/j.bbrc.2012.05.064;
RA Liu X., Zhu Y., Zhai H., Cai H., Ji W., Luo X., Li J., Bai X.;
RT "AtPP2CG1, a protein phosphatase 2C, positively regulates salt tolerance of
RT Arabidopsis in abscisic acid-dependent manner.";
RL Biochem. Biophys. Res. Commun. 422:710-715(2012).
CC -!- FUNCTION: Confers salt tolerance by triggering the expression of
CC stress-responsive genes. {ECO:0000269|PubMed:22627139}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01082};
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01082};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU01082};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22627139}. Cytoplasm
CC {ECO:0000269|PubMed:22627139}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flower, and
CC trichomes. {ECO:0000269|PubMed:22627139}.
CC -!- INDUCTION: Induced in shoots by drought in roots by abscisic acid
CC (ABA), and both in roots and shoot by salt stress.
CC {ECO:0000269|PubMed:22627139}.
CC -!- DISRUPTION PHENOTYPE: Decreased salt tolerance.
CC {ECO:0000269|PubMed:22627139}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; U78721; AAC69126.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08870.1; -; Genomic_DNA.
DR EMBL; AY070460; AAL49863.1; -; mRNA.
DR EMBL; AY091323; AAM14262.1; -; mRNA.
DR PIR; E84748; E84748.
DR RefSeq; NP_180926.1; NM_128928.3.
DR AlphaFoldDB; P93006; -.
DR SMR; P93006; -.
DR BioGRID; 3282; 1.
DR IntAct; P93006; 1.
DR STRING; 3702.AT2G33700.1; -.
DR iPTMnet; P93006; -.
DR PaxDb; P93006; -.
DR PRIDE; P93006; -.
DR ProteomicsDB; 248709; -.
DR EnsemblPlants; AT2G33700.1; AT2G33700.1; AT2G33700.
DR GeneID; 817935; -.
DR Gramene; AT2G33700.1; AT2G33700.1; AT2G33700.
DR KEGG; ath:AT2G33700; -.
DR Araport; AT2G33700; -.
DR TAIR; locus:2057635; AT2G33700.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_21_2_1; -.
DR InParanoid; P93006; -.
DR OMA; SMQRITT; -.
DR OrthoDB; 957254at2759; -.
DR PhylomeDB; P93006; -.
DR PRO; PR:P93006; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93006; baseline and differential.
DR Genevisible; P93006; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA: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 GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
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; 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 Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..380
FT /note="Probable protein phosphatase 2C 27"
FT /id="PRO_0000367956"
FT DOMAIN 84..344
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 41757 MW; B869BEFAE839C550 CRC64;
MSMDFSPLLT VLEGDFNKDN TSSATEIDTL ENLDDTRQIS KGKPPRHLTS SATRLQLAAN
ADVDVCNLVM KSLDDKSEFL PVYRSGSCAE QGAKQFMEDE HICIDDLVNH LGAAIQCSSL
GAFYGVFDGH GGTDAAHFVR KNILRFIVED SSFPLCVKKA IKSAFLKADY EFADDSSLDI
SSGTTALTAF IFGRRLIIAN AGDCRAVLGR RGRAIELSKD HKPNCTAEKV RIEKLGGVVY
DGYLNGQLSV ARAIGDWHMK GPKGSACPLS PEPELQETDL SEDDEFLIMG CDGLWDVMSS
QCAVTIARKE LMIHNDPERC SRELVREALK RNTCDNLTVI VVCFSPDPPQ RIEIRMQSRV
RRSISAEGLN LLKGVLDGYP
