P2C15_ARATH
ID P2C15_ARATH Reviewed; 436 AA.
AC Q9M9C6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable protein phosphatase 2C 15;
DE Short=AtPP2C15;
DE EC=3.1.3.16;
GN OrderedLocusNames=At1g68410; ORFNames=T2E12.9;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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}.
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DR EMBL; AC015986; AAF26041.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34790.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34791.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57864.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57865.1; -; Genomic_DNA.
DR EMBL; AY050881; AAK92818.1; -; mRNA.
DR EMBL; AY091295; AAM14234.1; -; mRNA.
DR PIR; A96708; A96708.
DR RefSeq; NP_001031252.1; NM_001036175.2.
DR RefSeq; NP_001320343.1; NM_001334363.1.
DR RefSeq; NP_001320344.1; NM_001334364.1.
DR RefSeq; NP_177008.1; NM_105512.3.
DR AlphaFoldDB; Q9M9C6; -.
DR SMR; Q9M9C6; -.
DR BioGRID; 28391; 1.
DR STRING; 3702.AT1G68410.2; -.
DR PaxDb; Q9M9C6; -.
DR PRIDE; Q9M9C6; -.
DR ProteomicsDB; 248871; -.
DR EnsemblPlants; AT1G68410.1; AT1G68410.1; AT1G68410.
DR EnsemblPlants; AT1G68410.2; AT1G68410.2; AT1G68410.
DR EnsemblPlants; AT1G68410.3; AT1G68410.3; AT1G68410.
DR EnsemblPlants; AT1G68410.4; AT1G68410.4; AT1G68410.
DR GeneID; 843170; -.
DR Gramene; AT1G68410.1; AT1G68410.1; AT1G68410.
DR Gramene; AT1G68410.2; AT1G68410.2; AT1G68410.
DR Gramene; AT1G68410.3; AT1G68410.3; AT1G68410.
DR Gramene; AT1G68410.4; AT1G68410.4; AT1G68410.
DR KEGG; ath:AT1G68410; -.
DR Araport; AT1G68410; -.
DR TAIR; locus:2202339; AT1G68410.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_3_1_1; -.
DR InParanoid; Q9M9C6; -.
DR OMA; IFTCAIC; -.
DR OrthoDB; 567418at2759; -.
DR PhylomeDB; Q9M9C6; -.
DR PRO; PR:Q9M9C6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9C6; baseline and differential.
DR Genevisible; Q9M9C6; 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 Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..436
FT /note="Probable protein phosphatase 2C 15"
FT /id="PRO_0000367946"
FT DOMAIN 30..302
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 436 AA; 47041 MW; F24CE21FBC283252 CRC64;
MASREGKRRN HNHDDEKLVP LAALISRETK AAKMEKPIVR FGQAAQSRKG EDYVLIKTDS
LRVPSNSSTA FSVFAVFDGH NGKAAAVYTR ENLLNHVISA LPSGLSRDEW LHALPRALVS
GFVKTDKEFQ SRGETSGTTA TFVIVDGWTV TVACVGDSRC ILDTKGGSVS NLTVDHRLED
NTEERERVTA SGGEVGRLSI VGGVEIGPLR CWPGGLCLSR SIGDMDVGEF IVPVPFVKQV
KLSNLGGRLI IASDGIWDAL SSEVAAKTCR GLSAELAARQ VVKEALRRRG LKDDTTCIVV
DIIPPENFQE PPPSPPKKHN NFFKSLLFRK KSNSSNKLSK KLSTVGIVEE LFEEGSAMLA
ERLGSGDCSK ESTTGGGIFT CAICQLDLAP SEGISVHAGS IFSTSLKPWQ GPFLCTDCRD
KKDAMEGKRP SGVKVI
