P2C26_ARATH
ID P2C26_ARATH Reviewed; 298 AA.
AC O64730; A8MQM8; Q94K51;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable protein phosphatase 2C 26;
DE Short=AtPP2C26;
DE EC=3.1.3.16;
GN OrderedLocusNames=At2g30170; ORFNames=T27E13.9;
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=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] (ISOFORM 1).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O64730-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O64730-2; Sequence=VSP_036765;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC004165; AAC16955.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08354.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61563.1; -; Genomic_DNA.
DR EMBL; AF370298; AAK44113.1; -; mRNA.
DR EMBL; AY063046; AAL34220.1; -; mRNA.
DR PIR; T00581; T00581.
DR RefSeq; NP_001077980.1; NM_001084511.3. [O64730-2]
DR RefSeq; NP_565696.1; NM_128572.5. [O64730-1]
DR AlphaFoldDB; O64730; -.
DR SMR; O64730; -.
DR BioGRID; 2918; 1.
DR IntAct; O64730; 1.
DR MINT; O64730; -.
DR STRING; 3702.AT2G30170.1; -.
DR PaxDb; O64730; -.
DR PRIDE; O64730; -.
DR EnsemblPlants; AT2G30170.1; AT2G30170.1; AT2G30170. [O64730-1]
DR EnsemblPlants; AT2G30170.3; AT2G30170.3; AT2G30170. [O64730-2]
DR GeneID; 817569; -.
DR Gramene; AT2G30170.1; AT2G30170.1; AT2G30170. [O64730-1]
DR Gramene; AT2G30170.3; AT2G30170.3; AT2G30170. [O64730-2]
DR KEGG; ath:AT2G30170; -.
DR Araport; AT2G30170; -.
DR TAIR; locus:2060822; AT2G30170.
DR eggNOG; KOG1379; Eukaryota.
DR HOGENOM; CLU_029404_3_3_1; -.
DR InParanoid; O64730; -.
DR OMA; MQSIYWT; -.
DR PhylomeDB; O64730; -.
DR PRO; PR:O64730; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64730; baseline and differential.
DR Genevisible; O64730; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; 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:0071482; P:cellular response to light stimulus; IMP:TAIR.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PTHR12320; 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..298
FT /note="Probable protein phosphatase 2C 26"
FT /id="PRO_0000367955"
FT DOMAIN 48..295
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
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 VAR_SEQ 1..77
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036765"
SQ SEQUENCE 298 AA; 32285 MW; 52327F83126D89F5 CRC64;
MAIPVTRMMV PHAIPSLRLS HPNPSRVDFL CRCAPSEIQP LRPELSLSVG IHAIPHPDKV
EKGGEDAFFV SSYRGGVMAV ADGVSGWAEQ DVDPSLFSKE LMANASRLVD DQEVRYDPGF
LIDKAHTATT SRGSATIILA MLEEVGILKI GNVGDCGLKL LREGQIIFAT APQEHYFDCP
YQLSSEGSAQ TYLDASFSIV EVQKGDVIVM GSDGLFDNVF DHEIVSIVTK HTDVAESSRL
LAEVASSHSR DTEFESPYAL EARAKGFDVP LWKKVLGKKL TGGKLDDVTV IVAKVVSS
