P2C09_ARATH
ID P2C09_ARATH Reviewed; 281 AA.
AC Q9LME4; Q3ED74; Q8LFF8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable protein phosphatase 2C 9;
DE Short=AtPP2C09;
DE EC=3.1.3.16;
DE AltName: Full=Phytochrome-associated protein phosphatase 2C;
DE Short=PAPP2C;
GN OrderedLocusNames=At1g22280; ORFNames=T16E15.10;
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] (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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE, INTERACTION WITH PHYTOCHROMES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=16705748; DOI=10.1002/pmic.200500222;
RA Phee B.-K., Shin D.H., Cho J.-H., Kim S.-H., Kim J.-I., Lee Y.-H.,
RA Jeon J.-S., Bhoo S.H., Hahn T.-R.;
RT "Identification of phytochrome-interacting protein candidates in
RT Arabidopsis thaliana by co-immunoprecipitation coupled with MALDI-TOF MS.";
RL Proteomics 6:3671-3680(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18564962; DOI=10.1042/bj20071555;
RA Phee B.-K., Kim J.-I., Shin D.H., Yoo J., Park K.-J., Han Y.-J.,
RA Kwon Y.-K., Cho M.H., Jeon J.-S., Bhoo S.H., Hahn T.-R.;
RT "A novel protein phosphatase indirectly regulates phytochrome-interacting
RT factor 3 via phytochrome.";
RL Biochem. J. 415:247-255(2008).
RN [9]
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [11]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Involved in the regulation of phytochrome signaling. May
CC regulate phytochrome-interacting factor 3 (PIF3) through the
CC dephosphorylation of phytochrome. {ECO:0000269|PubMed:18564962}.
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 -!- SUBUNIT: Interacts with phytochromes (via N-terminus).
CC {ECO:0000269|PubMed:16705748}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18564962,
CC ECO:0000269|PubMed:19245862}. Note=Localizes in the nucleus upon
CC illumination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LME4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LME4-2; Sequence=VSP_036759, VSP_036760;
CC -!- DISRUPTION PHENOTYPE: Abnormal hypocotyl elongation under continuous
CC red light. {ECO:0000269|PubMed:16705748}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC068562; AAF87263.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30220.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30221.1; -; Genomic_DNA.
DR EMBL; AY080735; AAL86005.1; -; mRNA.
DR EMBL; AY133737; AAM91671.1; -; mRNA.
DR EMBL; BX813947; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY084874; AAM61437.1; -; mRNA.
DR PIR; F86355; F86355.
DR RefSeq; NP_564165.1; NM_102079.5. [Q9LME4-1]
DR RefSeq; NP_973883.1; NM_202154.2. [Q9LME4-2]
DR AlphaFoldDB; Q9LME4; -.
DR SMR; Q9LME4; -.
DR BioGRID; 24074; 3.
DR IntAct; Q9LME4; 2.
DR STRING; 3702.AT1G22280.3; -.
DR iPTMnet; Q9LME4; -.
DR SwissPalm; Q9LME4; -.
DR PaxDb; Q9LME4; -.
DR PRIDE; Q9LME4; -.
DR ProteomicsDB; 248868; -. [Q9LME4-1]
DR EnsemblPlants; AT1G22280.1; AT1G22280.1; AT1G22280. [Q9LME4-1]
DR EnsemblPlants; AT1G22280.2; AT1G22280.2; AT1G22280. [Q9LME4-2]
DR GeneID; 838835; -.
DR Gramene; AT1G22280.1; AT1G22280.1; AT1G22280. [Q9LME4-1]
DR Gramene; AT1G22280.2; AT1G22280.2; AT1G22280. [Q9LME4-2]
DR KEGG; ath:AT1G22280; -.
DR Araport; AT1G22280; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_0_1_1; -.
DR InParanoid; Q9LME4; -.
DR PhylomeDB; Q9LME4; -.
DR PRO; PR:Q9LME4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LME4; baseline and differential.
DR Genevisible; Q9LME4; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..281
FT /note="Probable protein phosphatase 2C 9"
FT /id="PRO_0000367940"
FT DOMAIN 33..280
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 186..199
FT /note="DVPRVNGQLAVSRA -> KELILSIECLMKIE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036759"
FT VAR_SEQ 200..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036760"
FT CONFLICT 111..112
FT /note="DQ -> E (in Ref. 5; AAM61437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 30722 MW; 2EE90E4F8FB56768 CRC64;
MGKFCCFTSA SEVVGGQSSS RSGKGRSDEG MIKYGFSLVK GKANHPMEDY HVANFINIQD
HELGLFAIYD GHMGDSVPAY LQKRLFSNIL KEGEFWVDPR RSIAKAYEKT DQAILSNSSD
LGRGGSTAVT AILINGRKLW IANVGDSRAV LSHGGAITQM STDHEPRTER SSIEDRGGFV
SNLPGDVPRV NGQLAVSRAF GDKGLKTHLS SEPDIKEATV DSQTDVLLLA SDGIWKVMTN
EEAMEIARRV KDPQKAAKEL TAEALRRESK DDISCVVVRF R
