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Q9LME4 (P2C09_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable protein phosphatase 2C 9

Short name=AtPP2C09
EC=3.1.3.16
Alternative name(s):
Phytochrome-associated protein phosphatase 2C
Short name=PAPP2C
Gene names
Ordered Locus Names:At1g22280
ORF Names:T16E15.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of phytochrome signaling. May regulate phytochrome-interacting factor 3 (PIF3) through the dephosphorylation of phytochrome. Ref.8

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Subunit structure

Interacts with phytochromes (via N-terminus). Ref.6

Subcellular location

Nucleus. Note: Localizes in the nucleus upon illumination. Ref.8 Ref.11

Disruption phenotype

Abnormal hypocotyl elongation under continuous red light. Ref.6

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9LME4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9LME4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     186-199: DVPRVNGQLAVSRA → KELILSIECLMKIE
     200-281: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281Probable protein phosphatase 2C 9
PRO_0000367940

Regions

Domain32 – 273242PP2C-like

Sites

Metal binding701Manganese 1 By similarity
Metal binding701Manganese 2 By similarity
Metal binding711Manganese 1; via carbonyl oxygen By similarity
Metal binding2321Manganese 2 By similarity
Metal binding2711Manganese 2 By similarity

Natural variations

Alternative sequence186 – 19914DVPRV…AVSRA → KELILSIECLMKIE in isoform 2.
VSP_036759
Alternative sequence200 – 28182Missing in isoform 2.
VSP_036760

Experimental info

Sequence conflict111 – 1122DQ → E in AAM61437. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2EE90E4F8FB56768

FASTA28130,722
        10         20         30         40         50         60 
MGKFCCFTSA SEVVGGQSSS RSGKGRSDEG MIKYGFSLVK GKANHPMEDY HVANFINIQD 

        70         80         90        100        110        120 
HELGLFAIYD GHMGDSVPAY LQKRLFSNIL KEGEFWVDPR RSIAKAYEKT DQAILSNSSD 

       130        140        150        160        170        180 
LGRGGSTAVT AILINGRKLW IANVGDSRAV LSHGGAITQM STDHEPRTER SSIEDRGGFV 

       190        200        210        220        230        240 
SNLPGDVPRV NGQLAVSRAF GDKGLKTHLS SEPDIKEATV DSQTDVLLLA SDGIWKVMTN 

       250        260        270        280 
EEAMEIARRV KDPQKAAKEL TAEALRRESK DDISCVVVRF R 

« Hide

Isoform 2 [UniParc].

Checksum: 502ABB9152C7E9B2
Show »

FASTA19921,732

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[4]"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Identification of phytochrome-interacting protein candidates in Arabidopsis thaliana by co-immunoprecipitation coupled with MALDI-TOF MS."
Phee B.-K., Shin D.H., Cho J.-H., Kim S.-H., Kim J.-I., Lee Y.-H., Jeon J.-S., Bhoo S.H., Hahn T.-R.
Proteomics 6:3671-3680(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, INTERACTION WITH PHYTOCHROMES, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis."
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.
Mol. Cell. Proteomics 6:1711-1726(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Seedling.
[8]"A novel protein phosphatase indirectly regulates phytochrome-interacting factor 3 via phytochrome."
Phee B.-K., Kim J.-I., Shin D.H., Yoo J., Park K.-J., Han Y.-J., Kwon Y.-K., Cho M.H., Jeon J.-S., Bhoo S.H., Hahn T.-R.
Biochem. J. 415:247-255(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Genome-wide and expression analysis of protein phosphatase 2C in rice and Arabidopsis."
Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.
BMC Genomics 9:550-550(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[10]"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis."
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.
J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Root.
[11]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
[12]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC068562 Genomic DNA. Translation: AAF87263.1.
CP002684 Genomic DNA. Translation: AEE30220.1.
CP002684 Genomic DNA. Translation: AEE30221.1.
AY080735 mRNA. Translation: AAL86005.1.
AY133737 mRNA. Translation: AAM91671.1.
BX813947 mRNA. No translation available.
AY084874 mRNA. Translation: AAM61437.1.
PIRF86355.
RefSeqNP_564165.1. NM_102079.4. [Q9LME4-1]
NP_973883.1. NM_202154.2. [Q9LME4-2]
UniGeneAt.41611.

3D structure databases

ProteinModelPortalQ9LME4.
SMRQ9LME4. Positions 34-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid24074. 2 interactions.
IntActQ9LME4. 2 interactions.

Proteomic databases

PaxDbQ9LME4.
PRIDEQ9LME4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G22280.1; AT1G22280.1; AT1G22280. [Q9LME4-1]
GeneID838835.
KEGGath:AT1G22280.

Organism-specific databases

TAIRAT1G22280.

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000233896.
InParanoidQ9LME4.
PhylomeDBQ9LME4.

Enzyme and pathway databases

BioCycARA:AT1G22280-MONOMER.
ARA:GQT-527-MONOMER.

Gene expression databases

ArrayExpressQ9LME4.
GenevestigatorQ9LME4.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
ProtoNetSearch...

Entry information

Entry nameP2C09_ARATH
AccessionPrimary (citable) accession number: Q9LME4
Secondary accession number(s): Q3ED74, Q8LFF8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names