Q9LME4 (P2C09_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Subunit structure	Interacts with phytochromes (via N-terminus). Ref.7
Subcellular location	Nucleus. Note: Localizes in the nucleus upon illumination. Ref.8
Disruption phenotype	Abnormal hypocotyl elongation under continuous red light. Ref.7
Sequence similarities	Belongs to the PP2C family. Contains 1 PP2C-like domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 281	281	Probable protein phosphatase 2C 9		PRO_0000367940
Regions
	Domain	32 – 273	242	PP2C-like
Sites
	Metal binding	70	1	Manganese 1 By similarity
	Metal binding	70	1	Manganese 2 By similarity
	Metal binding	71	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	232	1	Manganese 2 By similarity
	Metal binding	271	1	Manganese 2 By similarity
Amino acid modifications
	Modified residue	118	1	Phosphoserine Ref.6 Ref.10
	Modified residue	119	1	Phosphoserine Ref.6
Natural variations
	Alternative sequence	186 – 199	14	DVPRV…AVSRA → KELILSIECLMKIE in isoform 2.		VSP_036759
	Alternative sequence	200 – 281	82	Missing in isoform 2.		VSP_036760
Experimental info
	Sequence conflict	111 – 112	2	DQ → E in AAM61437. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2EE90E4F8FB56768	FASTA	281	30,722
	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
	Isoform 2 [UniParc]. Checksum: 502ABB9152C7E9B2	FASTA	199	21,732
	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 SNLPGKELIL SIECLMKIE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-119, MASS SPECTROMETRY. Strain: cv. La-0.
[7]	"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.
[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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, SUBCELLULAR LOCATION, MASS SPECTROMETRY. Strain: cv. Columbia.
+	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.
IPI	IPI00521156. IPI00523000.
PIR	F86355.
RefSeq	NP_564165.1. NM_102079.4. NP_973883.1. NM_202154.2.
UniGene	At.41611.
3D structure databases
HSSP	HSSP built from PDB template 1A6Q based on UniProtKB P35813.
ProteinModelPortal	Q9LME4.
SMR	Q9LME4. Positions 65-281.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9LME4. 2 interactions.
Proteomic databases
PaxDb	Q9LME4.
PRIDE	Q9LME4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G22280.1; AT1G22280.1; AT1G22280.
GeneID	838835.
KEGG	ath:AT1G22280.
Organism-specific databases
TAIR	At1g22280.
Phylogenomic databases
eggNOG	COG0631.
HOGENOM	HOG000233896.
InParanoid	Q9LME4.
PhylomeDB	Q9LME4.
ProtClustDB	CLSN2917036.
Gene expression databases
ArrayExpress	Q9LME4.
Genevestigator	Q9LME4.
Family and domain databases
Gene3D	3.60.40.10. 1 hit.
InterPro	IPR001932. PP2C-like. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
PROSITE	PS01032. PP2C. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P2C09_ARATH

Accession

Primary (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:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program