Q9SLA1 (P2C22_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable protein phosphatase 2C 22
Short name=AtPP2C22
EC=3.1.3.16

Gene names

Ordered Locus Names:	At2g25620
ORF Names:	F3N11.7

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	392 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Sequence similarities	Belongs to the PP2C family. Contains 1 PP2C-like domain.

Ontologies

Keywords
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein dephosphorylation Inferred from electronic annotation. Source: InterPro regulation of defense response to virus Inferred from mutant phenotype PubMed 20508138. Source: TAIR
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 392	392	Probable protein phosphatase 2C 22		PRO_0000367952
Regions
	Domain	88 – 349	262	PP2C-like
Sites
	Metal binding	133	1	Manganese 1 By similarity
	Metal binding	133	1	Manganese 2 By similarity
	Metal binding	134	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	304	1	Manganese 2 By similarity
	Metal binding	347	1	Manganese 2 By similarity
Amino acid modifications
	Modified residue	376	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9SLA1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: AC09DC922197BE53	FASTA	392	42,674
	10 20 30 40 50 60 MEETRGISDP ENGSSSYGGK PPNPLSFSSS SAAAAVYRQT FDGERSLAPC NKRSLVRHSS 70 80 90 100 110 120 LVKTMVSDIS VENEFTIEKN KSEFVPATRS GAWSDIGSRS SMEDAYLCVD NFMDSFGLLN 130 140 150 160 170 180 SEAGPSAFYG VFDGHGGKHA AEFACHHIPR YIVEDQEFPS EINKVLSSAF LQTDTAFLEA 190 200 210 220 230 240 CSLDGSLASG TTALAAILFG RSLVVANAGD CRAVLSRQGK AIEMSRDHKP MSSKERRRIE 250 260 270 280 290 300 ASGGHVFDGY LNGQLNVARA LGDFHMEGMK KKKDGSDCGP LIAEPELMTT KLTEEDEFLI 310 320 330 340 350 360 IGCDGVWDVF MSQNAVDFAR RRLQEHNDPV MCSKELVEEA LKRKSADNVT AVVVCLQPQP 370 380 390 PPNLVAPRLR VHRSFSAEGL KDLQSYLDGL GN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [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]. Strain: cv. Columbia.
[4]	"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.
[5]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC006053 Genomic DNA. Translation: AAD31375.1. CP002685 Genomic DNA. Translation: AEC07725.1. AF326901 mRNA. Translation: AAG41483.1. AF339719 mRNA. Translation: AAK00401.1. AF436827 mRNA. Translation: AAL32009.1. AY039595 mRNA. Translation: AAK62650.1. AY057740 mRNA. Translation: AAL15370.1. BT002487 mRNA. Translation: AAO00847.1.
IPI	IPI00547598.
PIR	F84650.
RefSeq	NP_180133.1. NM_128120.1.
UniGene	At.24605. At.70222. At.74045.
3D structure databases
HSSP	HSSP built from PDB template 1A6Q based on UniProtKB P35813.
ProteinModelPortal	Q9SLA1.
SMR	Q9SLA1. Positions 90-354.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G25620.1-P.
Proteomic databases
PaxDb	Q9SLA1.
PRIDE	Q9SLA1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G25620.1; AT2G25620.1; AT2G25620.
GeneID	817102.
KEGG	ath:AT2G25620.
Organism-specific databases
GeneFarm	3542. 320.
TAIR	At2g25620.
Phylogenomic databases
eggNOG	COG0631.
HOGENOM	HOG000233896.
InParanoid	Q9SLA1.
KO	K14803.
OMA	HAADFVC.
PhylomeDB	Q9SLA1.
ProtClustDB	PLN03145.
Gene expression databases
Genevestigator	Q9SLA1.
Family and domain databases
Gene3D	3.60.40.10. 1 hit.
InterPro	IPR001932. PP2C-like. IPR000222. PP2C_Mn2_Asp60_BS. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P2C22_ARATH

Accession

Primary (citable) accession number: Q9SLA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program