Q8RXV3 (P2C59_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable protein phosphatase 2C 59
Short name=AtPP2C59
EC=3.1.3.16

Alternative name(s):
HopW1-1-interacting protein 2
Protein phosphatase 2C WIN2
Short name=PP2C WIN2

Gene names

Name:	WIN2
Ordered Locus Names:	At4g31750
ORF Names:	F28M20.60

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

General annotation (Comments)

Function	Protein phosphatase that modulates defense response to pathogenic bacteria, conferring resistance and promoting salicylic acid (SA) accumulation. Ref.1
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Enzyme regulation	Inhibited by sodium fluoride (NaF). Ref.1
Subunit structure	Interacts with the Pseudomonas syringae pv. maculicola effector HopW1-1 (via C-terminus). Ref.1
Sequence similarities	Belongs to the PP2C family. Contains 1 PP2C-like domain.
Sequence caution	The sequence CAA19748.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79893.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Plant defense
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from mutant phenotype Ref.1. Source: TAIR interspecies interaction between organisms Inferred from physical interaction Ref.1. Source: UniProtKB protein dephosphorylation Inferred from direct assay Ref.1. Source: TAIR
Cellular_component	plasma membrane Inferred from direct assay PubMed 17317660. Source: TAIR
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 311	311	Probable protein phosphatase 2C 59		PRO_0000367981
Regions
	Domain	60 – 272	213	PP2C-like
Sites
	Metal binding	69	1	Manganese 1 By similarity
	Metal binding	69	1	Manganese 2 By similarity
	Metal binding	70	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	231	1	Manganese 2 By similarity
	Metal binding	270	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8RXV3 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 5E3098E91F116BFD	FASTA	311	33,248
	10 20 30 40 50 60 MGYLNSVLSS SSQVHSDDGP VSGGGLSQNG KFSYGYASSP GKRSSMEDFY ETRIDGVEGE 70 80 90 100 110 120 IVGLFGVFDG HGGARAAEYV KQNLFSNLIR HPKFISDTTA AIADAYNQTD SEFLKSENSQ 130 140 150 160 170 180 NRDAGSTAST AILVGDRLLV ANVGDSRAVI CRGGNAIAVS RDHKPDQSDE RQRIEDAGGF 190 200 210 220 230 240 VMWAGTWRVG GVLAVSRAFG DRLLKQYVVA DPEIQEEKVD SSLEFLILAS DGLWDVVSNE 250 260 270 280 290 300 EAVGMIKAIE DPEEGAKRLM MEAYQRGSAD NITCVVVRFF SDQAGGIGSS STNIPIDHGI 310 VPDRISGDSS T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis proteins important for modulating defense responses to Pseudomonas syringae that secrete HopW1-1." Lee M.W., Jelenska J., Greenberg J.T. Plant J. 54:452-465(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, INTERACTION WITH PSEUDOMONAS SYRINGAE MACULICOLA HOPW1-1. Strain: cv. Wassilewskija.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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.
[5]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EU214909 mRNA. Translation: ABW84225.1. AL031004 Genomic DNA. Translation: CAA19748.1. Sequence problems. AL161579 Genomic DNA. Translation: CAB79893.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE85953.1. AY080658 mRNA. Translation: AAL86334.1. AY133761 mRNA. Translation: AAM91695.1.
IPI	IPI00537408.
PIR	T05095.
RefSeq	NP_194903.2. NM_119324.3.
UniGene	At.31716. At.51039.
3D structure databases
HSSP	HSSP built from PDB template 1A6Q based on UniProtKB P35813.
ProteinModelPortal	Q8RXV3.
SMR	Q8RXV3. Positions 34-277.
ModBase	Search...
Proteomic databases
PaxDb	Q8RXV3.
PRIDE	Q8RXV3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G31750.1; AT4G31750.1; AT4G31750.
GeneID	829303.
KEGG	ath:AT4G31750.
Organism-specific databases
TAIR	At4g31750.
Phylogenomic databases
eggNOG	COG0631.
HOGENOM	HOG000233896.
InParanoid	Q8RXV3.
OMA	NHDEAGT.
PhylomeDB	Q8RXV3.
ProtClustDB	CLSN2680208.
Gene expression databases
Genevestigator	Q8RXV3.
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

P2C59_ARATH

Accession

Primary (citable) accession number: Q8RXV3
Secondary accession number(s): O81773

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program