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Q8RXV3 (P2C59_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Probable protein phosphatase 2C 59
PRO_0000367981

Regions

Domain60 – 272213PP2C-like

Sites

Metal binding691Manganese 1 By similarity
Metal binding691Manganese 2 By similarity
Metal binding701Manganese 1; via carbonyl oxygen By similarity
Metal binding2311Manganese 2 By similarity
Metal binding2701Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RXV3 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 5E3098E91F116BFD

FASTA31133,248
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. 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].
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.
PIRT05095.
RefSeqNP_194903.2. NM_119324.3.
UniGeneAt.31716.
At.51039.

3D structure databases

ProteinModelPortalQ8RXV3.
SMRQ8RXV3. Positions 34-277.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ8RXV3.
PRIDEQ8RXV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G31750.1; AT4G31750.1; AT4G31750.
GeneID829303.
KEGGath:AT4G31750.

Organism-specific databases

TAIRAT4G31750.

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000233896.
InParanoidQ8RXV3.
KOK17506.
OMANHDEAGT.
PhylomeDBQ8RXV3.

Enzyme and pathway databases

BioCycARA:AT4G31750-MONOMER.

Gene expression databases

GenevestigatorQ8RXV3.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
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.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP2C59_ARATH
AccessionPrimary (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 14, 2014
This is version 83 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