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P49598 (P2C37_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 2C 37

Short name=AtPP2C37
EC=3.1.3.16
Alternative name(s):
Protein ABA-HYPERSENSITIVE GERMINATION 3
Protein phosphatase 2C A
Short name=PP2CA
Gene names
Name:PP2CA
Synonyms:AHG3
Ordered Locus Names:At3g11410
ORF Names:F24K9.8
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major negative regulator of abscisic acid (ABA) responses during seed germination and cold acclimation. Confers insensitivity to ABA. Modulates negatively the AKT2/3 activity, which mediates K+ transport and membrane polarization during stress situations, probably by dephosphorylation. Prevent stomata closure by inactivating the S-type anion efflux channel SLAC1 and its activator SRK2E. Ref.5 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.16

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

Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner. Ref.17

Subunit structure

Interacts with AKT2/AKT3. Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL9 and PYL12, and with free PYL2, PYL3 and PYL4. Binds to and inactivates SLAC1 and SRK2E. The inactivation of SRK2E does not require phosphatase activity. Interacts with CBL1, CBL2, CBL3, CBL5, and CBL7, but not CBL4, CBL6, and CBL9. Ref.6 Ref.8 Ref.16 Ref.17 Ref.18

Tissue specificity

Mostly expressed in seeds and leaves, and, to a lower extent, in roots, stems, and flowers, particularly in siliques. Essentially found in the phloem. Ref.7 Ref.8 Ref.11 Ref.13

Induction

Repressed by MYB44. Induced by cold stress, drought, high salt, and ABA. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17

Domain

The 'lock' site stabilizes the complex made of PP2C, ABA and PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch' loops in closed positions By similarity.

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Ontologies

Keywords
   Biological processAbscisic acid signaling pathway
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processabscisic acid-activated signaling pathway

Inferred from mutant phenotype Ref.11. Source: TAIR

negative regulation of abscisic acid-activated signaling pathway

Inferred from mutant phenotype Ref.11Ref.12. Source: TAIR

negative regulation of anion channel activity

Inferred from direct assay Ref.16. Source: UniProtKB

protein dephosphorylation

Inferred from electronic annotation. Source: InterPro

regulation of stomatal movement

Inferred from mutant phenotype Ref.12. Source: TAIR

response to abscisic acid

Inferred from mutant phenotype PubMed 19458118. Source: TAIR

response to cold

Inferred from expression pattern Ref.10. Source: TAIR

response to water deprivation

Inferred from expression pattern Ref.12PubMed 18552355. Source: TAIR

   Cellular_componentcytosol

Inferred from direct assay PubMed 22198272. Source: TAIR

nucleus

Inferred from direct assay PubMed 22198272. Source: TAIR

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 19458118. Source: TAIR

protein kinase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from mutant phenotype Ref.11. Source: TAIR

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AKT2Q388985EBI-1764934,EBI-1552774

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Protein phosphatase 2C 37
PRO_0000057769

Regions

Domain103 – 382280PP2C-like

Sites

Metal binding1421Manganese 1 By similarity
Metal binding1421Manganese 2 By similarity
Metal binding1431Manganese 1; via carbonyl oxygen By similarity
Metal binding3271Manganese 2 By similarity
Metal binding3801Manganese 2 By similarity
Site2801Lock By similarity

Experimental info

Mutagenesis1391G → D: Loss of phosphatase activity. Loss of kinase activity but intact binding and repression of SRK2E; when associated with D-145. Ref.5 Ref.8 Ref.16
Mutagenesis1451G → D: Insensitive to ABA and loss of phosphatase activity. Loss of kinase activity but intact binding and repression of SRK2E; when associated with D-139. Ref.5 Ref.11 Ref.16
Mutagenesis2871G → E in ahg3-1; hypersensitivity to ABA during seed germination, and loss of phosphatase activity. Ref.11

Secondary structure

........................................... 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49598 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 83B82E32FEC71D4D

FASTA39943,350
        10         20         30         40         50         60 
MAGICCGVVG ETEPAAPVDS TSRASLRRRL DLLPSIKIVA DSAVAPPLEN CRKRQKRETV 

        70         80         90        100        110        120 
VLSTLPGNLD LDSNVRSENK KARSAVTNSN SVTEAESFFS DVPKIGTTSV CGRRRDMEDA 

       130        140        150        160        170        180 
VSIHPSFLQR NSENHHFYGV FDGHGCSHVA EKCRERLHDI VKKEVEVMAS DEWTETMVKS 

       190        200        210        220        230        240 
FQKMDKEVSQ RECNLVVNGA TRSMKNSCRC ELQSPQCDAV GSTAVVSVVT PEKIIVSNCG 

       250        260        270        280        290        300 
DSRAVLCRNG VAIPLSVDHK PDRPDELIRI QQAGGRVIYW DGARVLGVLA MSRAIGDNYL 

       310        320        330        340        350        360 
KPYVIPDPEV TVTDRTDEDE CLILASDGLW DVVPNETACG VARMCLRGAG AGDDSDAAHN 

       370        380        390 
ACSDAALLLT KLALARQSSD NVSVVVVDLR KRRNNQASS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of cDNAs from Arabidopsis thaliana that encode putative protein phosphatase 2C and a human Dr1-like protein by transformation of a fission yeast mutant."
Kuromori T., Yamamoto M.
Nucleic Acids Res. 22:5296-5301(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [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]"Mutational analysis of protein phosphatase 2C involved in abscisic acid signal transduction in higher plants."
Sheen J.
Proc. Natl. Acad. Sci. U.S.A. 95:975-980(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-139 AND GLY-145.
[6]"The AKT3 potassium channel protein interacts with the AtPP2CA protein phosphatase 2C."
Vranova E., Taehtiharju S., Sriprang R., Willekens H., Heino P., Palva E.T., Inze D., Van Camp W.
J. Exp. Bot. 52:181-182(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AKT2/AKT3.
[7]"Antisense inhibition of protein phosphatase 2C accelerates cold acclimation in Arabidopsis thaliana."
Taehtiharju S., Palva T.
Plant J. 26:461-470(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[8]"Physical and functional interaction of the Arabidopsis K(+) channel AKT2 and phosphatase AtPP2CA."
Cherel I., Michard E., Platet N., Mouline K., Alcon C., Sentenac H., Thibaud J.-B.
Plant Cell 14:1133-1146(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-139, TISSUE SPECIFICITY, INDUCTION BY ABA, INTERACTION WITH AKT2/AKT3.
[9]"Plant PP2C phosphatases: emerging functions in stress signaling."
Schweighofer A., Hirt H., Meskiene I.
Trends Plant Sci. 9:236-243(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[10]"The Arabidopsis cold-responsive transcriptome and its regulation by ICE1."
Lee B.-H., Henderson D.A., Zhu J.-K.
Plant Cell 17:3155-3175(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY COLD STRESS.
[11]"ABA-hypersensitive germination3 encodes a protein phosphatase 2C (AtPP2CA) that strongly regulates abscisic acid signaling during germination among Arabidopsis protein phosphatase 2Cs."
Yoshida T., Nishimura N., Kitahata N., Kuromori T., Ito T., Asami T., Shinozaki K., Hirayama T.
Plant Physiol. 140:115-126(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY ABA, MUTAGENESIS OF GLY-145 AND GLY-287, TISSUE SPECIFICITY.
[12]"The protein phosphatase AtPP2CA negatively regulates abscisic acid signal transduction in Arabidopsis, and effects of abh1 on AtPP2CA mRNA."
Kuhn J.M., Boisson-Dernier A., Dizon M.B., Maktabi M.H., Schroeder J.I.
Plant Physiol. 140:127-139(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[13]"ABA-Hypersensitive Germination1 encodes a protein phosphatase 2C, an essential component of abscisic acid signaling in Arabidopsis seed."
Nishimura N., Yoshida T., Kitahata N., Asami T., Shinozaki K., Hirayama T.
Plant J. 50:935-949(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY ABA, TISSUE SPECIFICITY.
[14]"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.
[15]"Overexpression of AtMYB44 enhances stomatal closure to confer abiotic stress tolerance in transgenic Arabidopsis."
Jung C., Seo J.S., Han S.W., Koo Y.J., Kim C.H., Song S.I., Nahm B.H., Choi Y.D., Cheong J.-J.
Plant Physiol. 146:623-635(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY MYB44 AND SALT.
[16]"A protein kinase-phosphatase pair interacts with an ion channel to regulate ABA signaling in plant guard cells."
Lee S.C., Lan W., Buchanan B.B., Luan S.
Proc. Natl. Acad. Sci. U.S.A. 106:21419-21424(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SLAC1 AND SRK2E/OST1, MUTAGENESIS OF GLY-139 AND GLY-145.
[17]"Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins."
Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y., Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D., Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P., Zhu J.-K. expand/collapse author list , Schroeder J.I., Volkman B.F., Cutler S.R.
Science 324:1068-1071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PYR1; PYL1; PYL2; PYL3; PYL4; PYL9 AND PYL12, ENZYME REGULATION.
[18]"Mechanistic analysis of AKT1 regulation by the CBL-CIPK-PP2CA interactions."
Lan W.Z., Lee S.C., Che Y.F., Jiang Y.Q., Luan S.
Mol. Plant 4:527-536(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL1; CBL2; CBL3; CBL4; CBL5; CBL6; CBL7 AND CBL9.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38109 mRNA. Translation: BAA07287.1.
AC008153 Genomic DNA. Translation: AAG51448.1.
CP002686 Genomic DNA. Translation: AEE75044.1.
AY074368 mRNA. Translation: AAL67064.1.
AY091391 mRNA. Translation: AAM14330.1.
PIRS55457.
RefSeqNP_187748.1. NM_111974.3.
UniGeneAt.20739.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4N0GX-ray2.38A/B72-399[»]
ProteinModelPortalP49598.
SMRP49598. Positions 98-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid5648. 15 interactions.
DIPDIP-40197N.
IntActP49598. 9 interactions.
MINTMINT-8390822.
STRING3702.AT3G11410.1-P.

Proteomic databases

PRIDEP49598.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G11410.1; AT3G11410.1; AT3G11410.
GeneID820314.
KEGGath:AT3G11410.

Organism-specific databases

TAIRAT3G11410.

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000233896.
InParanoidP49598.
KOK14497.
OMAVMASDEW.
PhylomeDBP49598.
ProtClustDBCLSN2914762.

Enzyme and pathway databases

BioCycARA:AT3G11410-MONOMER.

Gene expression databases

GenevestigatorP49598.

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 nameP2C37_ARATH
AccessionPrimary (citable) accession number: P49598
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 114 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names