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P49598

- P2C37_ARATH

UniProt

P49598 - P2C37_ARATH

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Protein

Protein phosphatase 2C 37

Gene

PP2CA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Binds 2 magnesium or manganese ions per subunit.By similarity

Enzyme regulationi

Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi142 – 1421Manganese 1By similarity
Metal bindingi142 – 1421Manganese 2By similarity
Metal bindingi143 – 1431Manganese 1; via carbonyl oxygenBy similarity
Sitei280 – 2801LockBy similarity
Metal bindingi327 – 3271Manganese 2By similarity
Metal bindingi380 – 3801Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: TAIR
  3. protein kinase binding Source: UniProtKB
  4. protein serine/threonine phosphatase activity Source: TAIR

GO - Biological processi

  1. abscisic acid-activated signaling pathway Source: TAIR
  2. negative regulation of abscisic acid-activated signaling pathway Source: TAIR
  3. negative regulation of anion channel activity Source: UniProtKB
  4. protein dephosphorylation Source: InterPro
  5. regulation of stomatal movement Source: TAIR
  6. response to abscisic acid Source: TAIR
  7. response to cold Source: TAIR
  8. response to water deprivation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Abscisic acid signaling pathway

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G11410-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 2C 37 (EC:3.1.3.16)
Short name:
AtPP2C37
Alternative name(s):
Protein ABA-HYPERSENSITIVE GERMINATION 3
Protein phosphatase 2C A
Short name:
PP2CA
Gene namesi
Name:PP2CA
Synonyms:AHG3
Ordered Locus Names:At3g11410
ORF Names:F24K9.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G11410.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. nucleus Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi139 – 1391G → D: Loss of phosphatase activity. Loss of kinase activity but intact binding and repression of SRK2E; when associated with D-145. 3 Publications
Mutagenesisi145 – 1451G → 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. 3 Publications
Mutagenesisi287 – 2871G → E in ahg3-1; hypersensitivity to ABA during seed germination, and loss of phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Protein phosphatase 2C 37PRO_0000057769Add
BLAST

Proteomic databases

PRIDEiP49598.

Expressioni

Tissue specificityi

Mostly expressed in seeds and leaves, and, to a lower extent, in roots, stems, and flowers, particularly in siliques. Essentially found in the phloem.4 Publications

Inductioni

Repressed by MYB44. Induced by cold stress, drought, high salt, and ABA.7 Publications

Gene expression databases

GenevestigatoriP49598.

Interactioni

Subunit structurei

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 CBL9.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT2Q388985EBI-1764934,EBI-1552774

Protein-protein interaction databases

BioGridi5648. 30 interactions.
DIPiDIP-40197N.
IntActiP49598. 9 interactions.
MINTiMINT-8390822.
STRINGi3702.AT3G11410.1-P.

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi105 – 1106Combined sources
Beta strandi119 – 13214Combined sources
Beta strandi134 – 14714Combined sources
Helixi148 – 16518Combined sources
Helixi173 – 18917Combined sources
Turni209 – 2124Combined sources
Helixi216 – 2194Combined sources
Beta strandi224 – 2296Combined sources
Beta strandi231 – 24111Combined sources
Beta strandi243 – 2486Combined sources
Beta strandi251 – 2566Combined sources
Helixi264 – 2729Combined sources
Beta strandi277 – 2859Combined sources
Turni286 – 2883Combined sources
Beta strandi289 – 2935Combined sources
Helixi298 – 3003Combined sources
Turni301 – 3033Combined sources
Beta strandi309 – 3146Combined sources
Beta strandi319 – 3257Combined sources
Helixi327 – 3304Combined sources
Helixi335 – 34511Combined sources
Helixi361 – 37515Combined sources
Beta strandi382 – 3887Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4N0GX-ray2.38A/B72-399[»]
ProteinModelPortaliP49598.
SMRiP49598. Positions 98-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 382280PP2C-likeAdd
BLAST

Domaini

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 similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PP2C-like domain.Curated

Phylogenomic databases

eggNOGiCOG0631.
HOGENOMiHOG000233896.
InParanoidiP49598.
KOiK14497.
OMAiSCRCELQ.
PhylomeDBiP49598.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PP2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49598-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGICCGVVG ETEPAAPVDS TSRASLRRRL DLLPSIKIVA DSAVAPPLEN
60 70 80 90 100
CRKRQKRETV VLSTLPGNLD LDSNVRSENK KARSAVTNSN SVTEAESFFS
110 120 130 140 150
DVPKIGTTSV CGRRRDMEDA VSIHPSFLQR NSENHHFYGV FDGHGCSHVA
160 170 180 190 200
EKCRERLHDI VKKEVEVMAS DEWTETMVKS FQKMDKEVSQ RECNLVVNGA
210 220 230 240 250
TRSMKNSCRC ELQSPQCDAV GSTAVVSVVT PEKIIVSNCG DSRAVLCRNG
260 270 280 290 300
VAIPLSVDHK PDRPDELIRI QQAGGRVIYW DGARVLGVLA MSRAIGDNYL
310 320 330 340 350
KPYVIPDPEV TVTDRTDEDE CLILASDGLW DVVPNETACG VARMCLRGAG
360 370 380 390
AGDDSDAAHN ACSDAALLLT KLALARQSSD NVSVVVVDLR KRRNNQASS
Length:399
Mass (Da):43,350
Last modified:February 1, 1996 - v1
Checksum:i83B82E32FEC71D4D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS55457.
RefSeqiNP_187748.1. NM_111974.3.
UniGeneiAt.20739.

Genome annotation databases

EnsemblPlantsiAT3G11410.1; AT3G11410.1; AT3G11410.
GeneIDi820314.
KEGGiath:AT3G11410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S55457.
RefSeqi NP_187748.1. NM_111974.3.
UniGenei At.20739.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4N0G X-ray 2.38 A/B 72-399 [» ]
ProteinModelPortali P49598.
SMRi P49598. Positions 98-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 5648. 30 interactions.
DIPi DIP-40197N.
IntActi P49598. 9 interactions.
MINTi MINT-8390822.
STRINGi 3702.AT3G11410.1-P.

Proteomic databases

PRIDEi P49598.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G11410.1 ; AT3G11410.1 ; AT3G11410 .
GeneIDi 820314.
KEGGi ath:AT3G11410.

Organism-specific databases

TAIRi AT3G11410.

Phylogenomic databases

eggNOGi COG0631.
HOGENOMi HOG000233896.
InParanoidi P49598.
KOi K14497.
OMAi SCRCELQ.
PhylomeDBi P49598.

Enzyme and pathway databases

BioCyci ARA:AT3G11410-MONOMER.

Gene expression databases

Genevestigatori P49598.

Family and domain databases

Gene3Di 3.60.40.10. 1 hit.
InterProi IPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
Pfami PF00481. PP2C. 1 hit.
[Graphical view ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81606. SSF81606. 1 hit.
PROSITEi PS01032. PP2C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiP2C37_ARATH
AccessioniPrimary (citable) accession number: P49598
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3