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P49598

- P2C37_ARATH

UniProt

P49598 - P2C37_ARATH

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
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    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 binding Source: UniProtKB
    4. protein kinase binding Source: UniProtKB
    5. 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

    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

    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 – 1106
    Beta strandi119 – 13214
    Beta strandi134 – 14714
    Helixi148 – 16518
    Helixi173 – 18917
    Turni209 – 2124
    Helixi216 – 2194
    Beta strandi224 – 2296
    Beta strandi231 – 24111
    Beta strandi243 – 2486
    Beta strandi251 – 2566
    Helixi264 – 2729
    Beta strandi277 – 2859
    Turni286 – 2883
    Beta strandi289 – 2935
    Helixi298 – 3003
    Turni301 – 3033
    Beta strandi309 – 3146
    Beta strandi319 – 3257
    Helixi327 – 3304
    Helixi335 – 34511
    Helixi361 – 37515
    Beta strandi382 – 3887

    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

    MAGICCGVVG ETEPAAPVDS TSRASLRRRL DLLPSIKIVA DSAVAPPLEN    50
    CRKRQKRETV VLSTLPGNLD LDSNVRSENK KARSAVTNSN SVTEAESFFS 100
    DVPKIGTTSV CGRRRDMEDA VSIHPSFLQR NSENHHFYGV FDGHGCSHVA 150
    EKCRERLHDI VKKEVEVMAS DEWTETMVKS FQKMDKEVSQ RECNLVVNGA 200
    TRSMKNSCRC ELQSPQCDAV GSTAVVSVVT PEKIIVSNCG DSRAVLCRNG 250
    VAIPLSVDHK PDRPDELIRI QQAGGRVIYW DGARVLGVLA MSRAIGDNYL 300
    KPYVIPDPEV TVTDRTDEDE CLILASDGLW DVVPNETACG VARMCLRGAG 350
    AGDDSDAAHN ACSDAALLLT KLALARQSSD NVSVVVVDLR KRRNNQASS 399
    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

    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 1, 2014
    This is version 117 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