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O04719

- P2C77_ARATH

UniProt

O04719 - P2C77_ARATH

Protein

Protein phosphatase 2C 77

Gene

ABI2

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 128 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), high light stress, response to glucose, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as H2O2 and oxidative burst in response to ABA and dehydration. Controls negatively fibrillin that is involved in mediating ABA-induced photoprotection. May be implicated in ABA content regulation. Involved in acquired thermotolerance of root growth and seedling survival. Required for the Erwinia amylovora harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic response.23 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.1 Publication

    Enzyme regulationi

    Phosphatase activity repressed by oxidized ATGPX3, free fatty acids (e.g. arachidonic acid (20:4) and Linolenic acid (18:3)) and by H2O2. Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner.3 Publications

    pH dependencei

    Optimum pH is 8.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi165 – 1651Manganese 1By similarity
    Metal bindingi165 – 1651Manganese 2By similarity
    Metal bindingi166 – 1661Manganese 1; via carbonyl oxygenBy similarity
    Sitei290 – 2901LockBy similarity
    Metal bindingi337 – 3371Manganese 2By similarity
    Metal bindingi402 – 4021Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. abscisic acid-activated signaling pathway Source: UniProtKB-KW
    2. negative regulation of abscisic acid-activated signaling pathway Source: TAIR
    3. negative regulation of protein kinase activity Source: TAIR
    4. photoinhibition Source: TAIR
    5. protein dephosphorylation Source: InterPro
    6. response to abscisic acid Source: TAIR
    7. response to heat Source: TAIR
    8. response to osmotic stress Source: TAIR
    9. 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:AT5G57050-MONOMER.
    ARA:GQT-1437-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 2C 77 (EC:3.1.3.16)
    Short name:
    AtPP2C77
    Alternative name(s):
    Protein ABSCISIC ACID-INSENSITIVE 2
    Protein phosphatase 2C ABI2
    Short name:
    PP2C ABI2
    Gene namesi
    Name:ABI2
    Ordered Locus Names:At5g57050
    ORF Names:MHM17.19
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G57050.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi168 – 1681G → D in abi2; reduced phosphatase activity, reduced affinity with magnesium ions, loss of interaction with the fibrillin precursor protein, impaired ABA-mediated binding to PYR1, and reduced negative control on fibrillin activity. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 423423Protein phosphatase 2C 77PRO_0000057767Add
    BLAST

    Proteomic databases

    PaxDbiO04719.
    PRIDEiO04719.

    Expressioni

    Inductioni

    Repressed by MYB44 and ERF4. Induced by salt stress and ABA.4 Publications

    Gene expression databases

    GenevestigatoriO04719.

    Interactioni

    Subunit structurei

    Interacts with CIPK15/PKS3, GPX3, SCAR1, SCAR2, SCAR3 and SCARL. Interacts also with CIPK24/SOS2. Binds to the fibrillin precursor protein. Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL5, PYL6, PYL8 and PYL9, and with free PYL2, PYL3 and PYL4.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CIPK24Q9LDI34EBI-537680,EBI-537551
    PAP1O814395EBI-537680,EBI-962363
    PYL9Q84MC73EBI-537680,EBI-2349513
    PYR1O496863EBI-537680,EBI-2349590
    SWI3BQ84JG22EBI-537680,EBI-1102271

    Protein-protein interaction databases

    BioGridi21053. 14 interactions.
    DIPiDIP-35025N.
    IntActiO04719. 8 interactions.
    MINTiMINT-274841.

    Structurei

    Secondary structure

    1
    423
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi105 – 1084
    Beta strandi113 – 1186
    Beta strandi122 – 1243
    Beta strandi127 – 1326
    Helixi135 – 1395
    Helixi154 – 1563
    Beta strandi159 – 17012
    Helixi171 – 19121
    Helixi195 – 1973
    Helixi199 – 21719
    Helixi220 – 2245
    Beta strandi234 – 2396
    Beta strandi241 – 25111
    Beta strandi253 – 2586
    Beta strandi261 – 2666
    Helixi274 – 28310
    Beta strandi287 – 2959
    Turni296 – 2983
    Beta strandi299 – 3035
    Helixi308 – 3103
    Turni311 – 3133
    Beta strandi319 – 3246
    Beta strandi329 – 3357
    Helixi337 – 3404
    Helixi345 – 36117
    Helixi372 – 3765
    Beta strandi378 – 3803
    Helixi382 – 39716
    Beta strandi404 – 4107

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NMVX-ray2.10B101-423[»]
    3UJKX-ray1.90A101-423[»]
    3UJLX-ray2.50B101-423[»]
    ProteinModelPortaliO04719.
    SMRiO04719. Positions 103-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO04719.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 404294PP2C-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.
    InParanoidiO04719.
    KOiK14497.
    OMAiFEINTRQ.
    PhylomeDBiO04719.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O04719-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDEVSPAVAV PFRPFTDPHA GLRGYCNGES RVTLPESSCS GDGAMKDSSF    50
    EINTRQDSLT SSSSAMAGVD ISAGDEINGS DEFDPRSMNQ SEKKVLSRTE 100
    SRSLFEFKCV PLYGVTSICG RRPEMEDSVS TIPRFLQVSS SSLLDGRVTN 150
    GFNPHLSAHF FGVYDGHGGS QVANYCRERM HLALTEEIVK EKPEFCDGDT 200
    WQEKWKKALF NSFMRVDSEI ETVAHAPETV GSTSVVAVVF PTHIFVANCG 250
    DSRAVLCRGK TPLALSVDHK PDRDDEAARI EAAGGKVIRW NGARVFGVLA 300
    MSRSIGDRYL KPSVIPDPEV TSVRRVKEDD CLILASDGLW DVMTNEEVCD 350
    LARKRILLWH KKNAMAGEAL LPAEKRGEGK DPAAMSAAEY LSKMALQKGS 400
    KDNISVVVVD LKGIRKFKSK SLN 423
    Length:423
    Mass (Da):46,306
    Last modified:July 1, 1997 - v1
    Checksum:i67CAAC76DA531A71
    GO
    Isoform 2 (identifier: O04719-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         29-68: Missing.

    Note: Derived from EST data. No experimental confirmation available.

    Show »
    Length:383
    Mass (Da):42,197
    Checksum:i4E346383F40C3C34
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei29 – 6840Missing in isoform 2. CuratedVSP_034834Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08966 Genomic DNA. Translation: CAA70163.1.
    Y08965 mRNA. Translation: CAA70162.1.
    Y11840 Genomic DNA. Translation: CAA72538.1.
    AB024035 Genomic DNA. Translation: BAA97035.1.
    CP002688 Genomic DNA. Translation: AED96839.1.
    CP002688 Genomic DNA. Translation: AED96840.1.
    AY136415 mRNA. Translation: AAM97081.1.
    BT008860 mRNA. Translation: AAP68299.1.
    RefSeqiNP_001119448.1. NM_001125976.1. [O04719-2]
    NP_200515.1. NM_125087.2. [O04719-1]
    UniGeneiAt.22051.

    Genome annotation databases

    EnsemblPlantsiAT5G57050.1; AT5G57050.1; AT5G57050. [O04719-1]
    GeneIDi835809.
    KEGGiath:AT5G57050.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08966 Genomic DNA. Translation: CAA70163.1 .
    Y08965 mRNA. Translation: CAA70162.1 .
    Y11840 Genomic DNA. Translation: CAA72538.1 .
    AB024035 Genomic DNA. Translation: BAA97035.1 .
    CP002688 Genomic DNA. Translation: AED96839.1 .
    CP002688 Genomic DNA. Translation: AED96840.1 .
    AY136415 mRNA. Translation: AAM97081.1 .
    BT008860 mRNA. Translation: AAP68299.1 .
    RefSeqi NP_001119448.1. NM_001125976.1. [O04719-2 ]
    NP_200515.1. NM_125087.2. [O04719-1 ]
    UniGenei At.22051.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NMV X-ray 2.10 B 101-423 [» ]
    3UJK X-ray 1.90 A 101-423 [» ]
    3UJL X-ray 2.50 B 101-423 [» ]
    ProteinModelPortali O04719.
    SMRi O04719. Positions 103-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 21053. 14 interactions.
    DIPi DIP-35025N.
    IntActi O04719. 8 interactions.
    MINTi MINT-274841.

    Proteomic databases

    PaxDbi O04719.
    PRIDEi O04719.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G57050.1 ; AT5G57050.1 ; AT5G57050 . [O04719-1 ]
    GeneIDi 835809.
    KEGGi ath:AT5G57050.

    Organism-specific databases

    TAIRi AT5G57050.

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000233896.
    InParanoidi O04719.
    KOi K14497.
    OMAi FEINTRQ.
    PhylomeDBi O04719.

    Enzyme and pathway databases

    BioCyci ARA:AT5G57050-MONOMER.
    ARA:GQT-1437-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O04719.

    Gene expression databases

    Genevestigatori O04719.

    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. "The Arabidopsis ABSCISIC ACID-INSENSITIVE2 (ABI2) and ABI1 genes encode homologous protein phosphatases 2C involved in abscisic acid signal transduction."
      Leung J., Merlot S., Giraudat J.
      Plant Cell 9:759-771(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF GLY-168.
      Strain: cv. Columbia and cv. Landsberg erecta.
    2. "ABI2, a second protein phosphatase 2C involved in abscisic acid signal transduction in Arabidopsis."
      Rodriguez P.L., Benning G., Grill E.
      FEBS Lett. 421:185-190(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Landsberg erecta.
    3. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
      Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
      DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "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.
    6. "Maternal effects govern variable dominance of two abscisic acid response mutations in Arabidopsis thaliana."
      Finkelstein R.R.
      Plant Physiol. 105:1203-1208(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Abscisic acid induces the alcohol dehydrogenase gene in Arabidopsis."
      de Bruxelles G.L., Peacock W.J., Dennis E.S., Dolferus R.
      Plant Physiol. 111:381-391(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Abscisic acid-independent and abscisic acid-dependent regulation of proline biosynthesis following cold and osmotic stresses in Arabidopsis thaliana."
      Savoure A., Hua X.-J., Bertauche N., Van Montagu M., Verbruggen N.
      Mol. Gen. Genet. 254:104-109(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Differential abscisic acid regulation of guard cell slow anion channels in Arabidopsis wild-type and abi1 and abi2 mutants."
      Pei Z.-M., Kuchitsu K., Ward J.M., Schwarz M., Schroeder J.I.
      Plant Cell 9:409-423(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Convergence of the abscisic acid, CO2, and extracellular calcium signal transduction pathways in stomatal guard cells."
      Webb A.A.R., Hetherington A.M.
      Plant Physiol. 114:1557-1560(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Arabidopsis abi1-1 and abi2-1 phosphatase mutations reduce abscisic acid-induced cytoplasmic calcium rises in guard cells."
      Allen G.J., Kuchitsu K., Chu S.P., Murata Y., Schroeder J.I.
      Plant Cell 11:1785-1798(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Analysis of Arabidopsis glucose insensitive mutants, gin5 and gin6, reveals a central role of the plant hormone ABA in the regulation of plant vegetative development by sugar."
      Arenas-Huertero F., Arroyo A., Zhou L., Sheen J., Leon P.
      Genes Dev. 14:2085-2096(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "The genes ABI1 and ABI2 are involved in abscisic acid- and drought-inducible expression of the Daucus carota L. Dc3 promoter in guard cells of transgenic Arabidopsis thaliana (L.) Heynh."
      Chak R.K.F., Thomas T.L., Quatrano R.S., Rock C.D.
      Planta 210:875-883(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Abscisic acid activation of plasma membrane Ca(2+) channels in guard cells requires cytosolic NAD(P)H and is differentially disrupted upstream and downstream of reactive oxygen species production in abi1-1 and abi2-1 protein phosphatase 2C mutants."
      Murata Y., Pei Z.-M., Mori I.C., Schroeder J.
      Plant Cell 13:2513-2523(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "The ABI1 and ABI2 protein phosphatases 2C act in a negative feedback regulatory loop of the abscisic acid signalling pathway."
      Merlot S., Gosti F., Guerrier D., Vavasseur A., Giraudat J.
      Plant J. 25:295-303(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "The role of ABA and the transpiration stream in the regulation of the osmotic water permeability of leaf cells."
      Morillon R., Chrispeels M.J.
      Proc. Natl. Acad. Sci. U.S.A. 98:14138-14143(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "A calcium sensor and its interacting protein kinase are global regulators of abscisic acid signaling in Arabidopsis."
      Guo Y., Xiong L., Song C.-P., Gong D., Halfter U., Zhu J.-K.
      Dev. Cell 3:233-244(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CIPK15/PKS3.
    18. "The sensitivity of ABI2 to hydrogen peroxide links the abscisic acid-response regulator to redox signalling."
      Meinhard M., Rodriguez P.L., Grill E.
      Planta 214:775-782(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    19. "Hydrotropism in abscisic acid, wavy, and gravitropic mutants of Arabidopsis thaliana."
      Takahashi N., Goto N., Okada K., Takahashi H.
      Planta 216:203-211(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Hypersensitivity of abscisic acid-induced cytosolic calcium increases in the Arabidopsis farnesyltransferase mutant era1-2."
      Allen G.J., Murata Y., Chu S.P., Nafisi M., Schroeder J.I.
      Plant Cell 14:1649-1662(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Regulation of the ABA-sensitive Arabidopsis potassium channel gene GORK in response to water stress."
      Becker D., Hoth S., Ache P., Wenkel S., Roelfsema M.R.G., Meyerhoff O., Hartung W., Hedrich R.
      FEBS Lett. 554:119-126(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and leaf water status during excess light stress reveals a functional organisation of Arabidopsis leaves."
      Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M., Baker N.R.
      Plant J. 33:691-705(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "A novel domain in the protein kinase SOS2 mediates interaction with the protein phosphatase 2C ABI2."
      Ohta M., Guo Y., Halfter U., Zhu J.-K.
      Proc. Natl. Acad. Sci. U.S.A. 100:11771-11776(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIPK24/SOS2.
    24. "Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is concertedly regulated by metabolic and stress-associated signals."
      Stepansky A., Galili G.
      Plant Physiol. 133:1407-1415(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Gain-of-function and loss-of-function phenotypes of the protein phosphatase 2C HAB1 reveal its role as a negative regulator of abscisic acid signalling."
      Saez A., Apostolova N., Gonzalez-Guzman M., Gonzalez-Garcia M.P., Nicolas C., Lorenzo O., Rodriguez P.L.
      Plant J. 37:354-369(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ABA.
    26. "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.
    27. "The ABI2-dependent abscisic acid signalling controls HrpN-induced drought tolerance in Arabidopsis."
      Dong H.-P., Yu H., Bao Z., Guo X., Peng J., Yao Z., Chen G., Qu S., Dong H.
      Planta 221:313-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "Arabidopsis ERF4 is a transcriptional repressor capable of modulating ethylene and abscisic acid responses."
      Yang Z., Tian L., Latoszek-Green M., Brown D., Wu K.
      Plant Mol. Biol. 58:585-596(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ERF4.
    29. "Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling pathways in the acquisition of thermotolerance."
      Larkindale J., Hall J.D., Knight M.R., Vierling E.
      Plant Physiol. 138:882-897(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "Role of abscisic acid (ABA) and Arabidopsis thaliana ABA-insensitive loci in low water potential-induced ABA and proline accumulation."
      Verslues P.E., Bray E.A.
      J. Exp. Bot. 57:201-212(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. "An Arabidopsis glutathione peroxidase functions as both a redox transducer and a scavenger in abscisic acid and drought stress responses."
      Miao Y., Lv D., Wang P., Wang X.-C., Chen J., Miao C., Song C.-P.
      Plant Cell 18:2749-2766(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPX3, REPRESSION BY OXIDIZED GPX3.
    32. "Fibrillin expression is regulated by abscisic acid response regulators and is involved in abscisic acid-mediated photoprotection."
      Yang Y., Sulpice R., Himmelbach A., Meinhard M., Christmann A., Grill E.
      Proc. Natl. Acad. Sci. U.S.A. 103:6061-6066(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-168, INTERACTION WITH THE FIBRILLIN PRECURSOR PROTEIN.
    33. "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell morphogenesis."
      Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M., Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.
      Development 134:967-977(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCAR1; SCAR2; SCAR3 AND SCARL.
    34. "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.
    35. "Interaction between sugar and abscisic acid signalling during early seedling development in Arabidopsis."
      Dekkers B.J.W., Schuurmans J.A.M.J., Smeekens S.C.M.
      Plant Mol. Biol. 67:151-167(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    36. "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.
    37. "Regulators of PP2C phosphatase activity function as abscisic acid sensors."
      Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A., Grill E.
      Science 324:1064-1068(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PYL9/RCAR1.
    38. Cited for: INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, ENZYME REGULATION, MUTAGENESIS OF GLY-168.
    39. "Closely related receptor complexes differ in their ABA selectivity and sensitivity."
      Szostkiewicz I., Richter K., Kepka M., Demmel S., Ma Y., Korte A., Assaad F.F., Christmann A., Grill E.
      Plant J. 61:25-35(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PYL8/RCAR3, ENZYME REGULATION BY PYR/PYL/RCAR.

    Entry informationi

    Entry nameiP2C77_ARATH
    AccessioniPrimary (citable) accession number: O04719
    Secondary accession number(s): B3H561
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The reduced form of ABI2 is converted to the oxidized form by the addition of oxidized GPX3 or H2O2.

    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