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O04719

- P2C77_ARATH

UniProt

O04719 - P2C77_ARATH

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Protein
Protein phosphatase 2C 77
Gene
ABI2, At5g57050, MHM17.19
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1 By similarity
Metal bindingi165 – 1651Manganese 2 By similarity
Metal bindingi166 – 1661Manganese 1; via carbonyl oxygen By similarity
Sitei290 – 2901Lock By similarity
Metal bindingi337 – 3371Manganese 2 By similarity
Metal bindingi402 – 4021Manganese 2 By 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
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: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 77
PRO_0000057767Add
BLAST

Proteomic databases

PaxDbiO04719.
PRIDEiO04719.

Expressioni

Inductioni

Repressed by MYB44 and ERF4. Induced by salt stress and ABA.6 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

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.

Miscellaneous databases

EvolutionaryTraceiO04719.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 404294PP2C-like
Add
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.
Contains 1 PP2C-like domain.

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.
VSP_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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 127 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

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