Reviewed, UniProtKB/Swiss-Prot P49597 (P2C56_ARATH)

Names and origin

Protein names

Recommended name:
    Protein phosphatase 2C 56
      Short name=AtPP2C56
    EC=3.1.3.16
Alternative name(s):
    Protein phosphatase 2C ABI1
      Short name=PP2C ABI1
    Protein ABSCISIC ACID-INSENSITIVE 1

Gene names

Name:	ABI1
Ordered Locus Names:	At4g26080
ORF Names:	F20B18.190

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Key component and 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), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates SRK2E/OST1 in response to ABA-dependent stimuli. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.46 Ref.47 Ref.49 Ref.50 Ref.51 Ref.52 Ref.54 Ref.56 Ref.57 Ref.59 Ref.60 Ref.62
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. Ref.15 Ref.26 Ref.24
Cofactor	Binds 2 magnesium or manganese ions per subunit. Ref.15 Ref.24
Enzyme regulation	Phosphatase activity repressed by oxidized GPX3 and phosphatidic acid (PA). PA is produced by PLD alpha 1 in response to ABA. Ref.47 Ref.57
Subunit structure	Interacts with ATHB-6, CIPK15/PKS3, GPX3, SRK2E/OST1, SCAR1, SCAR2, SCAR3 and SCARL. Binds to the PA released by the phospholipase D alpha 1 (PLDALPHA1) in response to ABA during the stomatal closure regulation. Ref.37 Ref.38 Ref.47 Ref.51 Ref.57 Ref.53 Ref.58
Subcellular location	Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein. Note: Associated to the plasma membrane when in complex with PA, subsequently to ABA signaling. Ref.47 Ref.62
Tissue specificity	Expressed in seeds and seedlings. In roots, confined to lateral root caps and columella cells. Ref.62 Ref.55
Induction	Repressed by MYB44. Induced by low temperature, drought, high salt, ABA and ethylene. Ref.60 Ref.55 Ref.35 Ref.45 Ref.63
Miscellaneous	Enhanced ABA signaling repressor activity by the proteosomal inhibitor MG132 accompanied by a cytoplasmic localization. Plants insensitive to ABA (abi1-1) are more resitant to P.syringae.
Sequence similarities	Belongs to the PP2C family. Contains 1 PP2C-like domain.
Biophysicochemical properties	pH dependence: Optimum pH is 8.

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	abscisic acid mediated signaling Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of abscisic acid mediated signaling Ref.57 Inferred from mutant phenotype. Source: TAIR protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro regulation of stomatal movement Ref.57 Inferred from mutant phenotype. Source: TAIR response to cold Ref.8 Ref.14 Inferred from mutant phenotype. Source: TAIR response to heat Ref.50 Inferred from mutant phenotype. Source: TAIR
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.62 Inferred from direct assay. Source: TAIR plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell protein serine/threonine phosphatase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.51 Inferred from physical interaction. Source: IntAct protein serine/threonine phosphatase activity Ref.24 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SRK2E	Q940H6	2	EBI-782526,EBI-782514

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 434	434	Protein phosphatase 2C 56		PRO_0000057766
Regions
	Domain	127 – 415	289	PP2C-like
	Motif	423 – 427	5	Nuclear localization signal Ref.62
	Compositional bias	417 – 420	4	Poly-Val
Sites
	Metal binding	177	1	Manganese 1 By similarity
	Metal binding	177	1	Manganese 2 By similarity
	Metal binding	178	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	347	1	Manganese 2 By similarity
	Metal binding	413	1	Manganese 2 By similarity
Experimental info
	Mutagenesis	67 – 68	2	RK → GA: Normal binding with PA, no reduction of phosphatase activity.
	Mutagenesis	73	1	R → A: Loss of binding with PA, no reduction of phosphatase activity. Ref.47 Ref.57
	Mutagenesis	93	1	D → A: No phenotype. Ref.25
	Mutagenesis	141 – 143	3	MED → IHG: Reduced inhibition of the ABA signaling pathway and loss of phosphatase activity. Ref.25
	Mutagenesis	174	1	G → D: No inhibition of the ABA signaling pathway and loss of phosphatase activity. Ref.25
	Mutagenesis	177 – 179	3	DGH → KLN: No inhibition of the ABA signaling pathway and loss of phosphatase activity. Ref.25 Ref.38 Ref.54 Ref.62
	Mutagenesis	177	1	D → A: Loss of phosphatase activity, impaired negative regulation of the ABA signaling pathway, reduced interaction with ATHB-6, and reduced negative control on fibrillin expression. Ref.38 Ref.54 Ref.62
	Mutagenesis	180	1	G → D in abi1; wilty phenotype, reduced phosphatase activity, ABA-insensitive seed germination and growth, and reduced interaction with ATHB-6. Increased sensitivity to ABA and loss of phosphatase activity; when associated with T-185, or Y-259, or C-304, or D-307, or F-314, or L-328, or N-316. No inhibition of the ABA signaling pathway and loss of phosphatase activity; when associated with D-174. Ref.15 Ref.25 Ref.28 Ref.38 Ref.62 Ref.24 Ref.3
	Mutagenesis	185	1	A → T: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.28
	Mutagenesis	259	1	C → Y: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.28
	Mutagenesis	304	1	R → C: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.28
	Mutagenesis	307	1	G → D: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.28
	Mutagenesis	314	1	S → F: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.28
	Mutagenesis	328	1	P → L: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.28
	Mutagenesis	416	1	S → N: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.28
	Mutagenesis	425 – 427	3	RRK → QNN: Cytoplasmic subcellular localization, and loss of negative regulation of the ABA signaling pathway. Ref.62
	Sequence conflict	24	1	G → R in AAK59578. Ref.5
	Sequence conflict	105	1	I → V in CAA55484. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P49597-1 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 4A4C54F04195F572	FASTA	434	47,506
	10 20 30 40 50 60 MEEVSPAIAG PFRPFSETQM DFTGIRLGKG YCNNQYSNQD SENGDLMVSL PETSSCSVSG 70 80 90 100 110 120 SHGSESRKVL ISRINSPNLN MKESAAADIV VVDISAGDEI NGSDITSEKK MISRTESRSL 130 140 150 160 170 180 FEFKSVPLYG FTSICGRRPE MEDAVSTIPR FLQSSSGSML DGRFDPQSAA HFFGVYDGHG 190 200 210 220 230 240 GSQVANYCRE RMHLALAEEI AKEKPMLCDG DTWLEKWKKA LFNSFLRVDS EIESVAPETV 250 260 270 280 290 300 GSTSVVAVVF PSHIFVANCG DSRAVLCRGK TALPLSVDHK PDREDEAARI EAAGGKVIQW 310 320 330 340 350 360 NGARVFGVLA MSRSIGDRYL KPSIIPDPEV TAVKRVKEDD CLILASDGVW DVMTDEEACE 370 380 390 400 410 420 MARKRILLWH KKNAVAGDAS LLADERRKEG KDPAAMSAAE YLSKLAIQRG SKDNISVVVV 430 DLKPRRKLKS KPLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The A. thaliana disease resistance gene RPS2 encodes a protein containing a nucleotide-binding site and leucine-rich repeats." Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M. Cell 78:1089-1099(1994) [PubMed: 7923358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Leaf.
[2]	"Arabidopsis ABA response gene ABI1: features of a calcium-modulated protein phosphatase." Leung J., Bouvier-Durand M., Morris P.C., Guerrier D., Chefdor F., Giraudat J. Science 264:1448-1452(1994) [PubMed: 7910981] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Leaf.
[3]	"A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana." Meyer K., Leube M.P., Grill E. Science 264:1452-1455(1994) [PubMed: 8197457] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-180. Strain: cv. Landsberg erecta.
[4]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"The isolation and characterization of abscisic-acid insensitive mutants of Arabidopsis thaliana." Kornneef M., Reuling G., Karssen C.M. Physiol. Plantarum 61:377-383(1984) Cited for: FUNCTION.
[8]	"Cold acclimation and cold-regulated gene expression in ABA mutants of Arabidopsis thaliana." Gilmour S.J., Thomashow M.F. Plant Mol. Biol. 17:1233-1240(1991) [PubMed: 1834244] [Abstract] Cited for: FUNCTION.
[9]	"Abscisic acid elicits the water-stress response in root hairs of Arabidopsis thaliana." Schnall J.A., Quatrano R.S. Plant Physiol. 100:216-218(1992) [PubMed: 16652949] [Abstract] Cited for: FUNCTION.
[10]	"Abscisic acid-insensitive mutations provide evidence for stage-specific signal pathways regulating expression of an Arabidopsis late embryogenesis-abundant (lea) gene." Finkelstein R.R. Mol. Gen. Genet. 238:401-408(1993) [PubMed: 8492808] [Abstract] Cited for: FUNCTION.
[11]	"Maternal effects govern variable dominance of two abscisic acid response mutations in Arabidopsis thaliana." Finkelstein R.R. Plant Physiol. 105:1203-1208(1994) [PubMed: 12232276] [Abstract] Cited for: FUNCTION.
[12]	"Drought rhizogenesis in Arabidopsis thaliana (differential responses of hormonal mutants)." Vartanian N., Marcotte L., Giraudat J. Plant Physiol. 104:761-767(1994) [PubMed: 12232124] [Abstract] Cited for: FUNCTION.
[13]	"Sensitivity to abscisic acid of guard-cell K+ channels is suppressed by abi1-1, a mutant Arabidopsis gene encoding a putative protein phosphatase." Armstrong F., Leung J., Grabov A., Brearley J., Giraudat J., Blatt M.R. Proc. Natl. Acad. Sci. U.S.A. 92:9520-9524(1995) [PubMed: 7568166] [Abstract] Cited for: FUNCTION.
[14]	"Role of abscisic acid in drought-induced freezing tolerance, cold acclimation, and accumulation of lt178 and rab18 proteins in Arabidopsis thaliana." Maentylae E., Laang V., Palva E.T. Plant Physiol. 107:141-148(1995) [PubMed: 12228349] [Abstract] Cited for: FUNCTION.
[15]	"Protein phosphatase activity of abscisic acid insensitive 1 (ABI1) protein from Arabidopsis thaliana." Bertauche N., Leung J., Giraudat J. Eur. J. Biochem. 241:193-200(1996) [PubMed: 8898906] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-180, CATALYTIC ACTIVITY, COFACTORS.
[16]	"The Arabidopsis homeobox gene ATHB-7 is induced by water deficit and by abscisic acid." Soederman E., Mattsson J., Engstroem P. Plant J. 10:375-381(1996) [PubMed: 8771791] [Abstract] Cited for: FUNCTION.
[17]	"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: 9108297] [Abstract] Cited for: FUNCTION.
[18]	"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: 9090884] [Abstract] Cited for: FUNCTION.
[19]	"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: 9165752] [Abstract] Cited for: FUNCTION.
[20]	"Interactions between the ABI1 and the ectopically expressed ABI3 genes in controlling abscisic acid responses in Arabidopsis vegetative tissues." Parcy F., Giraudat J. Plant J. 11:693-702(1997) [PubMed: 9161030] [Abstract] Cited for: FUNCTION.
[21]	"Alteration of anion channel kinetics in wild-type and abi1-1 transgenic Nicotiana benthamiana guard cells by abscisic acid." Grabov A., Leung J., Giraudat J., Blatt M.R. Plant J. 12:203-213(1997) [PubMed: 9263461] [Abstract] Cited for: FUNCTION.
[22]	"Differential expression of two P5CS genes controlling proline accumulation during salt-stress requires ABA and is regulated by ABA1, ABI1 and AXR2 in Arabidopsis." Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A., Schell J., Koncz C., Szabados L. Plant J. 12:557-569(1997) [PubMed: 9351242] [Abstract] Cited for: FUNCTION.
[23]	"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: 9276963] [Abstract] Cited for: FUNCTION.
[24]	"ABI1 of Arabidopsis is a protein serine/threonine phosphatase highly regulated by the proton and magnesium ion concentration." Leube M.P., Grill E., Amrhein N. FEBS Lett. 424:100-104(1998) [PubMed: 9537523] [Abstract] Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-180, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[25]	"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: 9448270] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-93; 141-MET--ASP-143; GLY-174; 177-ASP--HIS-179 AND GLY-180.
[26]	"The role of ABI1 in abscisic acid signal transduction: from gene to cell." Leung J., Merlot S., Gosti F., Bertauche N., Blatt M.R., Giraudat J. Symp. Soc. Exp. Biol. 51:65-71(1998) [PubMed: 10645425] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[27]	"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: 10488243] [Abstract] Cited for: FUNCTION.
[28]	"ABI1 protein phosphatase 2C is a negative regulator of abscisic acid signaling." Gosti F., Beaudoin N., Serizet C., Webb A.A.R., Vartanian N., Giraudat J. Plant Cell 11:1897-1909(1999) [PubMed: 10521520] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-180; ALA-185; CYS-259; ARG-304; GLY-307; SER-314; PRO-328 AND SER-416.
[29]	"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: 10950871] [Abstract] Cited for: FUNCTION.
[30]	"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: 10872217] [Abstract] Cited for: FUNCTION.
[31]	"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: 11707572] [Abstract] Cited for: FUNCTION.
[32]	"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: 11208021] [Abstract] Cited for: FUNCTION.
[33]	"Dissection of abscisic acid signal transduction pathways in barley aleurone layers." Shen Q., Gomez-Cadenas A., Zhang P., Walker-Simmons M.K., Sheen J., Ho T.-H.D. Plant Mol. Biol. 47:437-448(2001) [PubMed: 11587514] [Abstract] Cited for: FUNCTION.
[34]	"Cortical actin filaments in guard cells respond differently to abscisic acid in wild-type and abi1-1 mutant Arabidopsis." Eun S.-O., Bae S.-H., Lee Y. Planta 212:466-469(2001) [PubMed: 11289613] [Abstract] Cited for: FUNCTION.
[35]	"Antisense inhibition of protein phosphatase 2C accelerates cold acclimation in Arabidopsis thaliana." Taehtiharju S., Palva T. Plant J. 26:461-470(2001) [PubMed: 11439132] [Abstract] Cited for: INDUCTION.
[36]	"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: 11701885] [Abstract] Cited for: FUNCTION.
[37]	"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: 12194854] [Abstract] Cited for: FUNCTION, INTERACTION WITH CIPK15/PKS3.
[38]	"Homeodomain protein ATHB6 is a target of the protein phosphatase ABI1 and regulates hormone responses in Arabidopsis." Himmelbach A., Hoffmann T., Leube M., Hoehener B., Grill E. EMBO J. 21:3029-3038(2002) [PubMed: 12065416] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-177 AND GLY-180, INTERACTION WITH ATHB-6.
[39]	"Genome-wide gene expression profiling in Arabidopsis thaliana reveals new targets of abscisic acid and largely impaired gene regulation in the abi1-1 mutant." Hoth S., Morgante M., Sanchez J.-P., Hanafey M.K., Tingey S.V., Chua N.-H. J. Cell Sci. 115:4891-4900(2002) [PubMed: 12432076] [Abstract] Cited for: FUNCTION.
[40]	"Use of infrared thermal imaging to isolate Arabidopsis mutants defective in stomatal regulation." Merlot S., Mustilli A.-C., Genty B., North H., Lefebvre V., Sotta B., Vavasseur A., Giraudat J. Plant J. 30:601-609(2002) [PubMed: 12047634] [Abstract] Cited for: FUNCTION.
[41]	"The abi1-1 mutation blocks ABA signaling downstream of cADPR action." Wu Y., Sanchez J.P., Lopez-Molina L., Himmelbach A., Grill E., Chua N.-H. Plant J. 34:307-315(2003) [PubMed: 12713537] [Abstract] Cited for: FUNCTION.
[42]	"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: 14576281] [Abstract] Cited for: FUNCTION.
[43]	"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: 14596925] [Abstract] Cited for: FUNCTION.
[44]	"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: 12609042] [Abstract] Cited for: FUNCTION.
[45]	"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: 14731256] [Abstract] Cited for: INDUCTION BY ABA.
[46]	"Drought tolerance established by enhanced expression of the CC-NBS-LRR gene, ADR1, requires salicylic acid, EDS1 and ABI1." Chini A., Grant J.J., Seki M., Shinozaki K., Loake G.J. Plant J. 38:810-822(2004) [PubMed: 15144382] [Abstract] Cited for: FUNCTION.
[47]	"Phospholipase D alpha 1-derived phosphatidic acid interacts with ABI1 phosphatase 2C and regulates abscisic acid signaling." Zhang W., Qin C., Zhao J., Wang X. Proc. Natl. Acad. Sci. U.S.A. 101:9508-9513(2004) [PubMed: 15197253] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 67-ARG-LYS-68 AND ARG-73, SUBCELLULAR LOCATION, ENZYME REGULATION, INTERACTION WITH PA.
[48]	"Plant PP2C phosphatases: emerging functions in stress signaling." Schweighofer A., Hirt H., Meskiene I. Trends Plant Sci. 9:236-243(2004) [PubMed: 15130549] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[49]	"Generation of active pools of abscisic acid revealed by in vivo imaging of water-stressed Arabidopsis." Christmann A., Hoffmann T., Teplova I., Grill E., Mueller A. Plant Physiol. 137:209-219(2005) [PubMed: 15618419] [Abstract] Cited for: FUNCTION.
[50]	"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: 15923322] [Abstract] Cited for: FUNCTION.
[51]	"The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and integrates abscisic acid (ABA) and osmotic stress signals controlling stomatal closure in Arabidopsis." Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F., Shinozaki K. J. Biol. Chem. 281:5310-5318(2006) [PubMed: 16365038] [Abstract] Cited for: FUNCTION, INTERACTION WITH SRK2E.
[52]	"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: 16339784] [Abstract] Cited for: FUNCTION.
[53]	"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: 16998070] [Abstract] Cited for: INTERACTION WITH GPX3, REPRESSION BY OXIDIZED GPX3.
[54]	"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: 16571665] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-177.
[55]	"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: 16339800] [Abstract] Cited for: INDUCTION BY ABA, TISSUE SPECIFICITY.
[56]	"Enhancement of abscisic acid sensitivity and reduction of water consumption in Arabidopsis by combined inactivation of the protein phosphatases type 2C ABI1 and HAB1." Saez A., Robert N., Maktabi M.H., Schroeder J.I., Serrano R., Rodriguez P.L. Plant Physiol. 141:1389-1399(2006) [PubMed: 16798945] [Abstract] Cited for: FUNCTION.
[57]	"A bifurcating pathway directs abscisic acid effects on stomatal closure and opening in Arabidopsis." Mishra G., Zhang W., Deng F., Zhao J., Wang X. Science 312:264-266(2006) [PubMed: 16614222] [Abstract] Cited for: FUNCTION, INTERACTION WITH PA, ENZYME REGULATION, MUTAGENESIS OF ARG-73.
[58]	"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: 17267444] [Abstract] Cited for: INTERACTION WITH SCAR1; SCAR2; SCAR3 AND SCARL.
[59]	"Pseudomonas syringae pv. tomato hijacks the Arabidopsis abscisic acid signalling pathway to cause disease." de Torres-Zabala M., Truman W., Bennett M.H., Lafforgue G., Mansfield J.W., Rodriguez Egea P., Bogre L., Grant M. EMBO J. 26:1434-1443(2007) [PubMed: 17304219] [Abstract] Cited for: FUNCTION.
[60]	"Abscisic acid antagonizes ethylene-induced hyponastic growth in Arabidopsis." Benschop J.J., Millenaar F.F., Smeets M.E., van Zanten M., Voesenek L.A.C.J., Peeters A.J.M. Plant Physiol. 143:1013-1023(2007) [PubMed: 17158582] [Abstract] Cited for: FUNCTION, INDUCTION BY ETHYLENE.
[61]	"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: 19021904] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[62]	"Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards ABA responses in Arabidopsis." Moes D., Himmelbach A., Korte A., Haberer G., Grill E. Plant J. 54:806-819(2008) [PubMed: 18298671] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-177; GLY-180 AND 425-ARG--LYS-427, NLS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[63]	"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: 18162593] [Abstract] Cited for: INDUCTION BY MYB44 AND SALT.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U12856 mRNA. Translation: AAA50237.1. X77116 mRNA. Translation: CAA54383.1. X78886 Genomic DNA. Translation: CAA55484.1. AL049483 Genomic DNA. Translation: CAB39673.1. AL161564 Genomic DNA. Translation: CAB79463.1. AY035073 mRNA. Translation: AAK59578.1. AY142623 mRNA. Translation: AAN13081.1. AK226529 mRNA. Translation: BAE98668.1.
IPI	IPI00517333.
PIR	T04263.
RefSeq	NP_194338.1.
UniGene	At.21332
3D structure databases
HSSP	HSSP built from PDB template 1A6Q based on UniProtKB P35813.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49597. 1 interaction.
Genome annotation databases
GeneID	828714.
GenomeReviews	Gene locus AT4G26080 in contig CT486007_GR.
KEGG	ath:AT4G26080.
Organism-specific databases
TAIR	At4g26080.
Phylogenomic databases
OMA	P49597. NEEVCDA.
Enzyme and pathway databases
BRENDA	3.1.3.16. 302.
Gene expression databases
ArrayExpress	P49597.
GermOnline	AT4G26080. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR015655. PP2C. IPR001932. PP2C-related. IPR000222. PP2C_Mn2_Asp60_BS. IPR014045. PP2C_N. [Graphical view]
Gene3D	G3DSA:3.60.40.10. PP2C-related. 1 hit.
PANTHER	PTHR13832. PP2C. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P2C56_ARATH

Accession

Primary (citable) accession number: P49597
Secondary accession number(s): Q0WW30, Q43717, Q94C87

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	June 6, 2002
Last modified:	July 7, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)