P49597 (P2C56_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase 2C 56
Short name=AtPP2C56
EC=3.1.3.16

Alternative name(s):
Protein ABSCISIC ACID-INSENSITIVE 1
Protein phosphatase 2C ABI1
Short name=PP2C ABI1

Gene names

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

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
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/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1. 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.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.47 Ref.48 Ref.50 Ref.51 Ref.52 Ref.53 Ref.55 Ref.57 Ref.58 Ref.60 Ref.61 Ref.63 Ref.66
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. Ref.16 Ref.25 Ref.27
Cofactor	Binds 2 magnesium or manganese ions per subunit. Ref.16 Ref.25
Enzyme regulation	Phosphatase activity repressed by oxidized GPX3 and phosphatidic acid (PA). PA is produced by PLD alpha 1 in response to ABA. Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner. Ref.48 Ref.58 Ref.68 Ref.70
Subunit structure	Interacts with ATHB-6, CIPK15/PKS3, GPX3, SRK2E/OST1, SRK2D, SRK2I, 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. Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL5, PYL6, PYL7, PYL8, PYL9, PYL10, and with free PYL2, PYL3 and PYL4. Binds to RPL12B, CPK21 and CPK23. Ref.38 Ref.39 Ref.48 Ref.52 Ref.54 Ref.58 Ref.59 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73
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.48 Ref.63
Tissue specificity	Expressed in seeds and seedlings. In roots, confined to lateral root caps and columella cells. Ref.56 Ref.63
Induction	Repressed by MYB44. Induced by low temperature, drought, high salt, ABA and ethylene. Ref.36 Ref.46 Ref.48 Ref.56 Ref.58 Ref.61 Ref.64 Ref.68 Ref.70
Domain	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.
Miscellaneous	Enhanced ABA signaling repressor activity by the proteasomal inhibitor MG132 accompanied by a cytoplasmic localization. Plants insensitive to ABA (abi1-1) are more resistant to P.syringae.
Sequence similarities	Belongs to the PP2C family. Contains 1 PP2C-like domain.
Biophysicochemical properties	pH dependence: Optimum pH is 8. Ref.25

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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscisic acid mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of abscisic acid mediated signaling pathway Inferred from genetic interaction PubMed 18835996. Source: UniProtKB protein dephosphorylation Inferred from electronic annotation. Source: InterPro regulation of stomatal movement Inferred from mutant phenotype Ref.58. Source: TAIR response to abscisic acid stimulus Inferred from mutant phenotype Ref.11. Source: TAIR response to cold Inferred from mutant phenotype Ref.15Ref.9. Source: TAIR response to heat Inferred from mutant phenotype Ref.51. Source: TAIR
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.63. Source: TAIR plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay Ref.25. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PYL4	O80920	3	EBI-782526,EBI-2349683
PYL5	Q9FLB1	3	EBI-782526,EBI-2363181
PYL9	Q84MC7	4	EBI-782526,EBI-2349513
PYR1	O49686	7	EBI-782526,EBI-2349590
SRK2D	Q39192	4	EBI-782526,EBI-2363308
SRK2E	Q940H6	4	EBI-782526,EBI-782514
SRK2I	Q39193	3	EBI-782526,EBI-2620383

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.63

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

Site

300

1

Lock

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.48 Ref.58

Mutagenesis

93

1

D → A: No phenotype. Ref.26

Mutagenesis

141 – 143

3

MED → IHG: Reduced inhibition of the ABA signaling pathway and loss of phosphatase activity. Ref.26

Mutagenesis

142

1

E → A: Reduced binding affinity for PYL1, and impaired phosphatase activity. Ref.73

Mutagenesis

174

1

G → D: No inhibition of the ABA signaling pathway and loss of phosphatase activity. Ref.26

Mutagenesis

177 – 179

3

DGH → KLN: No inhibition of the ABA signaling pathway and loss of phosphatase activity. Ref.26 Ref.39 Ref.55 Ref.63

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.39 Ref.55 Ref.63

Mutagenesis

180

1

G → D in abi1; wilty phenotype, reduced phosphatase activity, ABA-insensitive seed germination and growth, impaired ABA-mediated binding to PYR1, 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.3 Ref.16 Ref.25 Ref.26 Ref.29 Ref.39 Ref.63 Ref.68

Mutagenesis

185

1

A → T: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.29

Mutagenesis

239

1

T → A: Normal affinity for PYL1. Ref.73

Mutagenesis

259

1

C → Y: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.29

Mutagenesis

298

1

I → A: Loss of affinity for PYL1. Ref.73

Mutagenesis

300

1

W → A: Loss of affinity for PYL1. Ref.73

Mutagenesis

304

1

R → A: Loss of affinity for PYL1. Ref.29 Ref.73

Mutagenesis

304

1

R → C: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.29 Ref.73

Mutagenesis

306

1

F → A: Reduced affinity for PYL1. Ref.73

Mutagenesis

307

1

G → D: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.29

Mutagenesis

308

1

V → A: Reduced affinity for PYL1. Ref.73

Mutagenesis

314

1

S → F: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.29

Mutagenesis

319

1

Y → A: Reduced affinity for PYL1. Ref.73

Mutagenesis

328

1

P → L: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.29

Mutagenesis

416

1

S → N: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. Ref.29

Mutagenesis

425 – 427

3

RRK → QNN: Cytoplasmic subcellular localization, and loss of negative regulation of the ABA signaling pathway. Ref.63

Sequence conflict

24

1

G → R in AAK59578. Ref.6

Sequence conflict

105

1

I → V in CAA55484. Ref.3

Secondary structure

1

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434

Helix Strand Turn

Details...

Beta strand

129 – 134

6

Beta strand

138 – 140

3

Beta strand

143 – 148

6

Turn

149 – 152

4

Helix

166 – 169

4

Beta strand

171 – 182

12

Helix

183 – 203

21

Helix

207 – 210

4

Helix

211 – 231

21

Helix

232 – 234

3

Beta strand

244 – 249

6

Beta strand

251 – 261

11

Beta strand

263 – 268

6

Beta strand

271 – 275

5

Helix

284 – 292

9

Beta strand

297 – 305

9

Turn

306 – 308

3

Helix

318 – 320

3

Turn

321 – 323

3

Beta strand

329 – 334

6

Beta strand

339 – 345

7

Helix

347 – 350

4

Helix

355 – 369

15

Helix

393 – 408

16

Beta strand

415 – 421

7

Sequences

	Sequence		Length	Mass (Da)
	P49597 [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

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[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"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.
[13]	"Drought rhizogenesis in Arabidopsis thaliana (differential responses of hormonal mutants)." Vartanian N., Marcotte L., Giraudat J. Plant Physiol. 104:761-767(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-180, CATALYTIC ACTIVITY, COFACTORS.
[17]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"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.
[19]	"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.
[20]	"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: FUNCTION.
[21]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[24]	"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.
[25]	"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] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-180, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[26]	"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 ASP-93; 141-MET--ASP-143; GLY-174; 177-ASP--HIS-179 AND GLY-180.
[27]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[28]	"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.
[29]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-180; ALA-185; CYS-259; ARG-304; GLY-307; SER-314; PRO-328 AND SER-416.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[35]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[36]	"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: INDUCTION.
[37]	"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.
[38]	"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.
[39]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-177 AND GLY-180, INTERACTION WITH ATHB-6.
[40]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[41]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[42]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[48]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 67-ARG-LYS-68 AND ARG-73, SUBCELLULAR LOCATION, ENZYME REGULATION, INTERACTION WITH PA.
[49]	"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.
[50]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[51]	"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.
[52]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SRK2E.
[53]	"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.
[54]	"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.
[55]	"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 ASP-177.
[56]	"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: INDUCTION BY ABA, TISSUE SPECIFICITY.
[57]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[58]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PA, ENZYME REGULATION, MUTAGENESIS OF ARG-73.
[59]	"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.
[60]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[61]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION BY ETHYLENE.
[62]	"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.
[63]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-177; GLY-180 AND 425-ARG--LYS-427, NUCLEAR LOCALIZATION SIGNAL, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[64]	"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.
[65]	"PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-interacting proteins in Arabidopsis." Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C., Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I. Plant J. 61:290-299(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RPL12B; PYR1; PYL1; PYL4; PYL5; PYL6; PYL7; PYL8; PYL9; PYL10; SRK2E/OST1; SRK2D/SNRK2-2 AND SRK2I/SNRK2-3.
[66]	"Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair." Geiger D., Scherzer S., Mumm P., Stange A., Marten I., Bauer H., Ache P., Matschi S., Liese A., Al-Rasheid K.A.S., Romeis T., Hedrich R. Proc. Natl. Acad. Sci. U.S.A. 106:21425-21430(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SRK2E/OST1.
[67]	"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.
[68]	"Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins." Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y., Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D., Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P., Zhu J.-K. , Schroeder J.I., Volkman B.F., Cutler S.R. Science 324:1068-1071(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, MUTAGENESIS OF GLY-180, ENZYME REGULATION.
[69]	"Structural mechanism of abscisic acid binding and signaling by dimeric PYR1." Nishimura N., Hitomi K., Arvai A.S., Rambo R.P., Hitomi C., Cutler S.R., Schroeder J.I., Getzoff E.D. Science 326:1373-1379(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PYR1.
[70]	"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.
[71]	"Guard cell anion channel SLAC1 is regulated by CDPK protein kinases with distinct Ca2+ affinities." Geiger D., Scherzer S., Mumm P., Marten I., Ache P., Matschi S., Liese A., Wellmann C., Al-Rasheid K.A.S., Grill E., Romeis T., Hedrich R. Proc. Natl. Acad. Sci. U.S.A. 107:8023-8028(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CPK21 AND CPK23.
[72]	"Structural insights into the mechanism of abscisic acid signaling by PYL proteins." Yin P., Fan H., Hao Q., Yuan X., Wu D., Pang Y., Yan C., Li W., Wang J., Yan N. Nat. Struct. Mol. Biol. 16:1230-1236(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 119-434 IN COMPLEX WITH ABA AND PYL1, INTERACTION WITH PYL2.
[73]	"Structural basis of abscisic acid signalling." Miyazono K.-I., Miyakawa T., Sawano Y., Kubota K., Kang H.-J., Asano A., Miyauchi Y., Takahashi M., Zhi Y., Fujita Y., Yoshida T., Kodaira K.-S., Yamaguchi-Shinozaki K., Tanokura M. Nature 462:609-614(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 125-429 IN COMPLEX WITH ABSCISIC ACID AND PYL1, MUTAGENESIS OF GLU-142; THR-239; ILE-298; TRP-300; ARG-304; PHE-306; VAL-308 AND TYR-319, INTERACTION WITH PYL1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
CP002687 Genomic DNA. Translation: AEE85155.1.
AY035073 mRNA. Translation: AAK59578.1.
AY142623 mRNA. Translation: AAN13081.1.
AK226529 mRNA. Translation: BAE98668.1.

IPI

IPI00517333.

PIR

T04263.

RefSeq

NP_194338.1. NM_118741.2.

UniGene

At.21332.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JRQ	X-ray	2.10	A	125-429	[»]
3KDJ	X-ray	1.88	B	119-434	[»]
3NMN	X-ray	2.15	B/D	117-434	[»]

ProteinModelPortal

P49597.

SMR

P49597. Positions 125-424.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36706N.

IntAct

P49597. 21 interactions.

MINT

MINT-8390807.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT4G26080.1; AT4G26080.1; AT4G26080.

GeneID

828714.

KEGG

ath:AT4G26080.

Organism-specific databases

TAIR

At4g26080.

Phylogenomic databases

eggNOG

COG0631.

HOGENOM

HOG000233896.

InParanoid

P49597.

KO

K14497.

OMA

QRGSKDN.

PhylomeDB

P49597.

ProtClustDB

CLSN2685901.

Gene expression databases

Genevestigator

P49597.

GermOnline

AT4G26080. Arabidopsis thaliana.

Family and domain databases

Gene3D

3.60.40.10. 1 hit.

InterPro

IPR001932. PP2C-like.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]

PANTHER

PTHR13832. PTHR13832. 1 hit.

Pfam

PF00481. PP2C. 1 hit.
[Graphical view]

SMART

SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]

SUPFAM

SSF81606. PP2C-related. 1 hit.

PROSITE

PS01032. PP2C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P49597.

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:	May 29, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program