O04719 (P2C77_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase 2C 77
Short name=AtPP2C77
EC=3.1.3.16

Alternative name(s):
Protein ABSCISIC ACID-INSENSITIVE 2
Protein phosphatase 2C ABI2
Short name=PP2C ABI2

Gene names

Name:	ABI2
Ordered Locus Names:	At5g57050
ORF Names:	MHM17.19

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	423 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.27 Ref.29 Ref.30 Ref.32 Ref.35
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit. Ref.18
Enzyme regulation	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. Ref.18 Ref.38 Ref.39
Subunit structure	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. Ref.17 Ref.23 Ref.31 Ref.32 Ref.33 Ref.37 Ref.38 Ref.39
Induction	Repressed by MYB44 and ERF4. Induced by salt stress and ABA. Ref.18 Ref.25 Ref.28 Ref.36 Ref.38 Ref.39
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 By similarity.
Miscellaneous	The reduced form of ABI2 is converted to the oxidized form by the addition of oxidized GPX3 or H2O2.
Sequence similarities	Belongs to the PP2C family. Contains 1 PP2C-like domain.
Biophysicochemical properties	pH dependence: Optimum pH is 8. Ref.18

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway
Coding sequence diversity	Alternative splicing
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 Ref.15. Source: TAIR negative regulation of protein kinase activity Inferred from direct assay PubMed 22730405. Source: TAIR photoinhibition Inferred from mutant phenotype Ref.32. Source: TAIR protein dephosphorylation Inferred from electronic annotation. Source: InterPro response to abscisic acid stimulus Inferred from mutant phenotype Ref.15. Source: TAIR response to heat Inferred from mutant phenotype Ref.29. Source: TAIR response to osmotic stress Inferred from mutant phenotype PubMed 11779861. Source: TAIR response to water deprivation Inferred from mutant phenotype Ref.27. Source: TAIR
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from sequence or structural similarity Ref.2. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CIPK24	Q9LDI3	4	EBI-537680,EBI-537551
PAP1	O81439	5	EBI-537680,EBI-962363
PYL9	Q84MC7	3	EBI-537680,EBI-2349513
PYR1	O49686	3	EBI-537680,EBI-2349590
SWI3B	Q84JG2	2	EBI-537680,EBI-1102271

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O04719-1)

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.

Isoform 2 (identifier: O04719-2)

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

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 423

423

Protein phosphatase 2C 77

PRO_0000057767

Regions

Domain

111 – 404

294

PP2C-like

Sites

Metal binding

165

1

Manganese 1 By similarity

Metal binding

165

1

Manganese 2 By similarity

Metal binding

166

1

Manganese 1; via carbonyl oxygen By similarity

Metal binding

337

1

Manganese 2 By similarity

Metal binding

402

1

Manganese 2 By similarity

Site

290

1

Lock By similarity

Natural variations

Alternative sequence

29 – 68

40

Missing in isoform 2.

VSP_034834

Experimental info

Mutagenesis

168

1

G → 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. Ref.1 Ref.32 Ref.38

Secondary structure

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423

Helix Strand Turn

Details...

Helix

105 – 108

4

Beta strand

113 – 118

6

Beta strand

122 – 124

3

Beta strand

127 – 132

6

Helix

135 – 139

5

Helix

154 – 156

3

Beta strand

159 – 170

12

Helix

171 – 191

21

Helix

195 – 197

3

Helix

199 – 217

19

Helix

220 – 224

5

Beta strand

234 – 239

6

Beta strand

241 – 251

11

Beta strand

253 – 258

6

Beta strand

261 – 266

6

Helix

274 – 283

10

Beta strand

287 – 295

9

Turn

296 – 298

3

Beta strand

299 – 303

5

Helix

308 – 310

3

Turn

311 – 313

3

Beta strand

319 – 324

6

Beta strand

329 – 335

7

Helix

337 – 340

4

Helix

345 – 361

17

Helix

372 – 376

5

Beta strand

378 – 380

3

Helix

382 – 397

16

Beta strand

404 – 410

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 67CAAC76DA531A71	FASTA	423	46,306
	10 20 30 40 50 60 MDEVSPAVAV PFRPFTDPHA GLRGYCNGES RVTLPESSCS GDGAMKDSSF EINTRQDSLT 70 80 90 100 110 120 SSSSAMAGVD ISAGDEINGS DEFDPRSMNQ SEKKVLSRTE SRSLFEFKCV PLYGVTSICG 130 140 150 160 170 180 RRPEMEDSVS TIPRFLQVSS SSLLDGRVTN GFNPHLSAHF FGVYDGHGGS QVANYCRERM 190 200 210 220 230 240 HLALTEEIVK EKPEFCDGDT WQEKWKKALF NSFMRVDSEI ETVAHAPETV GSTSVVAVVF 250 260 270 280 290 300 PTHIFVANCG DSRAVLCRGK TPLALSVDHK PDRDDEAARI EAAGGKVIRW NGARVFGVLA 310 320 330 340 350 360 MSRSIGDRYL KPSVIPDPEV TSVRRVKEDD CLILASDGLW DVMTNEEVCD LARKRILLWH 370 380 390 400 410 420 KKNAMAGEAL LPAEKRGEGK DPAAMSAAEY LSKMALQKGS KDNISVVVVD LKGIRKFKSK SLN
	Isoform 2 [UniParc]. Checksum: 4E346383F40C3C34	FASTA	383	42,197
	10 20 30 40 50 60 MDEVSPAVAV PFRPFTDPHA GLRGYCNGVD ISAGDEINGS DEFDPRSMNQ SEKKVLSRTE 70 80 90 100 110 120 SRSLFEFKCV PLYGVTSICG RRPEMEDSVS TIPRFLQVSS SSLLDGRVTN GFNPHLSAHF 130 140 150 160 170 180 FGVYDGHGGS QVANYCRERM HLALTEEIVK EKPEFCDGDT WQEKWKKALF NSFMRVDSEI 190 200 210 220 230 240 ETVAHAPETV GSTSVVAVVF PTHIFVANCG DSRAVLCRGK TPLALSVDHK PDRDDEAARI 250 260 270 280 290 300 EAAGGKVIRW NGARVFGVLA MSRSIGDRYL KPSVIPDPEV TSVRRVKEDD CLILASDGLW 310 320 330 340 350 360 DVMTNEEVCD LARKRILLWH KKNAMAGEAL LPAEKRGEGK DPAAMSAAEY LSKMALQKGS 370 380 KDNISVVVVD LKGIRKFKSK SLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00534643.
IPI00892255.

RefSeq

NP_001119448.1. NM_001125976.1.
NP_200515.1. NM_125087.2.

UniGene

At.22051.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O04719.

SMR

O04719. Positions 103-415.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35025N.

IntAct

O04719. 7 interactions.

MINT

MINT-274841.

Proteomic databases

PaxDb

O04719.

PRIDE

O04719.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G57050.1; AT5G57050.1; AT5G57050.

GeneID

835809.

KEGG

ath:AT5G57050.

Organism-specific databases

TAIR

At5g57050.

Phylogenomic databases

eggNOG

COG0631.

HOGENOM

HOG000233896.

InParanoid

O04719.

KO

K14497.

OMA

NAMAGEA.

PhylomeDB

O04719.

ProtClustDB

CLSN2685901.

Gene expression databases

Genevestigator

O04719.

GermOnline

AT5G57050. 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

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EvolutionaryTrace

O04719.

Entry information

Entry name

P2C77_ARATH

Accession

Primary (citable) accession number: O04719
Secondary accession number(s): B3H561

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program