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Protein phosphatase 2C 56 (AtPP2C56) (EC 3.1.3.16) (Protein ABSCISIC ACID-INSENSITIVE 1) (Protein phosphatase 2C ABI1) (PP2C ABI1)

 P2C56_ARATH             Reviewed;         434 AA.
P49597; Q0WW30; Q43717; Q94C87;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
25-OCT-2017, entry version 172.
RecName: Full=Protein phosphatase 2C 56;
Short=AtPP2C56;
EC=3.1.3.16;
AltName: Full=Protein ABSCISIC ACID-INSENSITIVE 1;
AltName: Full=Protein phosphatase 2C ABI1;
Short=PP2C ABI1;
Name=ABI1; OrderedLocusNames=At4g26080; ORFNames=F20B18.190;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=7923358; DOI=10.1016/0092-8674(94)90282-8;
Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M.;
"The A. thaliana disease resistance gene RPS2 encodes a protein
containing a nucleotide-binding site and leucine-rich repeats.";
Cell 78:1089-1099(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=7910981; DOI=10.1126/science.7910981;
Leung J., Bouvier-Durand M., Morris P.C., Guerrier D., Chefdor F.,
Giraudat J.;
"Arabidopsis ABA response gene ABI1: features of a calcium-modulated
protein phosphatase.";
Science 264:1448-1452(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-180.
STRAIN=cv. Landsberg erecta;
PubMed=8197457; DOI=10.1126/science.8197457;
Meyer K., Leube M.P., Grill E.;
"A protein phosphatase 2C involved in ABA signal transduction in
Arabidopsis thaliana.";
Science 264:1452-1455(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
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.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION.
DOI=10.1111/j.1399-3054.1984.tb06343.x;
Kornneef M., Reuling G., Karssen C.M.;
"The isolation and characterization of abscisic-acid insensitive
mutants of Arabidopsis thaliana.";
Physiol. Plantarum 61:377-383(1984).
[9]
FUNCTION.
PubMed=1834244; DOI=10.1007/BF00028738;
Gilmour S.J., Thomashow M.F.;
"Cold acclimation and cold-regulated gene expression in ABA mutants of
Arabidopsis thaliana.";
Plant Mol. Biol. 17:1233-1240(1991).
[10]
FUNCTION.
PubMed=16652949; DOI=10.1104/pp.100.1.216;
Schnall J.A., Quatrano R.S.;
"Abscisic acid elicits the water-stress response in root hairs of
Arabidopsis thaliana.";
Plant Physiol. 100:216-218(1992).
[11]
FUNCTION.
PubMed=8492808; DOI=10.1007/BF00291999;
Finkelstein R.R.;
"Abscisic acid-insensitive mutations provide evidence for stage-
specific signal pathways regulating expression of an Arabidopsis late
embryogenesis-abundant (lea) gene.";
Mol. Gen. Genet. 238:401-408(1993).
[12]
FUNCTION.
PubMed=12232276; DOI=10.1104/pp.105.4.1203;
Finkelstein R.R.;
"Maternal effects govern variable dominance of two abscisic acid
response mutations in Arabidopsis thaliana.";
Plant Physiol. 105:1203-1208(1994).
[13]
FUNCTION.
PubMed=12232124; DOI=10.1104/pp.104.2.761;
Vartanian N., Marcotte L., Giraudat J.;
"Drought rhizogenesis in Arabidopsis thaliana (differential responses
of hormonal mutants).";
Plant Physiol. 104:761-767(1994).
[14]
FUNCTION.
PubMed=7568166; DOI=10.1073/pnas.92.21.9520;
Armstrong F., Leung J., Grabov A., Brearley J., Giraudat J.,
Blatt M.R.;
"Sensitivity to abscisic acid of guard-cell K+ channels is suppressed
by abi1-1, a mutant Arabidopsis gene encoding a putative protein
phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 92:9520-9524(1995).
[15]
FUNCTION.
PubMed=12228349; DOI=10.1104/pp.107.1.141;
Maentylae E., Laang V., Palva E.T.;
"Role of abscisic acid in drought-induced freezing tolerance, cold
acclimation, and accumulation of lt178 and rab18 proteins in
Arabidopsis thaliana.";
Plant Physiol. 107:141-148(1995).
[16]
FUNCTION, MUTAGENESIS OF GLY-180, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=8898906; DOI=10.1111/j.1432-1033.1996.0193t.x;
Bertauche N., Leung J., Giraudat J.;
"Protein phosphatase activity of abscisic acid insensitive 1 (ABI1)
protein from Arabidopsis thaliana.";
Eur. J. Biochem. 241:193-200(1996).
[17]
FUNCTION.
PubMed=8771791; DOI=10.1046/j.1365-313X.1996.10020375.x;
Soederman E., Mattsson J., Engstroem P.;
"The Arabidopsis homeobox gene ATHB-7 is induced by water deficit and
by abscisic acid.";
Plant J. 10:375-381(1996).
[18]
FUNCTION.
PubMed=9108297; DOI=10.1007/s004380050397;
Savoure A., Hua X.-J., Bertauche N., Van Montagu M., Verbruggen N.;
"Abscisic acid-independent and abscisic acid-dependent regulation of
proline biosynthesis following cold and osmotic stresses in
Arabidopsis thaliana.";
Mol. Gen. Genet. 254:104-109(1997).
[19]
FUNCTION.
PubMed=9090884; DOI=10.1105/tpc.9.3.409;
Pei Z.-M., Kuchitsu K., Ward J.M., Schwarz M., Schroeder J.I.;
"Differential abscisic acid regulation of guard cell slow anion
channels in Arabidopsis wild-type and abi1 and abi2 mutants.";
Plant Cell 9:409-423(1997).
[20]
FUNCTION.
PubMed=9165752; DOI=10.1105/tpc.9.5.759;
Leung J., Merlot S., Giraudat J.;
"The Arabidopsis ABSCISIC ACID-INSENSITIVE2 (ABI2) and ABI1 genes
encode homologous protein phosphatases 2C involved in abscisic acid
signal transduction.";
Plant Cell 9:759-771(1997).
[21]
FUNCTION.
PubMed=9161030; DOI=10.1046/j.1365-313X.1997.11040693.x;
Parcy F., Giraudat J.;
"Interactions between the ABI1 and the ectopically expressed ABI3
genes in controlling abscisic acid responses in Arabidopsis vegetative
tissues.";
Plant J. 11:693-702(1997).
[22]
FUNCTION.
PubMed=9263461; DOI=10.1046/j.1365-313X.1997.12010203.x;
Grabov A., Leung J., Giraudat J., Blatt M.R.;
"Alteration of anion channel kinetics in wild-type and abi1-1
transgenic Nicotiana benthamiana guard cells by abscisic acid.";
Plant J. 12:203-213(1997).
[23]
FUNCTION.
PubMed=9351242; DOI=10.1046/j.1365-313X.1997.00557.x;
Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A.,
Schell J., Koncz C., Szabados L.;
"Differential expression of two P5CS genes controlling proline
accumulation during salt-stress requires ABA and is regulated by ABA1,
ABI1 and AXR2 in Arabidopsis.";
Plant J. 12:557-569(1997).
[24]
FUNCTION.
PubMed=9276963; DOI=10.1104/pp.114.4.1557;
Webb A.A.R., Hetherington A.M.;
"Convergence of the abscisic acid, CO2, and extracellular calcium
signal transduction pathways in stomatal guard cells.";
Plant Physiol. 114:1557-1560(1997).
[25]
CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-180, BIOPHYSICOCHEMICAL
PROPERTIES, AND COFACTOR.
PubMed=9537523; DOI=10.1016/S0014-5793(98)00149-5;
Leube M.P., Grill E., Amrhein N.;
"ABI1 of Arabidopsis is a protein serine/threonine phosphatase highly
regulated by the proton and magnesium ion concentration.";
FEBS Lett. 424:100-104(1998).
[26]
FUNCTION, AND MUTAGENESIS OF ASP-93; 141-MET--ASP-143; GLY-174;
177-ASP--HIS-179 AND GLY-180.
PubMed=9448270; DOI=10.1073/pnas.95.3.975;
Sheen J.;
"Mutational analysis of protein phosphatase 2C involved in abscisic
acid signal transduction in higher plants.";
Proc. Natl. Acad. Sci. U.S.A. 95:975-980(1998).
[27]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10645425;
Leung J., Merlot S., Gosti F., Bertauche N., Blatt M.R., Giraudat J.;
"The role of ABI1 in abscisic acid signal transduction: from gene to
cell.";
Symp. Soc. Exp. Biol. 51:65-71(1998).
[28]
FUNCTION.
PubMed=10488243; DOI=10.1105/tpc.11.9.1785;
Allen G.J., Kuchitsu K., Chu S.P., Murata Y., Schroeder J.I.;
"Arabidopsis abi1-1 and abi2-1 phosphatase mutations reduce abscisic
acid-induced cytoplasmic calcium rises in guard cells.";
Plant Cell 11:1785-1798(1999).
[29]
FUNCTION, AND MUTAGENESIS OF GLY-180; ALA-185; CYS-259; ARG-304;
GLY-307; SER-314; PRO-328 AND SER-416.
PubMed=10521520; DOI=10.1105/tpc.11.10.1897;
Gosti F., Beaudoin N., Serizet C., Webb A.A.R., Vartanian N.,
Giraudat J.;
"ABI1 protein phosphatase 2C is a negative regulator of abscisic acid
signaling.";
Plant Cell 11:1897-1909(1999).
[30]
FUNCTION.
PubMed=10950871;
Arenas-Huertero F., Arroyo A., Zhou L., Sheen J., Leon P.;
"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.";
Genes Dev. 14:2085-2096(2000).
[31]
FUNCTION.
PubMed=10872217; DOI=10.1007/s004250050692;
Chak R.K.F., Thomas T.L., Quatrano R.S., Rock C.D.;
"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.";
Planta 210:875-883(2000).
[32]
FUNCTION.
PubMed=11707572; DOI=10.1073/pnas.231471998;
Morillon R., Chrispeels M.J.;
"The role of ABA and the transpiration stream in the regulation of the
osmotic water permeability of leaf cells.";
Proc. Natl. Acad. Sci. U.S.A. 98:14138-14143(2001).
[33]
FUNCTION.
PubMed=11208021; DOI=10.1046/j.1365-313x.2001.00965.x;
Merlot S., Gosti F., Guerrier D., Vavasseur A., Giraudat J.;
"The ABI1 and ABI2 protein phosphatases 2C act in a negative feedback
regulatory loop of the abscisic acid signalling pathway.";
Plant J. 25:295-303(2001).
[34]
FUNCTION.
PubMed=11587514; DOI=10.1023/A:1011667312754;
Shen Q., Gomez-Cadenas A., Zhang P., Walker-Simmons M.K., Sheen J.,
Ho T.-H.D.;
"Dissection of abscisic acid signal transduction pathways in barley
aleurone layers.";
Plant Mol. Biol. 47:437-448(2001).
[35]
FUNCTION.
PubMed=11289613; DOI=10.1007/s004250000489;
Eun S.-O., Bae S.-H., Lee Y.;
"Cortical actin filaments in guard cells respond differently to
abscisic acid in wild-type and abi1-1 mutant Arabidopsis.";
Planta 212:466-469(2001).
[36]
INDUCTION.
PubMed=11439132; DOI=10.1046/j.1365-313X.2001.01048.x;
Taehtiharju S., Palva T.;
"Antisense inhibition of protein phosphatase 2C accelerates cold
acclimation in Arabidopsis thaliana.";
Plant J. 26:461-470(2001).
[37]
FUNCTION.
PubMed=11701885; DOI=10.1105/tpc.13.11.2513;
Murata Y., Pei Z.-M., Mori I.C., Schroeder J.;
"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.";
Plant Cell 13:2513-2523(2001).
[38]
FUNCTION, AND INTERACTION WITH CIPK15/PKS3.
PubMed=12194854; DOI=10.1016/S1534-5807(02)00229-0;
Guo Y., Xiong L., Song C.-P., Gong D., Halfter U., Zhu J.-K.;
"A calcium sensor and its interacting protein kinase are global
regulators of abscisic acid signaling in Arabidopsis.";
Dev. Cell 3:233-244(2002).
[39]
FUNCTION, MUTAGENESIS OF ASP-177 AND GLY-180, AND INTERACTION WITH
ATHB-6.
PubMed=12065416; DOI=10.1093/emboj/cdf316;
Himmelbach A., Hoffmann T., Leube M., Hoehener B., Grill E.;
"Homeodomain protein ATHB6 is a target of the protein phosphatase ABI1
and regulates hormone responses in Arabidopsis.";
EMBO J. 21:3029-3038(2002).
[40]
FUNCTION.
PubMed=12432076; DOI=10.1242/jcs.00175;
Hoth S., Morgante M., Sanchez J.-P., Hanafey M.K., Tingey S.V.,
Chua N.-H.;
"Genome-wide gene expression profiling in Arabidopsis thaliana reveals
new targets of abscisic acid and largely impaired gene regulation in
the abi1-1 mutant.";
J. Cell Sci. 115:4891-4900(2002).
[41]
FUNCTION.
PubMed=12047634; DOI=10.1046/j.1365-313X.2002.01322.x;
Merlot S., Mustilli A.-C., Genty B., North H., Lefebvre V., Sotta B.,
Vavasseur A., Giraudat J.;
"Use of infrared thermal imaging to isolate Arabidopsis mutants
defective in stomatal regulation.";
Plant J. 30:601-609(2002).
[42]
FUNCTION.
PubMed=12713537; DOI=10.1046/j.1365-313X.2003.01721.x;
Wu Y., Sanchez J.P., Lopez-Molina L., Himmelbach A., Grill E.,
Chua N.-H.;
"The abi1-1 mutation blocks ABA signaling downstream of cADPR
action.";
Plant J. 34:307-315(2003).
[43]
FUNCTION.
PubMed=14576281; DOI=10.1104/pp.103.026294;
Stepansky A., Galili G.;
"Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate
reductase/saccharopine dehydrogenase enzyme of lysine catabolism is
concertedly regulated by metabolic and stress-associated signals.";
Plant Physiol. 133:1407-1415(2003).
[44]
FUNCTION.
PubMed=14596925; DOI=10.1016/S0014-5793(03)01118-9;
Becker D., Hoth S., Ache P., Wenkel S., Roelfsema M.R.G.,
Meyerhoff O., Hartung W., Hedrich R.;
"Regulation of the ABA-sensitive Arabidopsis potassium channel gene
GORK in response to water stress.";
FEBS Lett. 554:119-126(2003).
[45]
FUNCTION.
PubMed=12609042; DOI=10.1046/j.1365-313X.2003.01656.x;
Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M.,
Baker N.R.;
"Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and
leaf water status during excess light stress reveals a functional
organisation of Arabidopsis leaves.";
Plant J. 33:691-705(2003).
[46]
INDUCTION BY ABA.
PubMed=14731256; DOI=10.1046/j.1365-313X.2003.01966.x;
Saez A., Apostolova N., Gonzalez-Guzman M., Gonzalez-Garcia M.P.,
Nicolas C., Lorenzo O., Rodriguez P.L.;
"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.";
Plant J. 37:354-369(2004).
[47]
FUNCTION.
PubMed=15144382; DOI=10.1111/j.1365-313X.2004.02086.x;
Chini A., Grant J.J., Seki M., Shinozaki K., Loake G.J.;
"Drought tolerance established by enhanced expression of the CC-NBS-
LRR gene, ADR1, requires salicylic acid, EDS1 and ABI1.";
Plant J. 38:810-822(2004).
[48]
FUNCTION, MUTAGENESIS OF 67-ARG-LYS-68 AND ARG-73, SUBCELLULAR
LOCATION, ENZYME REGULATION, AND INTERACTION WITH PA.
PubMed=15197253; DOI=10.1073/pnas.0402112101;
Zhang W., Qin C., Zhao J., Wang X.;
"Phospholipase D alpha 1-derived phosphatidic acid interacts with ABI1
phosphatase 2C and regulates abscisic acid signaling.";
Proc. Natl. Acad. Sci. U.S.A. 101:9508-9513(2004).
[49]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15130549; DOI=10.1016/j.tplants.2004.03.007;
Schweighofer A., Hirt H., Meskiene I.;
"Plant PP2C phosphatases: emerging functions in stress signaling.";
Trends Plant Sci. 9:236-243(2004).
[50]
FUNCTION.
PubMed=15618419; DOI=10.1104/pp.104.053082;
Christmann A., Hoffmann T., Teplova I., Grill E., Mueller A.;
"Generation of active pools of abscisic acid revealed by in vivo
imaging of water-stressed Arabidopsis.";
Plant Physiol. 137:209-219(2005).
[51]
FUNCTION.
PubMed=15923322; DOI=10.1104/pp.105.062257;
Larkindale J., Hall J.D., Knight M.R., Vierling E.;
"Heat stress phenotypes of Arabidopsis mutants implicate multiple
signaling pathways in the acquisition of thermotolerance.";
Plant Physiol. 138:882-897(2005).
[52]
FUNCTION, AND INTERACTION WITH SRK2E.
PubMed=16365038; DOI=10.1074/jbc.M509820200;
Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F.,
Shinozaki K.;
"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.";
J. Biol. Chem. 281:5310-5318(2006).
[53]
FUNCTION.
PubMed=16339784; DOI=10.1093/jxb/erj026;
Verslues P.E., Bray E.A.;
"Role of abscisic acid (ABA) and Arabidopsis thaliana ABA-insensitive
loci in low water potential-induced ABA and proline accumulation.";
J. Exp. Bot. 57:201-212(2006).
[54]
INTERACTION WITH GPX3, AND REPRESSION BY OXIDIZED GPX3.
PubMed=16998070; DOI=10.1105/tpc.106.044230;
Miao Y., Lv D., Wang P., Wang X.-C., Chen J., Miao C., Song C.-P.;
"An Arabidopsis glutathione peroxidase functions as both a redox
transducer and a scavenger in abscisic acid and drought stress
responses.";
Plant Cell 18:2749-2766(2006).
[55]
FUNCTION, AND MUTAGENESIS OF ASP-177.
PubMed=16571665; DOI=10.1073/pnas.0501720103;
Yang Y., Sulpice R., Himmelbach A., Meinhard M., Christmann A.,
Grill E.;
"Fibrillin expression is regulated by abscisic acid response
regulators and is involved in abscisic acid-mediated
photoprotection.";
Proc. Natl. Acad. Sci. U.S.A. 103:6061-6066(2006).
[56]
INDUCTION BY ABA, AND TISSUE SPECIFICITY.
PubMed=16339800; DOI=10.1104/pp.105.070128;
Yoshida T., Nishimura N., Kitahata N., Kuromori T., Ito T., Asami T.,
Shinozaki K., Hirayama T.;
"ABA-hypersensitive germination3 encodes a protein phosphatase 2C
(AtPP2CA) that strongly regulates abscisic acid signaling during
germination among Arabidopsis protein phosphatase 2Cs.";
Plant Physiol. 140:115-126(2006).
[57]
FUNCTION.
PubMed=16798945; DOI=10.1104/pp.106.081018;
Saez A., Robert N., Maktabi M.H., Schroeder J.I., Serrano R.,
Rodriguez P.L.;
"Enhancement of abscisic acid sensitivity and reduction of water
consumption in Arabidopsis by combined inactivation of the protein
phosphatases type 2C ABI1 and HAB1.";
Plant Physiol. 141:1389-1399(2006).
[58]
FUNCTION, INTERACTION WITH PA, ENZYME REGULATION, AND MUTAGENESIS OF
ARG-73.
PubMed=16614222; DOI=10.1126/science.1123769;
Mishra G., Zhang W., Deng F., Zhao J., Wang X.;
"A bifurcating pathway directs abscisic acid effects on stomatal
closure and opening in Arabidopsis.";
Science 312:264-266(2006).
[59]
INTERACTION WITH SPK1; SCAR1; SCAR2; SCAR3 AND SCARL.
PubMed=17267444; DOI=10.1242/dev.02792;
Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M.,
Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.;
"The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell
morphogenesis.";
Development 134:967-977(2007).
[60]
FUNCTION.
PubMed=17304219; DOI=10.1038/sj.emboj.7601575;
de Torres-Zabala M., Truman W., Bennett M.H., Lafforgue G.,
Mansfield J.W., Rodriguez Egea P., Bogre L., Grant M.;
"Pseudomonas syringae pv. tomato hijacks the Arabidopsis abscisic acid
signalling pathway to cause disease.";
EMBO J. 26:1434-1443(2007).
[61]
FUNCTION, AND INDUCTION BY ETHYLENE.
PubMed=17158582; DOI=10.1104/pp.106.092700;
Benschop J.J., Millenaar F.F., Smeets M.E., van Zanten M.,
Voesenek L.A.C.J., Peeters A.J.M.;
"Abscisic acid antagonizes ethylene-induced hyponastic growth in
Arabidopsis.";
Plant Physiol. 143:1013-1023(2007).
[62]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19021904; DOI=10.1186/1471-2164-9-550;
Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C.,
Zhong Y.;
"Genome-wide and expression analysis of protein phosphatase 2C in rice
and Arabidopsis.";
BMC Genomics 9:550-550(2008).
[63]
FUNCTION, MUTAGENESIS OF ASP-177; GLY-180 AND 425-ARG--LYS-427,
NUCLEAR LOCALIZATION SIGNAL, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=18298671; DOI=10.1111/j.1365-313X.2008.03454.x;
Moes D., Himmelbach A., Korte A., Haberer G., Grill E.;
"Nuclear localization of the mutant protein phosphatase abi1 is
required for insensitivity towards ABA responses in Arabidopsis.";
Plant J. 54:806-819(2008).
[64]
INDUCTION BY MYB44 AND SALT.
PubMed=18162593; DOI=10.1104/pp.107.110981;
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.;
"Overexpression of AtMYB44 enhances stomatal closure to confer abiotic
stress tolerance in transgenic Arabidopsis.";
Plant Physiol. 146:623-635(2008).
[65]
FUNCTION, AND INTERACTION WITH SRK2E/OST1.
PubMed=19955405; DOI=10.1073/pnas.0912021106;
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.;
"Activity of guard cell anion channel SLAC1 is controlled by drought-
stress signaling kinase-phosphatase pair.";
Proc. Natl. Acad. Sci. U.S.A. 106:21425-21430(2009).
[66]
INTERACTION WITH PYL9/RCAR1.
PubMed=19407143; DOI=10.1126/science.1172408;
Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A.,
Grill E.;
"Regulators of PP2C phosphatase activity function as abscisic acid
sensors.";
Science 324:1064-1068(2009).
[67]
INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, MUTAGENESIS OF
GLY-180, AND ENZYME REGULATION.
PubMed=19407142; DOI=10.1126/science.1173041;
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.;
"Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL
family of START proteins.";
Science 324:1068-1071(2009).
[68]
INTERACTION WITH PYR1.
PubMed=19933100; DOI=10.1126/science.1181829;
Nishimura N., Hitomi K., Arvai A.S., Rambo R.P., Hitomi C.,
Cutler S.R., Schroeder J.I., Getzoff E.D.;
"Structural mechanism of abscisic acid binding and signaling by
dimeric PYR1.";
Science 326:1373-1379(2009).
[69]
INTERACTION WITH PYL8/RCAR3, AND ENZYME REGULATION BY PYR/PYL/RCAR.
PubMed=19769575; DOI=10.1111/j.1365-313X.2009.04025.x;
Szostkiewicz I., Richter K., Kepka M., Demmel S., Ma Y., Korte A.,
Assaad F.F., Christmann A., Grill E.;
"Closely related receptor complexes differ in their ABA selectivity
and sensitivity.";
Plant J. 61:25-35(2010).
[70]
INTERACTION WITH RPL12B; PYR1; PYL1; PYL4; PYL5; PYL6; PYL7; PYL8;
PYL9; PYL10; SRK2E/OST1; SRK2D/SNRK2-2 AND SRK2I/SNRK2-3.
PubMed=19874541; DOI=10.1111/j.1365-313X.2009.04054.x;
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.;
"PYR/PYL/RCAR family members are major in-vivo ABI1 protein
phosphatase 2C-interacting proteins in Arabidopsis.";
Plant J. 61:290-299(2010).
[71]
INTERACTION WITH CPK21 AND CPK23.
PubMed=20385816; DOI=10.1073/pnas.0912030107;
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.;
"Guard cell anion channel SLAC1 is regulated by CDPK protein kinases
with distinct Ca2+ affinities.";
Proc. Natl. Acad. Sci. U.S.A. 107:8023-8028(2010).
[72]
INTERACTION WITH PYL10.
PubMed=21658606; DOI=10.1016/j.molcel.2011.05.011;
Hao Q., Yin P., Li W., Wang L., Yan C., Lin Z., Wu J.Z., Wang J.,
Yan S.F., Yan N.;
"The molecular basis of ABA-independent inhibition of PP2Cs by a
subclass of PYL proteins.";
Mol. Cell 42:662-672(2011).
[73]
INTERACTION WITH PYL13.
PubMed=24165892; DOI=10.1038/cr.2013.143;
Li W., Wang L., Sheng X., Yan C., Zhou R., Hang J., Yin P., Yan N.;
"Molecular basis for the selective and ABA-independent inhibition of
PP2CA by PYL13.";
Cell Res. 23:1369-1379(2013).
[74]
FUNCTION, INTERACTION WITH MAPKKK18, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=26443375; DOI=10.1093/pcp/pcv146;
Mitula F., Tajdel M., Ciesla A., Kasprowicz-Maluski A., Kulik A.,
Babula-Skowronska D., Michalak M., Dobrowolska G., Sadowski J.,
Ludwikow A.;
"Arabidopsis ABA-activated kinase MAPKKK18 is regulated by protein
phosphatase 2C ABI1 and the ubiquitin-proteasome pathway.";
Plant Cell Physiol. 56:2351-2367(2015).
[75]
INDUCTION BY ABSCISIC ACID.
STRAIN=cv. Columbia;
PubMed=25680457; DOI=10.1007/s11103-015-0295-0;
Matsuoka D., Yasufuku T., Furuya T., Nanmori T.;
"An abscisic acid inducible Arabidopsis MAPKKK, MAPKKK18 regulates
leaf senescence via its kinase activity.";
Plant Mol. Biol. 87:565-575(2015).
[76]
X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 119-434 IN COMPLEX WITH
MANGANESE; ABA AND PYL1, AND INTERACTION WITH PYL2.
PubMed=19893533; DOI=10.1038/nsmb.1730;
Yin P., Fan H., Hao Q., Yuan X., Wu D., Pang Y., Yan C., Li W.,
Wang J., Yan N.;
"Structural insights into the mechanism of abscisic acid signaling by
PYL proteins.";
Nat. Struct. Mol. Biol. 16:1230-1236(2009).
[77]
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, AND INTERACTION WITH
PYL1.
PubMed=19855379; DOI=10.1038/nature08583;
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.;
"Structural basis of abscisic acid signalling.";
Nature 462:609-614(2009).
[78]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 117-434 IN COMPLEX WITH
MAGNESIUM.
PubMed=20729862; DOI=10.1038/nsmb.1887;
Melcher K., Xu Y., Ng L.-M., Zhou X.E., Soon F.-F., Chinnusamy V.,
Suino-Powell K.M., Kovach A., Tham F.S., Cutler S.R., Li J.,
Yong E.-L., Zhu J.-K., Xu H.E.;
"Identification and mechanism of ABA receptor antagonism.";
Nat. Struct. Mol. Biol. 17:1102-1108(2010).
-!- 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.
Represses MAPKKK18 activity and promotes MAPKKK18 degradation by
the proteasome pathway upon abscisic acid (ABA) treatment
(PubMed:26443375). {ECO:0000269|PubMed:10488243,
ECO:0000269|PubMed:10521520, ECO:0000269|PubMed:10645425,
ECO:0000269|PubMed:10872217, ECO:0000269|PubMed:10950871,
ECO:0000269|PubMed:11208021, ECO:0000269|PubMed:11289613,
ECO:0000269|PubMed:11587514, ECO:0000269|PubMed:11701885,
ECO:0000269|PubMed:11707572, ECO:0000269|PubMed:12047634,
ECO:0000269|PubMed:12065416, ECO:0000269|PubMed:12194854,
ECO:0000269|PubMed:12228349, ECO:0000269|PubMed:12232124,
ECO:0000269|PubMed:12232276, ECO:0000269|PubMed:12432076,
ECO:0000269|PubMed:12609042, ECO:0000269|PubMed:12713537,
ECO:0000269|PubMed:14576281, ECO:0000269|PubMed:14596925,
ECO:0000269|PubMed:15144382, ECO:0000269|PubMed:15197253,
ECO:0000269|PubMed:15618419, ECO:0000269|PubMed:15923322,
ECO:0000269|PubMed:16339784, ECO:0000269|PubMed:16365038,
ECO:0000269|PubMed:16571665, ECO:0000269|PubMed:16614222,
ECO:0000269|PubMed:16652949, ECO:0000269|PubMed:16798945,
ECO:0000269|PubMed:17158582, ECO:0000269|PubMed:17304219,
ECO:0000269|PubMed:18298671, ECO:0000269|PubMed:1834244,
ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:26443375,
ECO:0000269|PubMed:7568166, ECO:0000269|PubMed:8492808,
ECO:0000269|PubMed:8771791, ECO:0000269|PubMed:8898906,
ECO:0000269|PubMed:9090884, ECO:0000269|PubMed:9108297,
ECO:0000269|PubMed:9161030, ECO:0000269|PubMed:9165752,
ECO:0000269|PubMed:9263461, ECO:0000269|PubMed:9276963,
ECO:0000269|PubMed:9351242, ECO:0000269|PubMed:9448270,
ECO:0000269|Ref.8}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:10645425, ECO:0000269|PubMed:8898906,
ECO:0000269|PubMed:9537523}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20729862,
ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9537523};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:19893533,
ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9537523};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000269|PubMed:19893533, ECO:0000269|PubMed:20729862,
ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9537523};
-!- 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. {ECO:0000269|PubMed:15197253,
ECO:0000269|PubMed:16614222, ECO:0000269|PubMed:19407142,
ECO:0000269|PubMed:19769575}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:9537523};
-!- SUBUNIT: Interacts with SPK1, 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, PYL4 and PYL13. Binds
to RPL12B, CPK21 and CPK23. Binds to MAPKKK18 (PubMed:26443375).
{ECO:0000269|PubMed:12065416, ECO:0000269|PubMed:12194854,
ECO:0000269|PubMed:15197253, ECO:0000269|PubMed:16365038,
ECO:0000269|PubMed:16614222, ECO:0000269|PubMed:16998070,
ECO:0000269|PubMed:17267444, ECO:0000269|PubMed:19407142,
ECO:0000269|PubMed:19407143, ECO:0000269|PubMed:19769575,
ECO:0000269|PubMed:19855379, ECO:0000269|PubMed:19874541,
ECO:0000269|PubMed:19893533, ECO:0000269|PubMed:19933100,
ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:20385816,
ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:24165892,
ECO:0000269|PubMed:26443375}.
-!- INTERACTION:
Q8VZS8:PYL1; NbExp=10; IntAct=EBI-782526, EBI-2363104;
O80992:PYL2; NbExp=3; IntAct=EBI-782526, EBI-2363125;
Q9SSM7:PYL3; NbExp=2; IntAct=EBI-782526, EBI-2363144;
O80920:PYL4; NbExp=6; IntAct=EBI-782526, EBI-2349683;
Q9FLB1:PYL5; NbExp=5; IntAct=EBI-782526, EBI-2363181;
Q8S8E3:PYL6; NbExp=4; IntAct=EBI-782526, EBI-2363192;
Q84MC7:PYL9; NbExp=5; IntAct=EBI-782526, EBI-2349513;
O49686:PYR1; NbExp=9; IntAct=EBI-782526, EBI-2349590;
Q93ZY2:ROPGEF1; NbExp=4; IntAct=EBI-782526, EBI-4425188;
Q39192:SRK2D; NbExp=7; IntAct=EBI-782526, EBI-2363308;
Q940H6:SRK2E; NbExp=15; IntAct=EBI-782526, EBI-782514;
Q39193:SRK2I; NbExp=8; IntAct=EBI-782526, EBI-2620383;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell membrane;
Peripheral membrane protein. Note=Associated to the plasma
membrane when in complex with PA, subsequently to ABA signaling.
-!- TISSUE SPECIFICITY: Expressed in seeds and seedlings. In roots,
confined to lateral root caps and columella cells.
{ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:18298671}.
-!- INDUCTION: Repressed by MYB44. Induced by low temperature,
drought, high salt, abscisic acid (ABA) and ethylene.
{ECO:0000269|PubMed:11439132, ECO:0000269|PubMed:14731256,
ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:16998070,
ECO:0000269|PubMed:17158582, ECO:0000269|PubMed:18162593}.
-!- 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. {ECO:0000250|UniProtKB:Q9CAJ0}.
-!- DISRUPTION PHENOTYPE: In abi1td, enhanced induction of MKKK18
activity after 90 minutes of abscisic acid (ABA) treatment and
reduced degradation of MKKK18 by the proteasome.
{ECO:0000269|PubMed:26443375}.
-!- MISCELLANEOUS: Enhanced ABA signaling repressor activity by the
proteasomal inhibitor MG132 accompanied by a cytoplasmic
localization.
-!- MISCELLANEOUS: Plants insensitive to ABA (abi1-1) are more
resistant to P.syringae.
-!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U12856; AAA50237.1; -; mRNA.
EMBL; X77116; CAA54383.1; -; mRNA.
EMBL; X78886; CAA55484.1; -; Genomic_DNA.
EMBL; AL049483; CAB39673.1; -; Genomic_DNA.
EMBL; AL161564; CAB79463.1; -; Genomic_DNA.
EMBL; CP002687; AEE85155.1; -; Genomic_DNA.
EMBL; AY035073; AAK59578.1; -; mRNA.
EMBL; AY142623; AAN13081.1; -; mRNA.
EMBL; AK226529; BAE98668.1; -; mRNA.
PIR; T04263; T04263.
RefSeq; NP_194338.1; NM_118741.3.
UniGene; At.21332; -.
PDB; 3JRQ; X-ray; 2.10 A; A=125-429.
PDB; 3KDJ; X-ray; 1.88 A; B=119-434.
PDB; 3NMN; X-ray; 2.15 A; B/D=117-434.
PDBsum; 3JRQ; -.
PDBsum; 3KDJ; -.
PDBsum; 3NMN; -.
ProteinModelPortal; P49597; -.
SMR; P49597; -.
BioGrid; 14001; 62.
DIP; DIP-36706N; -.
IntAct; P49597; 29.
MINT; MINT-8390807; -.
STRING; 3702.AT4G26080.1; -.
iPTMnet; P49597; -.
PaxDb; P49597; -.
EnsemblPlants; AT4G26080.1; AT4G26080.1; AT4G26080.
GeneID; 828714; -.
Gramene; AT4G26080.1; AT4G26080.1; AT4G26080.
KEGG; ath:AT4G26080; -.
Araport; AT4G26080; -.
TAIR; locus:2005488; AT4G26080.
eggNOG; KOG0698; Eukaryota.
eggNOG; COG0631; LUCA.
HOGENOM; HOG000233896; -.
InParanoid; P49597; -.
KO; K14497; -.
OMA; HGSESRK; -.
OrthoDB; EOG09360DDO; -.
PhylomeDB; P49597; -.
BRENDA; 3.1.3.16; 399.
EvolutionaryTrace; P49597; -.
PRO; PR:P49597; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; P49597; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:CACAO.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; IDA:CACAO.
GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
GO; GO:0009409; P:response to cold; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
CDD; cd00143; PP2Cc; 1.
Gene3D; 3.60.40.10; -; 1.
InterPro; IPR015655; PP2C.
InterPro; IPR000222; PP2C_BS.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
Pfam; PF00481; PP2C; 1.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS01032; PPM_1; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
3D-structure; Abscisic acid signaling pathway; Cell membrane;
Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese;
Membrane; Metal-binding; Nucleus; Protein phosphatase;
Reference proteome.
CHAIN 1 434 Protein phosphatase 2C 56.
/FTId=PRO_0000057766.
DOMAIN 128 422 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
MOTIF 423 427 Nuclear localization signal.
{ECO:0000269|PubMed:18298671}.
COMPBIAS 417 420 Poly-Val.
METAL 177 177 Magnesium or manganese 1.
{ECO:0000244|PDB:3NMN}.
METAL 177 177 Magnesium or manganese 2.
{ECO:0000244|PDB:3KDJ,
ECO:0000244|PDB:3NMN}.
METAL 178 178 Magnesium or manganese 1; via carbonyl
oxygen. {ECO:0000250|UniProtKB:P35813}.
METAL 261 261 Magnesium or manganese 1.
{ECO:0000244|PDB:3NMN}.
METAL 262 262 Magnesium or manganese 1.
{ECO:0000250|UniProtKB:O04719}.
METAL 347 347 Magnesium or manganese 1; via amide
nitrogen. {ECO:0000244|PDB:3NMN}.
METAL 347 347 Magnesium or manganese 2.
{ECO:0000244|PDB:3KDJ,
ECO:0000244|PDB:3NMN}.
METAL 351 351 Magnesium or manganese 1.
{ECO:0000250|UniProtKB:P49598}.
METAL 413 413 Magnesium or manganese 2.
{ECO:0000244|PDB:3KDJ,
ECO:0000244|PDB:3NMN}.
SITE 300 300 Lock. {ECO:0000250|UniProtKB:Q9CAJ0}.
MUTAGEN 67 68 RK->GA: Normal binding with PA, no
reduction of phosphatase activity.
{ECO:0000269|PubMed:15197253}.
MUTAGEN 73 73 R->A: Loss of binding with PA, no
reduction of phosphatase activity.
{ECO:0000269|PubMed:15197253,
ECO:0000269|PubMed:16614222}.
MUTAGEN 93 93 D->A: No phenotype.
{ECO:0000269|PubMed:9448270}.
MUTAGEN 141 143 MED->IHG: Reduced inhibition of the ABA
signaling pathway and loss of phosphatase
activity. {ECO:0000269|PubMed:9448270}.
MUTAGEN 142 142 E->A: Reduced binding affinity for PYL1,
and impaired phosphatase activity.
{ECO:0000269|PubMed:19855379}.
MUTAGEN 174 174 G->D: No inhibition of the ABA signaling
pathway and loss of phosphatase activity.
{ECO:0000269|PubMed:9448270}.
MUTAGEN 177 179 DGH->KLN: No inhibition of the ABA
signaling pathway and loss of phosphatase
activity. {ECO:0000269|PubMed:9448270}.
MUTAGEN 177 177 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.
{ECO:0000269|PubMed:12065416,
ECO:0000269|PubMed:16571665,
ECO:0000269|PubMed:18298671}.
MUTAGEN 180 180 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.
{ECO:0000269|PubMed:10521520,
ECO:0000269|PubMed:12065416,
ECO:0000269|PubMed:18298671,
ECO:0000269|PubMed:19407142,
ECO:0000269|PubMed:8197457,
ECO:0000269|PubMed:8898906,
ECO:0000269|PubMed:9448270,
ECO:0000269|PubMed:9537523}.
MUTAGEN 185 185 A->T: Increased sensitivity to ABA and
loss of phosphatase activity; when
associated with D-180.
{ECO:0000269|PubMed:10521520}.
MUTAGEN 239 239 T->A: Normal affinity for PYL1.
{ECO:0000269|PubMed:19855379}.
MUTAGEN 259 259 C->Y: Increased sensitivity to ABA and
loss of phosphatase activity; when
associated with D-180.
{ECO:0000269|PubMed:10521520}.
MUTAGEN 298 298 I->A: Loss of affinity for PYL1.
{ECO:0000269|PubMed:19855379}.
MUTAGEN 300 300 W->A: Loss of affinity for PYL1.
{ECO:0000269|PubMed:19855379}.
MUTAGEN 304 304 R->A: Loss of affinity for PYL1.
{ECO:0000269|PubMed:10521520,
ECO:0000269|PubMed:19855379}.
MUTAGEN 304 304 R->C: Increased sensitivity to ABA and
loss of phosphatase activity; when
associated with D-180.
{ECO:0000269|PubMed:10521520,
ECO:0000269|PubMed:19855379}.
MUTAGEN 306 306 F->A: Reduced affinity for PYL1.
{ECO:0000269|PubMed:19855379}.
MUTAGEN 307 307 G->D: Increased sensitivity to ABA and
loss of phosphatase activity; when
associated with D-180.
{ECO:0000269|PubMed:10521520}.
MUTAGEN 308 308 V->A: Reduced affinity for PYL1.
{ECO:0000269|PubMed:19855379}.
MUTAGEN 314 314 S->F: Increased sensitivity to ABA and
loss of phosphatase activity; when
associated with D-180.
{ECO:0000269|PubMed:10521520}.
MUTAGEN 319 319 Y->A: Reduced affinity for PYL1.
{ECO:0000269|PubMed:19855379}.
MUTAGEN 328 328 P->L: Increased sensitivity to ABA and
loss of phosphatase activity; when
associated with D-180.
{ECO:0000269|PubMed:10521520}.
MUTAGEN 416 416 S->N: Increased sensitivity to ABA and
loss of phosphatase activity; when
associated with D-180.
{ECO:0000269|PubMed:10521520}.
MUTAGEN 425 427 RRK->QNN: Cytoplasmic subcellular
localization, and loss of negative
regulation of the ABA signaling pathway.
{ECO:0000269|PubMed:18298671}.
CONFLICT 24 24 G -> R (in Ref. 6; AAK59578).
{ECO:0000305}.
CONFLICT 105 105 I -> V (in Ref. 3; CAA55484).
{ECO:0000305}.
STRAND 129 134 {ECO:0000244|PDB:3KDJ}.
STRAND 138 140 {ECO:0000244|PDB:3KDJ}.
STRAND 143 148 {ECO:0000244|PDB:3KDJ}.
TURN 149 152 {ECO:0000244|PDB:3JRQ}.
HELIX 166 169 {ECO:0000244|PDB:3KDJ}.
STRAND 171 182 {ECO:0000244|PDB:3KDJ}.
HELIX 183 203 {ECO:0000244|PDB:3KDJ}.
HELIX 207 210 {ECO:0000244|PDB:3KDJ}.
HELIX 211 231 {ECO:0000244|PDB:3KDJ}.
HELIX 232 234 {ECO:0000244|PDB:3KDJ}.
STRAND 244 249 {ECO:0000244|PDB:3KDJ}.
STRAND 251 261 {ECO:0000244|PDB:3KDJ}.
STRAND 263 268 {ECO:0000244|PDB:3KDJ}.
STRAND 271 275 {ECO:0000244|PDB:3KDJ}.
HELIX 284 292 {ECO:0000244|PDB:3KDJ}.
STRAND 297 305 {ECO:0000244|PDB:3KDJ}.
TURN 306 308 {ECO:0000244|PDB:3KDJ}.
HELIX 318 320 {ECO:0000244|PDB:3KDJ}.
TURN 321 323 {ECO:0000244|PDB:3KDJ}.
STRAND 329 334 {ECO:0000244|PDB:3KDJ}.
STRAND 339 345 {ECO:0000244|PDB:3KDJ}.
HELIX 347 350 {ECO:0000244|PDB:3KDJ}.
HELIX 355 369 {ECO:0000244|PDB:3KDJ}.
HELIX 393 408 {ECO:0000244|PDB:3KDJ}.
STRAND 415 421 {ECO:0000244|PDB:3KDJ}.
SEQUENCE 434 AA; 47506 MW; 4A4C54F04195F572 CRC64;
MEEVSPAIAG PFRPFSETQM DFTGIRLGKG YCNNQYSNQD SENGDLMVSL PETSSCSVSG
SHGSESRKVL ISRINSPNLN MKESAAADIV VVDISAGDEI NGSDITSEKK MISRTESRSL
FEFKSVPLYG FTSICGRRPE MEDAVSTIPR FLQSSSGSML DGRFDPQSAA HFFGVYDGHG
GSQVANYCRE RMHLALAEEI AKEKPMLCDG DTWLEKWKKA LFNSFLRVDS EIESVAPETV
GSTSVVAVVF PSHIFVANCG DSRAVLCRGK TALPLSVDHK PDREDEAARI EAAGGKVIQW
NGARVFGVLA MSRSIGDRYL KPSIIPDPEV TAVKRVKEDD CLILASDGVW DVMTDEEACE
MARKRILLWH KKNAVAGDAS LLADERRKEG KDPAAMSAAE YLSKLAIQRG SKDNISVVVV
DLKPRRKLKS KPLN


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