P2C56_ARATH
ID P2C56_ARATH Reviewed; 434 AA.
AC P49597; Q0WW30; Q43717; Q94C87;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Protein phosphatase 2C 56 {ECO:0000303|PubMed:19021904};
DE Short=AtPP2C56 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000269|PubMed:10645425, ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9537523};
DE AltName: Full=Protein ABSCISIC ACID-INSENSITIVE 1 {ECO:0000303|PubMed:7910981};
DE AltName: Full=Protein phosphatase 2C ABI1 {ECO:0000303|PubMed:7910981};
DE Short=PP2C ABI1 {ECO:0000303|PubMed:7910981};
GN Name=ABI1 {ECO:0000303|PubMed:7910981};
GN OrderedLocusNames=At4g26080 {ECO:0000312|Araport:AT4G26080};
GN ORFNames=F20B18.190 {ECO:0000312|EMBL:CAB39673.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7923358; DOI=10.1016/0092-8674(94)90282-8;
RA Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M.;
RT "The A. thaliana disease resistance gene RPS2 encodes a protein containing
RT a nucleotide-binding site and leucine-rich repeats.";
RL Cell 78:1089-1099(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7910981; DOI=10.1126/science.7910981;
RA Leung J., Bouvier-Durand M., Morris P.C., Guerrier D., Chefdor F.,
RA Giraudat J.;
RT "Arabidopsis ABA response gene ABI1: features of a calcium-modulated
RT protein phosphatase.";
RL Science 264:1448-1452(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-180.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8197457; DOI=10.1126/science.8197457;
RA Meyer K., Leube M.P., Grill E.;
RT "A protein phosphatase 2C involved in ABA signal transduction in
RT Arabidopsis thaliana.";
RL Science 264:1452-1455(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX DOI=10.1111/j.1399-3054.1984.tb06343.x;
RA Kornneef M., Reuling G., Karssen C.M.;
RT "The isolation and characterization of abscisic-acid insensitive mutants of
RT Arabidopsis thaliana.";
RL Physiol. Plantarum 61:377-383(1984).
RN [9]
RP FUNCTION.
RX PubMed=1834244; DOI=10.1007/bf00028738;
RA Gilmour S.J., Thomashow M.F.;
RT "Cold acclimation and cold-regulated gene expression in ABA mutants of
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 17:1233-1240(1991).
RN [10]
RP FUNCTION.
RX PubMed=16652949; DOI=10.1104/pp.100.1.216;
RA Schnall J.A., Quatrano R.S.;
RT "Abscisic acid elicits the water-stress response in root hairs of
RT Arabidopsis thaliana.";
RL Plant Physiol. 100:216-218(1992).
RN [11]
RP FUNCTION.
RX PubMed=8492808; DOI=10.1007/bf00291999;
RA Finkelstein R.R.;
RT "Abscisic acid-insensitive mutations provide evidence for stage-specific
RT signal pathways regulating expression of an Arabidopsis late embryogenesis-
RT abundant (lea) gene.";
RL Mol. Gen. Genet. 238:401-408(1993).
RN [12]
RP FUNCTION.
RX PubMed=12232276; DOI=10.1104/pp.105.4.1203;
RA Finkelstein R.R.;
RT "Maternal effects govern variable dominance of two abscisic acid response
RT mutations in Arabidopsis thaliana.";
RL Plant Physiol. 105:1203-1208(1994).
RN [13]
RP FUNCTION.
RX PubMed=12232124; DOI=10.1104/pp.104.2.761;
RA Vartanian N., Marcotte L., Giraudat J.;
RT "Drought rhizogenesis in Arabidopsis thaliana (differential responses of
RT hormonal mutants).";
RL Plant Physiol. 104:761-767(1994).
RN [14]
RP FUNCTION.
RX PubMed=7568166; DOI=10.1073/pnas.92.21.9520;
RA Armstrong F., Leung J., Grabov A., Brearley J., Giraudat J., Blatt M.R.;
RT "Sensitivity to abscisic acid of guard-cell K+ channels is suppressed by
RT abi1-1, a mutant Arabidopsis gene encoding a putative protein
RT phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9520-9524(1995).
RN [15]
RP FUNCTION.
RX PubMed=12228349; DOI=10.1104/pp.107.1.141;
RA Maentylae E., Laang V., Palva E.T.;
RT "Role of abscisic acid in drought-induced freezing tolerance, cold
RT acclimation, and accumulation of lt178 and rab18 proteins in Arabidopsis
RT thaliana.";
RL Plant Physiol. 107:141-148(1995).
RN [16]
RP FUNCTION, MUTAGENESIS OF GLY-180, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=8898906; DOI=10.1111/j.1432-1033.1996.0193t.x;
RA Bertauche N., Leung J., Giraudat J.;
RT "Protein phosphatase activity of abscisic acid insensitive 1 (ABI1) protein
RT from Arabidopsis thaliana.";
RL Eur. J. Biochem. 241:193-200(1996).
RN [17]
RP FUNCTION.
RX PubMed=8771791; DOI=10.1046/j.1365-313x.1996.10020375.x;
RA Soederman E., Mattsson J., Engstroem P.;
RT "The Arabidopsis homeobox gene ATHB-7 is induced by water deficit and by
RT abscisic acid.";
RL Plant J. 10:375-381(1996).
RN [18]
RP FUNCTION.
RX PubMed=9108297; DOI=10.1007/s004380050397;
RA Savoure A., Hua X.-J., Bertauche N., Van Montagu M., Verbruggen N.;
RT "Abscisic acid-independent and abscisic acid-dependent regulation of
RT proline biosynthesis following cold and osmotic stresses in Arabidopsis
RT thaliana.";
RL Mol. Gen. Genet. 254:104-109(1997).
RN [19]
RP FUNCTION.
RX PubMed=9090884; DOI=10.2307/3870491;
RA Pei Z.-M., Kuchitsu K., Ward J.M., Schwarz M., Schroeder J.I.;
RT "Differential abscisic acid regulation of guard cell slow anion channels in
RT Arabidopsis wild-type and abi1 and abi2 mutants.";
RL Plant Cell 9:409-423(1997).
RN [20]
RP FUNCTION.
RX PubMed=9165752; DOI=10.2307/3870430;
RA Leung J., Merlot S., Giraudat J.;
RT "The Arabidopsis ABSCISIC ACID-INSENSITIVE2 (ABI2) and ABI1 genes encode
RT homologous protein phosphatases 2C involved in abscisic acid signal
RT transduction.";
RL Plant Cell 9:759-771(1997).
RN [21]
RP FUNCTION.
RX PubMed=9161030; DOI=10.1046/j.1365-313x.1997.11040693.x;
RA Parcy F., Giraudat J.;
RT "Interactions between the ABI1 and the ectopically expressed ABI3 genes in
RT controlling abscisic acid responses in Arabidopsis vegetative tissues.";
RL Plant J. 11:693-702(1997).
RN [22]
RP FUNCTION.
RX PubMed=9263461; DOI=10.1046/j.1365-313x.1997.12010203.x;
RA Grabov A., Leung J., Giraudat J., Blatt M.R.;
RT "Alteration of anion channel kinetics in wild-type and abi1-1 transgenic
RT Nicotiana benthamiana guard cells by abscisic acid.";
RL Plant J. 12:203-213(1997).
RN [23]
RP FUNCTION.
RX PubMed=9351242; DOI=10.1111/j.0960-7412.1997.00557.x;
RA Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A.,
RA Schell J., Koncz C., Szabados L.;
RT "Differential expression of two P5CS genes controlling proline accumulation
RT during salt-stress requires ABA and is regulated by ABA1, ABI1 and AXR2 in
RT Arabidopsis.";
RL Plant J. 12:557-569(1997).
RN [24]
RP FUNCTION.
RX PubMed=9276963; DOI=10.1104/pp.114.4.1557;
RA Webb A.A.R., Hetherington A.M.;
RT "Convergence of the abscisic acid, CO2, and extracellular calcium signal
RT transduction pathways in stomatal guard cells.";
RL Plant Physiol. 114:1557-1560(1997).
RN [25]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-180, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND COFACTOR.
RX PubMed=9537523; DOI=10.1016/s0014-5793(98)00149-5;
RA Leube M.P., Grill E., Amrhein N.;
RT "ABI1 of Arabidopsis is a protein serine/threonine phosphatase highly
RT regulated by the proton and magnesium ion concentration.";
RL FEBS Lett. 424:100-104(1998).
RN [26]
RP FUNCTION, AND MUTAGENESIS OF ASP-93; 141-MET--ASP-143; GLY-174;
RP 177-ASP--HIS-179 AND GLY-180.
RX PubMed=9448270; DOI=10.1073/pnas.95.3.975;
RA Sheen J.;
RT "Mutational analysis of protein phosphatase 2C involved in abscisic acid
RT signal transduction in higher plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:975-980(1998).
RN [27]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10645425;
RA Leung J., Merlot S., Gosti F., Bertauche N., Blatt M.R., Giraudat J.;
RT "The role of ABI1 in abscisic acid signal transduction: from gene to
RT cell.";
RL Symp. Soc. Exp. Biol. 51:65-71(1998).
RN [28]
RP FUNCTION.
RX PubMed=10488243; DOI=10.2307/3871054;
RA Allen G.J., Kuchitsu K., Chu S.P., Murata Y., Schroeder J.I.;
RT "Arabidopsis abi1-1 and abi2-1 phosphatase mutations reduce abscisic acid-
RT induced cytoplasmic calcium rises in guard cells.";
RL Plant Cell 11:1785-1798(1999).
RN [29]
RP FUNCTION, AND MUTAGENESIS OF GLY-180; ALA-185; CYS-259; ARG-304; GLY-307;
RP SER-314; PRO-328 AND SER-416.
RX PubMed=10521520; DOI=10.2307/3871085;
RA Gosti F., Beaudoin N., Serizet C., Webb A.A.R., Vartanian N., Giraudat J.;
RT "ABI1 protein phosphatase 2C is a negative regulator of abscisic acid
RT signaling.";
RL Plant Cell 11:1897-1909(1999).
RN [30]
RP FUNCTION.
RX PubMed=10950871;
RA Arenas-Huertero F., Arroyo A., Zhou L., Sheen J., Leon P.;
RT "Analysis of Arabidopsis glucose insensitive mutants, gin5 and gin6,
RT reveals a central role of the plant hormone ABA in the regulation of plant
RT vegetative development by sugar.";
RL Genes Dev. 14:2085-2096(2000).
RN [31]
RP FUNCTION.
RX PubMed=10872217; DOI=10.1007/s004250050692;
RA Chak R.K.F., Thomas T.L., Quatrano R.S., Rock C.D.;
RT "The genes ABI1 and ABI2 are involved in abscisic acid- and drought-
RT inducible expression of the Daucus carota L. Dc3 promoter in guard cells of
RT transgenic Arabidopsis thaliana (L.) Heynh.";
RL Planta 210:875-883(2000).
RN [32]
RP FUNCTION.
RX PubMed=11707572; DOI=10.1073/pnas.231471998;
RA Morillon R., Chrispeels M.J.;
RT "The role of ABA and the transpiration stream in the regulation of the
RT osmotic water permeability of leaf cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14138-14143(2001).
RN [33]
RP FUNCTION.
RX PubMed=11208021; DOI=10.1046/j.1365-313x.2001.00965.x;
RA Merlot S., Gosti F., Guerrier D., Vavasseur A., Giraudat J.;
RT "The ABI1 and ABI2 protein phosphatases 2C act in a negative feedback
RT regulatory loop of the abscisic acid signalling pathway.";
RL Plant J. 25:295-303(2001).
RN [34]
RP FUNCTION.
RX PubMed=11587514; DOI=10.1023/a:1011667312754;
RA Shen Q., Gomez-Cadenas A., Zhang P., Walker-Simmons M.K., Sheen J.,
RA Ho T.-H.D.;
RT "Dissection of abscisic acid signal transduction pathways in barley
RT aleurone layers.";
RL Plant Mol. Biol. 47:437-448(2001).
RN [35]
RP FUNCTION.
RX PubMed=11289613; DOI=10.1007/s004250000489;
RA Eun S.-O., Bae S.-H., Lee Y.;
RT "Cortical actin filaments in guard cells respond differently to abscisic
RT acid in wild-type and abi1-1 mutant Arabidopsis.";
RL Planta 212:466-469(2001).
RN [36]
RP INDUCTION.
RX PubMed=11439132; DOI=10.1046/j.1365-313x.2001.01048.x;
RA Taehtiharju S., Palva T.;
RT "Antisense inhibition of protein phosphatase 2C accelerates cold
RT acclimation in Arabidopsis thaliana.";
RL Plant J. 26:461-470(2001).
RN [37]
RP FUNCTION.
RX PubMed=11701885; DOI=10.2307/3871591;
RA Murata Y., Pei Z.-M., Mori I.C., Schroeder J.;
RT "Abscisic acid activation of plasma membrane Ca(2+) channels in guard cells
RT requires cytosolic NAD(P)H and is differentially disrupted upstream and
RT downstream of reactive oxygen species production in abi1-1 and abi2-1
RT protein phosphatase 2C mutants.";
RL Plant Cell 13:2513-2523(2001).
RN [38]
RP FUNCTION, AND INTERACTION WITH CIPK15/PKS3.
RX PubMed=12194854; DOI=10.1016/s1534-5807(02)00229-0;
RA Guo Y., Xiong L., Song C.-P., Gong D., Halfter U., Zhu J.-K.;
RT "A calcium sensor and its interacting protein kinase are global regulators
RT of abscisic acid signaling in Arabidopsis.";
RL Dev. Cell 3:233-244(2002).
RN [39]
RP FUNCTION, MUTAGENESIS OF ASP-177 AND GLY-180, AND INTERACTION WITH ATHB-6.
RX PubMed=12065416; DOI=10.1093/emboj/cdf316;
RA Himmelbach A., Hoffmann T., Leube M., Hoehener B., Grill E.;
RT "Homeodomain protein ATHB6 is a target of the protein phosphatase ABI1 and
RT regulates hormone responses in Arabidopsis.";
RL EMBO J. 21:3029-3038(2002).
RN [40]
RP FUNCTION.
RX PubMed=12432076; DOI=10.1242/jcs.00175;
RA Hoth S., Morgante M., Sanchez J.-P., Hanafey M.K., Tingey S.V., Chua N.-H.;
RT "Genome-wide gene expression profiling in Arabidopsis thaliana reveals new
RT targets of abscisic acid and largely impaired gene regulation in the abi1-1
RT mutant.";
RL J. Cell Sci. 115:4891-4900(2002).
RN [41]
RP FUNCTION.
RX PubMed=12047634; DOI=10.1046/j.1365-313x.2002.01322.x;
RA Merlot S., Mustilli A.-C., Genty B., North H., Lefebvre V., Sotta B.,
RA Vavasseur A., Giraudat J.;
RT "Use of infrared thermal imaging to isolate Arabidopsis mutants defective
RT in stomatal regulation.";
RL Plant J. 30:601-609(2002).
RN [42]
RP FUNCTION.
RX PubMed=12713537; DOI=10.1046/j.1365-313x.2003.01721.x;
RA Wu Y., Sanchez J.P., Lopez-Molina L., Himmelbach A., Grill E., Chua N.-H.;
RT "The abi1-1 mutation blocks ABA signaling downstream of cADPR action.";
RL Plant J. 34:307-315(2003).
RN [43]
RP FUNCTION.
RX PubMed=14576281; DOI=10.1104/pp.103.026294;
RA Stepansky A., Galili G.;
RT "Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate
RT reductase/saccharopine dehydrogenase enzyme of lysine catabolism is
RT concertedly regulated by metabolic and stress-associated signals.";
RL Plant Physiol. 133:1407-1415(2003).
RN [44]
RP FUNCTION.
RX PubMed=14596925; DOI=10.1016/s0014-5793(03)01118-9;
RA Becker D., Hoth S., Ache P., Wenkel S., Roelfsema M.R.G., Meyerhoff O.,
RA Hartung W., Hedrich R.;
RT "Regulation of the ABA-sensitive Arabidopsis potassium channel gene GORK in
RT response to water stress.";
RL FEBS Lett. 554:119-126(2003).
RN [45]
RP FUNCTION.
RX PubMed=12609042; DOI=10.1046/j.1365-313x.2003.01656.x;
RA Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M.,
RA Baker N.R.;
RT "Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and leaf
RT water status during excess light stress reveals a functional organisation
RT of Arabidopsis leaves.";
RL Plant J. 33:691-705(2003).
RN [46]
RP INDUCTION BY ABA.
RX PubMed=14731256; DOI=10.1046/j.1365-313x.2003.01966.x;
RA Saez A., Apostolova N., Gonzalez-Guzman M., Gonzalez-Garcia M.P.,
RA Nicolas C., Lorenzo O., Rodriguez P.L.;
RT "Gain-of-function and loss-of-function phenotypes of the protein
RT phosphatase 2C HAB1 reveal its role as a negative regulator of abscisic
RT acid signalling.";
RL Plant J. 37:354-369(2004).
RN [47]
RP FUNCTION.
RX PubMed=15144382; DOI=10.1111/j.1365-313x.2004.02086.x;
RA Chini A., Grant J.J., Seki M., Shinozaki K., Loake G.J.;
RT "Drought tolerance established by enhanced expression of the CC-NBS-LRR
RT gene, ADR1, requires salicylic acid, EDS1 and ABI1.";
RL Plant J. 38:810-822(2004).
RN [48]
RP FUNCTION, MUTAGENESIS OF 67-ARG-LYS-68 AND ARG-73, SUBCELLULAR LOCATION,
RP ACTIVITY REGULATION, AND INTERACTION WITH PA.
RX PubMed=15197253; DOI=10.1073/pnas.0402112101;
RA Zhang W., Qin C., Zhao J., Wang X.;
RT "Phospholipase D alpha 1-derived phosphatidic acid interacts with ABI1
RT phosphatase 2C and regulates abscisic acid signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9508-9513(2004).
RN [49]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15130549; DOI=10.1016/j.tplants.2004.03.007;
RA Schweighofer A., Hirt H., Meskiene I.;
RT "Plant PP2C phosphatases: emerging functions in stress signaling.";
RL Trends Plant Sci. 9:236-243(2004).
RN [50]
RP FUNCTION.
RX PubMed=15618419; DOI=10.1104/pp.104.053082;
RA Christmann A., Hoffmann T., Teplova I., Grill E., Mueller A.;
RT "Generation of active pools of abscisic acid revealed by in vivo imaging of
RT water-stressed Arabidopsis.";
RL Plant Physiol. 137:209-219(2005).
RN [51]
RP FUNCTION.
RX PubMed=15923322; DOI=10.1104/pp.105.062257;
RA Larkindale J., Hall J.D., Knight M.R., Vierling E.;
RT "Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling
RT pathways in the acquisition of thermotolerance.";
RL Plant Physiol. 138:882-897(2005).
RN [52]
RP FUNCTION, AND INTERACTION WITH SRK2E.
RX PubMed=16365038; DOI=10.1074/jbc.m509820200;
RA Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F.,
RA Shinozaki K.;
RT "The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and
RT integrates abscisic acid (ABA) and osmotic stress signals controlling
RT stomatal closure in Arabidopsis.";
RL J. Biol. Chem. 281:5310-5318(2006).
RN [53]
RP FUNCTION.
RX PubMed=16339784; DOI=10.1093/jxb/erj026;
RA Verslues P.E., Bray E.A.;
RT "Role of abscisic acid (ABA) and Arabidopsis thaliana ABA-insensitive loci
RT in low water potential-induced ABA and proline accumulation.";
RL J. Exp. Bot. 57:201-212(2006).
RN [54]
RP INTERACTION WITH GPX3, AND REPRESSION BY OXIDIZED GPX3.
RX PubMed=16998070; DOI=10.1105/tpc.106.044230;
RA Miao Y., Lv D., Wang P., Wang X.-C., Chen J., Miao C., Song C.-P.;
RT "An Arabidopsis glutathione peroxidase functions as both a redox transducer
RT and a scavenger in abscisic acid and drought stress responses.";
RL Plant Cell 18:2749-2766(2006).
RN [55]
RP FUNCTION, AND MUTAGENESIS OF ASP-177.
RX PubMed=16571665; DOI=10.1073/pnas.0501720103;
RA Yang Y., Sulpice R., Himmelbach A., Meinhard M., Christmann A., Grill E.;
RT "Fibrillin expression is regulated by abscisic acid response regulators and
RT is involved in abscisic acid-mediated photoprotection.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6061-6066(2006).
RN [56]
RP INDUCTION BY ABA, AND TISSUE SPECIFICITY.
RX PubMed=16339800; DOI=10.1104/pp.105.070128;
RA Yoshida T., Nishimura N., Kitahata N., Kuromori T., Ito T., Asami T.,
RA Shinozaki K., Hirayama T.;
RT "ABA-hypersensitive germination3 encodes a protein phosphatase 2C (AtPP2CA)
RT that strongly regulates abscisic acid signaling during germination among
RT Arabidopsis protein phosphatase 2Cs.";
RL Plant Physiol. 140:115-126(2006).
RN [57]
RP FUNCTION.
RX PubMed=16798945; DOI=10.1104/pp.106.081018;
RA Saez A., Robert N., Maktabi M.H., Schroeder J.I., Serrano R.,
RA Rodriguez P.L.;
RT "Enhancement of abscisic acid sensitivity and reduction of water
RT consumption in Arabidopsis by combined inactivation of the protein
RT phosphatases type 2C ABI1 and HAB1.";
RL Plant Physiol. 141:1389-1399(2006).
RN [58]
RP FUNCTION, INTERACTION WITH PA, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP ARG-73.
RX PubMed=16614222; DOI=10.1126/science.1123769;
RA Mishra G., Zhang W., Deng F., Zhao J., Wang X.;
RT "A bifurcating pathway directs abscisic acid effects on stomatal closure
RT and opening in Arabidopsis.";
RL Science 312:264-266(2006).
RN [59]
RP INTERACTION WITH SPK1; SCAR1; SCAR2; SCAR3 AND SCARL.
RX PubMed=17267444; DOI=10.1242/dev.02792;
RA Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M.,
RA Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.;
RT "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell
RT morphogenesis.";
RL Development 134:967-977(2007).
RN [60]
RP FUNCTION.
RX PubMed=17304219; DOI=10.1038/sj.emboj.7601575;
RA de Torres-Zabala M., Truman W., Bennett M.H., Lafforgue G., Mansfield J.W.,
RA Rodriguez Egea P., Boegre L., Grant M.;
RT "Pseudomonas syringae pv. tomato hijacks the Arabidopsis abscisic acid
RT signalling pathway to cause disease.";
RL EMBO J. 26:1434-1443(2007).
RN [61]
RP FUNCTION, AND INDUCTION BY ETHYLENE.
RX PubMed=17158582; DOI=10.1104/pp.106.092700;
RA Benschop J.J., Millenaar F.F., Smeets M.E., van Zanten M.,
RA Voesenek L.A.C.J., Peeters A.J.M.;
RT "Abscisic acid antagonizes ethylene-induced hyponastic growth in
RT Arabidopsis.";
RL Plant Physiol. 143:1013-1023(2007).
RN [62]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT Arabidopsis.";
RL BMC Genomics 9:550-550(2008).
RN [63]
RP FUNCTION, MUTAGENESIS OF ASP-177; GLY-180 AND 425-ARG--LYS-427, NUCLEAR
RP LOCALIZATION SIGNAL, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18298671; DOI=10.1111/j.1365-313x.2008.03454.x;
RA Moes D., Himmelbach A., Korte A., Haberer G., Grill E.;
RT "Nuclear localization of the mutant protein phosphatase abi1 is required
RT for insensitivity towards ABA responses in Arabidopsis.";
RL Plant J. 54:806-819(2008).
RN [64]
RP INDUCTION BY MYB44 AND SALT.
RX PubMed=18162593; DOI=10.1104/pp.107.110981;
RA Jung C., Seo J.S., Han S.W., Koo Y.J., Kim C.H., Song S.I., Nahm B.H.,
RA Choi Y.D., Cheong J.-J.;
RT "Overexpression of AtMYB44 enhances stomatal closure to confer abiotic
RT stress tolerance in transgenic Arabidopsis.";
RL Plant Physiol. 146:623-635(2008).
RN [65]
RP FUNCTION, AND INTERACTION WITH SRK2E/OST1.
RX PubMed=19955405; DOI=10.1073/pnas.0912021106;
RA Geiger D., Scherzer S., Mumm P., Stange A., Marten I., Bauer H., Ache P.,
RA Matschi S., Liese A., Al-Rasheid K.A.S., Romeis T., Hedrich R.;
RT "Activity of guard cell anion channel SLAC1 is controlled by drought-stress
RT signaling kinase-phosphatase pair.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21425-21430(2009).
RN [66]
RP INTERACTION WITH PYL9/RCAR1.
RX PubMed=19407143; DOI=10.1126/science.1172408;
RA Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A.,
RA Grill E.;
RT "Regulators of PP2C phosphatase activity function as abscisic acid
RT sensors.";
RL Science 324:1064-1068(2009).
RN [67]
RP INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, MUTAGENESIS OF GLY-180,
RP AND ACTIVITY REGULATION.
RX PubMed=19407142; DOI=10.1126/science.1173041;
RA Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y.,
RA Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D.,
RA Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P.,
RA Zhu J.-K., Schroeder J.I., Volkman B.F., Cutler S.R.;
RT "Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family
RT of START proteins.";
RL Science 324:1068-1071(2009).
RN [68]
RP INTERACTION WITH PYR1.
RX PubMed=19933100; DOI=10.1126/science.1181829;
RA Nishimura N., Hitomi K., Arvai A.S., Rambo R.P., Hitomi C., Cutler S.R.,
RA Schroeder J.I., Getzoff E.D.;
RT "Structural mechanism of abscisic acid binding and signaling by dimeric
RT PYR1.";
RL Science 326:1373-1379(2009).
RN [69]
RP INTERACTION WITH PYL8/RCAR3, AND ACTIVITY REGULATION BY PYR/PYL/RCAR.
RX PubMed=19769575; DOI=10.1111/j.1365-313x.2009.04025.x;
RA Szostkiewicz I., Richter K., Kepka M., Demmel S., Ma Y., Korte A.,
RA Assaad F.F., Christmann A., Grill E.;
RT "Closely related receptor complexes differ in their ABA selectivity and
RT sensitivity.";
RL Plant J. 61:25-35(2010).
RN [70]
RP INTERACTION WITH RPL12B; PYR1; PYL1; PYL4; PYL5; PYL6; PYL7; PYL8; PYL9;
RP PYL10; SRK2E/OST1; SRK2D/SNRK2-2 AND SRK2I/SNRK2-3.
RX PubMed=19874541; DOI=10.1111/j.1365-313x.2009.04054.x;
RA Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C.,
RA Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.;
RT "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-
RT interacting proteins in Arabidopsis.";
RL Plant J. 61:290-299(2010).
RN [71]
RP INTERACTION WITH CPK21 AND CPK23.
RX PubMed=20385816; DOI=10.1073/pnas.0912030107;
RA Geiger D., Scherzer S., Mumm P., Marten I., Ache P., Matschi S., Liese A.,
RA Wellmann C., Al-Rasheid K.A.S., Grill E., Romeis T., Hedrich R.;
RT "Guard cell anion channel SLAC1 is regulated by CDPK protein kinases with
RT distinct Ca2+ affinities.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8023-8028(2010).
RN [72]
RP INTERACTION WITH PYL10.
RX PubMed=21658606; DOI=10.1016/j.molcel.2011.05.011;
RA Hao Q., Yin P., Li W., Wang L., Yan C., Lin Z., Wu J.Z., Wang J., Yan S.F.,
RA Yan N.;
RT "The molecular basis of ABA-independent inhibition of PP2Cs by a subclass
RT of PYL proteins.";
RL Mol. Cell 42:662-672(2011).
RN [73]
RP INTERACTION WITH PYL13.
RX PubMed=24165892; DOI=10.1038/cr.2013.143;
RA Li W., Wang L., Sheng X., Yan C., Zhou R., Hang J., Yin P., Yan N.;
RT "Molecular basis for the selective and ABA-independent inhibition of PP2CA
RT by PYL13.";
RL Cell Res. 23:1369-1379(2013).
RN [74]
RP INTERACTION WITH KIN10, AND FUNCTION.
RX PubMed=24179127; DOI=10.1105/tpc.113.114066;
RA Rodrigues A., Adamo M., Crozet P., Margalha L., Confraria A., Martinho C.,
RA Elias A., Rabissi A., Lumbreras V., Gonzalez-Guzman M., Antoni R.,
RA Rodriguez P.L., Baena-Gonzalez E.;
RT "ABI1 and PP2CA phosphatases are negative regulators of Snf1-related
RT protein kinase1 signaling in Arabidopsis.";
RL Plant Cell 25:3871-3884(2013).
RN [75]
RP FUNCTION, INTERACTION WITH MAPKKK18, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26443375; DOI=10.1093/pcp/pcv146;
RA Mitula F., Tajdel M., Ciesla A., Kasprowicz-Maluski A., Kulik A.,
RA Babula-Skowronska D., Michalak M., Dobrowolska G., Sadowski J.,
RA Ludwikow A.;
RT "Arabidopsis ABA-activated kinase MAPKKK18 is regulated by protein
RT phosphatase 2C ABI1 and the ubiquitin-proteasome pathway.";
RL Plant Cell Physiol. 56:2351-2367(2015).
RN [76]
RP INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=25680457; DOI=10.1007/s11103-015-0295-0;
RA Matsuoka D., Yasufuku T., Furuya T., Nanmori T.;
RT "An abscisic acid inducible Arabidopsis MAPKKK, MAPKKK18 regulates leaf
RT senescence via its kinase activity.";
RL Plant Mol. Biol. 87:565-575(2015).
RN [77]
RP FUNCTION.
RX PubMed=27913741; DOI=10.1104/pp.16.01386;
RA Li K., Yang F., Zhang G., Song S., Li Y., Ren D., Miao Y., Song C.-P.;
RT "AIK1, a mitogen-activated protein kinase, modulates abscisic acid
RT responses through the MKK5-MPK6 kinase cascade.";
RL Plant Physiol. 173:1391-1408(2017).
RN [78]
RP INTERACTION WITH PYL8/RCAR3.
RX PubMed=29928509; DOI=10.1038/s41421-018-0029-y;
RA Zhang L., Li X., Li D., Sun Y., Li Y., Luo Q., Liu Z., Wang J., Li X.,
RA Zhang H., Lou Z., Yang Y.;
RT "CARK1 mediates ABA signaling by phosphorylation of ABA receptors.";
RL Cell Discov. 4:30-30(2018).
RN [79]
RP REVIEW ON MITOGEN-ACTIVATED PROTEIN KINASE CASCADES.
RX PubMed=30349547; DOI=10.3389/fpls.2018.01387;
RA Jagodzik P., Tajdel-Zielinska M., Ciesla A., Marczak M., Ludwikow A.;
RT "Mitogen-activated protein kinase cascades in plant hormone signaling.";
RL Front. Plant Sci. 9:1387-1387(2018).
RN [80]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 119-434 IN COMPLEX WITH
RP MANGANESE; ABA AND PYL1, AND INTERACTION WITH PYL2.
RX PubMed=19893533; DOI=10.1038/nsmb.1730;
RA Yin P., Fan H., Hao Q., Yuan X., Wu D., Pang Y., Yan C., Li W., Wang J.,
RA Yan N.;
RT "Structural insights into the mechanism of abscisic acid signaling by PYL
RT proteins.";
RL Nat. Struct. Mol. Biol. 16:1230-1236(2009).
RN [81]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 125-429 IN COMPLEX WITH ABSCISIC
RP ACID AND PYL1, MUTAGENESIS OF GLU-142; THR-239; ILE-298; TRP-300; ARG-304;
RP PHE-306; VAL-308 AND TYR-319, AND INTERACTION WITH PYL1.
RX PubMed=19855379; DOI=10.1038/nature08583;
RA Miyazono K.-I., Miyakawa T., Sawano Y., Kubota K., Kang H.-J., Asano A.,
RA Miyauchi Y., Takahashi M., Zhi Y., Fujita Y., Yoshida T., Kodaira K.-S.,
RA Yamaguchi-Shinozaki K., Tanokura M.;
RT "Structural basis of abscisic acid signalling.";
RL Nature 462:609-614(2009).
RN [82]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 117-434 IN COMPLEX WITH
RP MAGNESIUM.
RX PubMed=20729862; DOI=10.1038/nsmb.1887;
RA Melcher K., Xu Y., Ng L.-M., Zhou X.E., Soon F.-F., Chinnusamy V.,
RA Suino-Powell K.M., Kovach A., Tham F.S., Cutler S.R., Li J., Yong E.-L.,
RA Zhu J.-K., Xu H.E.;
RT "Identification and mechanism of ABA receptor antagonism.";
RL Nat. Struct. Mol. Biol. 17:1102-1108(2010).
CC -!- FUNCTION: Key component and repressor of the abscisic acid (ABA)
CC signaling pathway that regulates numerous ABA responses, such as
CC stomatal closure, osmotic water permeability of the plasma membrane
CC (Pos), drought-induced resistance and rhizogenesis, response to
CC glucose, high light stress, seed germination and inhibition of
CC vegetative growth. During the stomatal closure regulation, modulates
CC the inward calcium-channel permeability as well as the actin
CC reorganization in guard cells in response to ABA. Involved in the
CC resistance to the bacterial pathogen Pseudomonas syringae pv. tomato.
CC Controls negatively fibrillin expression that is involved in mediating
CC ABA-induced photoprotection. May be involved in ABA content regulation.
CC Plays a role in the Pro accumulation in response to reduced water
CC availability (low water potential). Required for the ABA negative
CC regulation of the ethylene-induced hyponastic growth. Involved in
CC acquired thermotolerance of root growth and seedling survival.
CC Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli,
CC especially in stomata closure regulation involving SLAC1. Represses
CC MAPKKK18 activity and promotes MAPKKK18 degradation by the proteasome
CC pathway upon abscisic acid (ABA) treatment (PubMed:26443375). Represses
CC KIN10 activity by the specific dephosphorylation of its T-loop Thr-198,
CC leading to a poststress inactivation of SnRK1 signaling
CC (PubMed:24179127). Restricts MAPKKK20 activity by dephosphorylation
CC (PubMed:27913741). {ECO:0000269|PubMed:10488243,
CC ECO:0000269|PubMed:10521520, ECO:0000269|PubMed:10645425,
CC ECO:0000269|PubMed:10872217, ECO:0000269|PubMed:10950871,
CC ECO:0000269|PubMed:11208021, ECO:0000269|PubMed:11289613,
CC ECO:0000269|PubMed:11587514, ECO:0000269|PubMed:11701885,
CC ECO:0000269|PubMed:11707572, ECO:0000269|PubMed:12047634,
CC ECO:0000269|PubMed:12065416, ECO:0000269|PubMed:12194854,
CC ECO:0000269|PubMed:12228349, ECO:0000269|PubMed:12232124,
CC ECO:0000269|PubMed:12232276, ECO:0000269|PubMed:12432076,
CC ECO:0000269|PubMed:12609042, ECO:0000269|PubMed:12713537,
CC ECO:0000269|PubMed:14576281, ECO:0000269|PubMed:14596925,
CC ECO:0000269|PubMed:15144382, ECO:0000269|PubMed:15197253,
CC ECO:0000269|PubMed:15618419, ECO:0000269|PubMed:15923322,
CC ECO:0000269|PubMed:16339784, ECO:0000269|PubMed:16365038,
CC ECO:0000269|PubMed:16571665, ECO:0000269|PubMed:16614222,
CC ECO:0000269|PubMed:16652949, ECO:0000269|PubMed:16798945,
CC ECO:0000269|PubMed:17158582, ECO:0000269|PubMed:17304219,
CC ECO:0000269|PubMed:18298671, ECO:0000269|PubMed:1834244,
CC ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:24179127,
CC ECO:0000269|PubMed:26443375, ECO:0000269|PubMed:27913741,
CC ECO:0000269|PubMed:7568166, ECO:0000269|PubMed:8492808,
CC ECO:0000269|PubMed:8771791, ECO:0000269|PubMed:8898906,
CC ECO:0000269|PubMed:9090884, ECO:0000269|PubMed:9108297,
CC ECO:0000269|PubMed:9161030, ECO:0000269|PubMed:9165752,
CC ECO:0000269|PubMed:9263461, ECO:0000269|PubMed:9276963,
CC ECO:0000269|PubMed:9351242, ECO:0000269|PubMed:9448270,
CC ECO:0000269|Ref.8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:10645425, ECO:0000269|PubMed:8898906,
CC ECO:0000269|PubMed:9537523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:10645425, ECO:0000269|PubMed:8898906,
CC ECO:0000269|PubMed:9537523};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:8898906,
CC ECO:0000269|PubMed:9537523};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19893533, ECO:0000269|PubMed:8898906,
CC ECO:0000269|PubMed:9537523};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000269|PubMed:19893533, ECO:0000269|PubMed:20729862,
CC ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9537523};
CC -!- ACTIVITY REGULATION: Phosphatase activity repressed by oxidized GPX3
CC and phosphatidic acid (PA). PA is produced by PLD alpha 1 in response
CC to ABA. Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent
CC manner. {ECO:0000269|PubMed:15197253, ECO:0000269|PubMed:16614222,
CC ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19769575}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:9537523};
CC -!- SUBUNIT: Interacts with SPK1, ATHB-6, CIPK15/PKS3, GPX3, SRK2E/OST1,
CC SRK2D, SRK2I, SCAR1, SCAR2, SCAR3 and SCARL. Binds to the PA released
CC by the phospholipase D alpha 1 (PLDALPHA1) in response to ABA during
CC the stomatal closure regulation. Interacts with ABA-bounded PYR1, PYL1,
CC PYL2, PYL3, PYL4, PYL5, PYL6, PYL7, PYL8, PYL9, PYL10, and with free
CC PYL2, PYL3, PYL4 and PYL13. Binds to RPL12B, CPK21 and CPK23. Binds to
CC MAPKKK18 (PubMed:26443375). Interacts with KIN10 (PubMed:24179127).
CC Interacts with phosphorylated PYL8/RCAR3 (PubMed:29928509).
CC {ECO:0000269|PubMed:12065416, ECO:0000269|PubMed:12194854,
CC ECO:0000269|PubMed:15197253, ECO:0000269|PubMed:16365038,
CC ECO:0000269|PubMed:16614222, ECO:0000269|PubMed:16998070,
CC ECO:0000269|PubMed:17267444, ECO:0000269|PubMed:19407142,
CC ECO:0000269|PubMed:19407143, ECO:0000269|PubMed:19769575,
CC ECO:0000269|PubMed:19855379, ECO:0000269|PubMed:19874541,
CC ECO:0000269|PubMed:19893533, ECO:0000269|PubMed:19933100,
CC ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:20385816,
CC ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:24165892,
CC ECO:0000269|PubMed:24179127, ECO:0000269|PubMed:26443375,
CC ECO:0000269|PubMed:29928509}.
CC -!- INTERACTION:
CC P49597; Q8VZS8: PYL1; NbExp=13; IntAct=EBI-782526, EBI-2363104;
CC P49597; Q8H1R0: PYL10; NbExp=7; IntAct=EBI-782526, EBI-2363213;
CC P49597; Q9FJ50: PYL11; NbExp=3; IntAct=EBI-782526, EBI-2363233;
CC P49597; Q9FJ49: PYL12; NbExp=3; IntAct=EBI-782526, EBI-2363244;
CC P49597; Q9SN51: PYL13; NbExp=3; IntAct=EBI-782526, EBI-25515027;
CC P49597; O80992: PYL2; NbExp=6; IntAct=EBI-782526, EBI-2363125;
CC P49597; Q9SSM7: PYL3; NbExp=5; IntAct=EBI-782526, EBI-2363144;
CC P49597; O80920: PYL4; NbExp=9; IntAct=EBI-782526, EBI-2349683;
CC P49597; Q9FLB1: PYL5; NbExp=12; IntAct=EBI-782526, EBI-2363181;
CC P49597; Q8S8E3: PYL6; NbExp=9; IntAct=EBI-782526, EBI-2363192;
CC P49597; Q1ECF1: PYL7; NbExp=5; IntAct=EBI-782526, EBI-2363203;
CC P49597; Q9FGM1: PYL8; NbExp=7; IntAct=EBI-782526, EBI-2429535;
CC P49597; Q84MC7: PYL9; NbExp=14; IntAct=EBI-782526, EBI-2349513;
CC P49597; O49686: PYR1; NbExp=12; IntAct=EBI-782526, EBI-2349590;
CC P49597; Q93ZY2: ROPGEF1; NbExp=4; IntAct=EBI-782526, EBI-4425188;
CC P49597; Q39192: SRK2D; NbExp=7; IntAct=EBI-782526, EBI-2363308;
CC P49597; Q940H6: SRK2E; NbExp=15; IntAct=EBI-782526, EBI-782514;
CC P49597; Q39193: SRK2I; NbExp=8; IntAct=EBI-782526, EBI-2620383;
CC P49597; Q9LMA8: TIFY10A; NbExp=3; IntAct=EBI-782526, EBI-1388539;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell membrane; Peripheral
CC membrane protein. Note=Associated to the plasma membrane when in
CC complex with PA, subsequently to ABA signaling.
CC -!- TISSUE SPECIFICITY: Expressed in seeds and seedlings. In roots,
CC confined to lateral root caps and columella cells.
CC {ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:18298671}.
CC -!- INDUCTION: Repressed by MYB44. Induced by low temperature, drought,
CC high salt, abscisic acid (ABA) and ethylene.
CC {ECO:0000269|PubMed:11439132, ECO:0000269|PubMed:14731256,
CC ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:16998070,
CC ECO:0000269|PubMed:17158582, ECO:0000269|PubMed:18162593}.
CC -!- DOMAIN: The 'lock' site stabilizes the complex made of PP2C, ABA and
CC PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch' loops in
CC closed positions. {ECO:0000250|UniProtKB:Q9CAJ0}.
CC -!- DISRUPTION PHENOTYPE: In abi1td, enhanced induction of MKKK18 activity
CC after 90 minutes of abscisic acid (ABA) treatment and reduced
CC degradation of MKKK18 by the proteasome. {ECO:0000269|PubMed:26443375}.
CC -!- MISCELLANEOUS: Enhanced ABA signaling repressor activity by the
CC proteasomal inhibitor MG132 accompanied by a cytoplasmic localization.
CC -!- MISCELLANEOUS: Plants insensitive to ABA (abi1-1) are more resistant to
CC P.syringae.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; U12856; AAA50237.1; -; mRNA.
DR EMBL; X77116; CAA54383.1; -; mRNA.
DR EMBL; X78886; CAA55484.1; -; Genomic_DNA.
DR EMBL; AL049483; CAB39673.1; -; Genomic_DNA.
DR EMBL; AL161564; CAB79463.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85155.1; -; Genomic_DNA.
DR EMBL; AY035073; AAK59578.1; -; mRNA.
DR EMBL; AY142623; AAN13081.1; -; mRNA.
DR EMBL; AK226529; BAE98668.1; -; mRNA.
DR PIR; T04263; T04263.
DR RefSeq; NP_194338.1; NM_118741.3.
DR PDB; 3JRQ; X-ray; 2.10 A; A=125-429.
DR PDB; 3KDJ; X-ray; 1.88 A; B=119-434.
DR PDB; 3NMN; X-ray; 2.15 A; B/D=117-434.
DR PDBsum; 3JRQ; -.
DR PDBsum; 3KDJ; -.
DR PDBsum; 3NMN; -.
DR AlphaFoldDB; P49597; -.
DR SMR; P49597; -.
DR BioGRID; 14001; 65.
DR DIP; DIP-36706N; -.
DR IntAct; P49597; 34.
DR MINT; P49597; -.
DR STRING; 3702.AT4G26080.1; -.
DR iPTMnet; P49597; -.
DR PaxDb; P49597; -.
DR PRIDE; P49597; -.
DR ProteomicsDB; 248804; -.
DR EnsemblPlants; AT4G26080.1; AT4G26080.1; AT4G26080.
DR GeneID; 828714; -.
DR Gramene; AT4G26080.1; AT4G26080.1; AT4G26080.
DR KEGG; ath:AT4G26080; -.
DR Araport; AT4G26080; -.
DR TAIR; locus:2005488; AT4G26080.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_4_1; -.
DR InParanoid; P49597; -.
DR OMA; VICPTHI; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; P49597; -.
DR BRENDA; 3.1.3.16; 399.
DR EvolutionaryTrace; P49597; -.
DR PRO; PR:P49597; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P49597; baseline and differential.
DR Genevisible; P49597; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:CACAO.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:CACAO.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Cell membrane; Cytoplasm;
KW Hydrolase; Magnesium; Manganese; Membrane; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..434
FT /note="Protein phosphatase 2C 56"
FT /id="PRO_0000057766"
FT DOMAIN 128..422
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT MOTIF 423..427
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:18298671"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3NMN"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3NMN"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3NMN"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3NMN"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3NMN"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3NMN"
FT BINDING 413
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3NMN"
FT SITE 300
FT /note="Lock"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT MUTAGEN 67..68
FT /note="RK->GA: Normal binding with PA, no reduction of
FT phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15197253"
FT MUTAGEN 73
FT /note="R->A: Loss of binding with PA, no reduction of
FT phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15197253,
FT ECO:0000269|PubMed:16614222"
FT MUTAGEN 93
FT /note="D->A: No phenotype."
FT /evidence="ECO:0000269|PubMed:9448270"
FT MUTAGEN 141..143
FT /note="MED->IHG: Reduced inhibition of the ABA signaling
FT pathway and loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:9448270"
FT MUTAGEN 142
FT /note="E->A: Reduced binding affinity for PYL1, and
FT impaired phosphatase activity."
FT /evidence="ECO:0000269|PubMed:19855379"
FT MUTAGEN 174
FT /note="G->D: No inhibition of the ABA signaling pathway and
FT loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:9448270"
FT MUTAGEN 177..179
FT /note="DGH->KLN: No inhibition of the ABA signaling pathway
FT and loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:9448270"
FT MUTAGEN 177
FT /note="D->A: Loss of phosphatase activity, impaired
FT negative regulation of the ABA signaling pathway, reduced
FT interaction with ATHB-6, and reduced negative control on
FT fibrillin expression."
FT /evidence="ECO:0000269|PubMed:12065416,
FT ECO:0000269|PubMed:16571665, ECO:0000269|PubMed:18298671"
FT MUTAGEN 180
FT /note="G->D: In abi1; wilty phenotype, reduced phosphatase
FT activity, ABA-insensitive seed germination and growth,
FT impaired ABA-mediated binding to PYR1, and reduced
FT interaction with ATHB-6. Increased sensitivity to ABA and
FT loss of phosphatase activity; when associated with T-185,
FT or Y-259, or C-304, or D-307, or F-314, or L-328, or N-316.
FT No inhibition of the ABA signaling pathway and loss of
FT phosphatase activity; when associated with D-174."
FT /evidence="ECO:0000269|PubMed:10521520,
FT ECO:0000269|PubMed:12065416, ECO:0000269|PubMed:18298671,
FT ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:8197457,
FT ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9448270,
FT ECO:0000269|PubMed:9537523"
FT MUTAGEN 185
FT /note="A->T: Increased sensitivity to ABA and loss of
FT phosphatase activity; when associated with D-180."
FT /evidence="ECO:0000269|PubMed:10521520"
FT MUTAGEN 239
FT /note="T->A: Normal affinity for PYL1."
FT /evidence="ECO:0000269|PubMed:19855379"
FT MUTAGEN 259
FT /note="C->Y: Increased sensitivity to ABA and loss of
FT phosphatase activity; when associated with D-180."
FT /evidence="ECO:0000269|PubMed:10521520"
FT MUTAGEN 298
FT /note="I->A: Loss of affinity for PYL1."
FT /evidence="ECO:0000269|PubMed:19855379"
FT MUTAGEN 300
FT /note="W->A: Loss of affinity for PYL1."
FT /evidence="ECO:0000269|PubMed:19855379"
FT MUTAGEN 304
FT /note="R->A: Loss of affinity for PYL1."
FT /evidence="ECO:0000269|PubMed:10521520,
FT ECO:0000269|PubMed:19855379"
FT MUTAGEN 304
FT /note="R->C: Increased sensitivity to ABA and loss of
FT phosphatase activity; when associated with D-180."
FT /evidence="ECO:0000269|PubMed:10521520,
FT ECO:0000269|PubMed:19855379"
FT MUTAGEN 306
FT /note="F->A: Reduced affinity for PYL1."
FT /evidence="ECO:0000269|PubMed:19855379"
FT MUTAGEN 307
FT /note="G->D: Increased sensitivity to ABA and loss of
FT phosphatase activity; when associated with D-180."
FT /evidence="ECO:0000269|PubMed:10521520"
FT MUTAGEN 308
FT /note="V->A: Reduced affinity for PYL1."
FT /evidence="ECO:0000269|PubMed:19855379"
FT MUTAGEN 314
FT /note="S->F: Increased sensitivity to ABA and loss of
FT phosphatase activity; when associated with D-180."
FT /evidence="ECO:0000269|PubMed:10521520"
FT MUTAGEN 319
FT /note="Y->A: Reduced affinity for PYL1."
FT /evidence="ECO:0000269|PubMed:19855379"
FT MUTAGEN 328
FT /note="P->L: Increased sensitivity to ABA and loss of
FT phosphatase activity; when associated with D-180."
FT /evidence="ECO:0000269|PubMed:10521520"
FT MUTAGEN 416
FT /note="S->N: Increased sensitivity to ABA and loss of
FT phosphatase activity; when associated with D-180."
FT /evidence="ECO:0000269|PubMed:10521520"
FT MUTAGEN 425..427
FT /note="RRK->QNN: Cytoplasmic subcellular localization, and
FT loss of negative regulation of the ABA signaling pathway."
FT /evidence="ECO:0000269|PubMed:18298671"
FT CONFLICT 24
FT /note="G -> R (in Ref. 6; AAK59578)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="I -> V (in Ref. 3; CAA55484)"
FT /evidence="ECO:0000305"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3KDJ"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:3JRQ"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 171..182
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 183..203
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 211..231
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:3KDJ"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:3KDJ"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 355..369
FT /evidence="ECO:0007829|PDB:3KDJ"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:3KDJ"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:3KDJ"
SQ 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
