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 27-MAR-2024, entry version 207. 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=10.1105/tpc.9.3.409; 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=10.1105/tpc.9.5.759; 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=10.1046/j.1365-313x.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=10.1105/tpc.11.9.1785; 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=10.1105/tpc.11.10.1897; 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=10.1105/tpc.010210; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.P49597; -. DR iPTMnet; P49597; -. DR PaxDb; 3702-AT4G26080-1; -. 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; AT4G26080; ABI1. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_20_4_1; -. DR InParanoid; P49597; -. DR OMA; FFDIPLW; -. DR OrthoDB; 216736at2759; -. 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 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: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; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR47992:SF179; PROTEIN PHOSPHATASE 2C 56; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; P49597; AT. 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 //