P2C77_ARATH
ID P2C77_ARATH Reviewed; 423 AA.
AC O04719; B3H561;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Protein phosphatase 2C 77 {ECO:0000303|PubMed:19021904};
DE Short=AtPP2C77 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000269|PubMed:11882947};
DE AltName: Full=Protein ABSCISIC ACID-INSENSITIVE 2 {ECO:0000303|PubMed:9165752};
DE AltName: Full=Protein phosphatase 2C ABI2 {ECO:0000303|PubMed:9165752};
DE Short=PP2C ABI2 {ECO:0000303|PubMed:9165752};
GN Name=ABI2 {ECO:0000303|PubMed:9165752};
GN Synonyms=PP2C77 {ECO:0000303|PubMed:19021904};
GN OrderedLocusNames=At5g57050 {ECO:0000312|Araport:AT5G57050};
GN ORFNames=MHM17.19 {ECO:0000312|EMBL:BAA97035.1};
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 [GENOMIC DNA / MRNA], FUNCTION, AND MUTAGENESIS OF
RP GLY-168.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9468303; DOI=10.1016/s0014-5793(97)01558-5;
RA Rodriguez P.L., Benning G., Grill E.;
RT "ABI2, a second protein phosphatase 2C involved in abscisic acid signal
RT transduction in Arabidopsis.";
RL FEBS Lett. 421:185-190(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=8787023; DOI=10.1104/pp.111.2.381;
RA de Bruxelles G.L., Peacock W.J., Dennis E.S., Dolferus R.;
RT "Abscisic acid induces the alcohol dehydrogenase gene in Arabidopsis.";
RL Plant Physiol. 111:381-391(1996).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC
RP ACTIVITY.
RX PubMed=11882947; DOI=10.1007/s00425-001-0675-3;
RA Meinhard M., Rodriguez P.L., Grill E.;
RT "The sensitivity of ABI2 to hydrogen peroxide links the abscisic acid-
RT response regulator to redox signalling.";
RL Planta 214:775-782(2002).
RN [19]
RP FUNCTION.
RX PubMed=12447533; DOI=10.1007/s00425-002-0840-3;
RA Takahashi N., Goto N., Okada K., Takahashi H.;
RT "Hydrotropism in abscisic acid, wavy, and gravitropic mutants of
RT Arabidopsis thaliana.";
RL Planta 216:203-211(2002).
RN [20]
RP FUNCTION.
RX PubMed=12119381; DOI=10.1105/tpc.010448;
RA Allen G.J., Murata Y., Chu S.P., Nafisi M., Schroeder J.I.;
RT "Hypersensitivity of abscisic acid-induced cytosolic calcium increases in
RT the Arabidopsis farnesyltransferase mutant era1-2.";
RL Plant Cell 14:1649-1662(2002).
RN [21]
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 [22]
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 [23]
RP INTERACTION WITH CIPK24/SOS2.
RX PubMed=14504388; DOI=10.1073/pnas.2034853100;
RA Ohta M., Guo Y., Halfter U., Zhu J.-K.;
RT "A novel domain in the protein kinase SOS2 mediates interaction with the
RT protein phosphatase 2C ABI2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11771-11776(2003).
RN [24]
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 [25]
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 [26]
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 [27]
RP FUNCTION.
RX PubMed=15599761; DOI=10.1007/s00425-004-1444-x;
RA Dong H.-P., Yu H., Bao Z., Guo X., Peng J., Yao Z., Chen G., Qu S.,
RA Dong H.;
RT "The ABI2-dependent abscisic acid signalling controls HrpN-induced drought
RT tolerance in Arabidopsis.";
RL Planta 221:313-327(2005).
RN [28]
RP INDUCTION BY ERF4.
RX PubMed=16021341; DOI=10.1007/s11103-005-7294-5;
RA Yang Z., Tian L., Latoszek-Green M., Brown D., Wu K.;
RT "Arabidopsis ERF4 is a transcriptional repressor capable of modulating
RT ethylene and abscisic acid responses.";
RL Plant Mol. Biol. 58:585-596(2005).
RN [29]
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 [30]
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 [31]
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 [32]
RP FUNCTION, MUTAGENESIS OF GLY-168, AND INTERACTION WITH THE FIBRILLIN
RP PRECURSOR PROTEIN.
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 [33]
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 [34]
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 [35]
RP FUNCTION.
RX PubMed=18278579; DOI=10.1007/s11103-008-9308-6;
RA Dekkers B.J.W., Schuurmans J.A.M.J., Smeekens S.C.M.;
RT "Interaction between sugar and abscisic acid signalling during early
RT seedling development in Arabidopsis.";
RL Plant Mol. Biol. 67:151-167(2008).
RN [36]
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 [37]
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 [38]
RP INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF GLY-168.
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 [39]
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 [40]
RP FUNCTION, AND INTERACTION WITH GHR1 AND SRK2E/OST1.
RX PubMed=22730405; DOI=10.1105/tpc.112.100107;
RA Hua D., Wang C., He J., Liao H., Duan Y., Zhu Z., Guo Y., Chen Z., Gong Z.;
RT "A plasma membrane receptor kinase, GHR1, mediates abscisic acid- and
RT hydrogen peroxide-regulated stomatal movement in Arabidopsis.";
RL Plant Cell 24:2546-2561(2012).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 101-423 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).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 101-423 IN COMPLEX WITH
RP MAGNESIUM, AND DISULFIDE BONDS.
RX PubMed=22116026; DOI=10.1126/science.1215106;
RA Soon F.F., Ng L.M., Zhou X.E., West G.M., Kovach A., Tan M.H.,
RA Suino-Powell K.M., He Y., Xu Y., Chalmers M.J., Brunzelle J.S., Zhang H.,
RA Yang H., Jiang H., Li J., Yong E.L., Cutler S., Zhu J.K., Griffin P.R.,
RA Melcher K., Xu H.E.;
RT "Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C
RT phosphatases.";
RL Science 335:85-88(2012).
CC -!- FUNCTION: Repressor of the abscisic acid (ABA) signaling pathway that
CC regulates numerous ABA responses, such as stomatal closure, osmotic
CC water permeability of the plasma membrane (Pos), high light stress,
CC response to glucose, seed germination and inhibition of vegetative
CC growth. During the stomatal closure regulation, modulates the inward
CC calcium-channel permeability as well as H(2)O(2) and oxidative burst in
CC response to ABA and dehydration. Represses GHR1 and, to some extent,
CC SRK2E/OST1, kinases involved in the regulation of SLAC1-dependent
CC stomatal closure (PubMed:22730405). Controls negatively fibrillin that
CC is involved in mediating ABA-induced photoprotection. May be implicated
CC in ABA content regulation. Involved in acquired thermotolerance of root
CC growth and seedling survival. Required for the Erwinia amylovora
CC harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic
CC response. {ECO:0000269|PubMed:10488243, ECO:0000269|PubMed:10872217,
CC ECO:0000269|PubMed:10950871, ECO:0000269|PubMed:11208021,
CC ECO:0000269|PubMed:11701885, ECO:0000269|PubMed:11707572,
CC ECO:0000269|PubMed:12119381, ECO:0000269|PubMed:12194854,
CC ECO:0000269|PubMed:12232276, ECO:0000269|PubMed:12447533,
CC ECO:0000269|PubMed:12609042, ECO:0000269|PubMed:14576281,
CC ECO:0000269|PubMed:14596925, ECO:0000269|PubMed:15599761,
CC ECO:0000269|PubMed:15923322, ECO:0000269|PubMed:16339784,
CC ECO:0000269|PubMed:16571665, ECO:0000269|PubMed:18278579,
CC ECO:0000269|PubMed:22730405, ECO:0000269|PubMed:8787023,
CC ECO:0000269|PubMed:9090884, ECO:0000269|PubMed:9108297,
CC ECO:0000269|PubMed:9165752, ECO:0000269|PubMed:9276963}.
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:11882947};
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:11882947};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11882947, ECO:0000269|PubMed:20729862,
CC ECO:0000269|PubMed:22116026};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11882947};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000269|PubMed:11882947, ECO:0000269|PubMed:20729862,
CC ECO:0000269|PubMed:22116026};
CC -!- ACTIVITY REGULATION: Phosphatase activity repressed by oxidized ATGPX3,
CC free fatty acids (e.g. arachidonic acid (20:4) and Linolenic acid
CC (18:3)) and by H(2)O(2). Repressed by PYR/PYL/RCAR ABA receptors in an
CC ABA-dependent manner. {ECO:0000269|PubMed:11882947,
CC ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19769575}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:11882947};
CC -!- SUBUNIT: Interacts with SPK1, CIPK15/PKS3, GPX3, SCAR1, SCAR2, SCAR3
CC and SCARL. Interacts also with CIPK24/SOS2. Binds to the fibrillin
CC precursor protein. Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3,
CC PYL4, PYL5, PYL6, PYL8 and PYL9, and with free PYL2, PYL3 and PYL4.
CC Interacts with and represses GHR1, and, to a lesser extent, SRK2E/OST1
CC (PubMed:22730405). {ECO:0000269|PubMed:12194854,
CC ECO:0000269|PubMed:14504388, ECO:0000269|PubMed:16571665,
CC ECO:0000269|PubMed:16998070, ECO:0000269|PubMed:17267444,
CC ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19407143,
CC ECO:0000269|PubMed:19769575, ECO:0000269|PubMed:22730405}.
CC -!- INTERACTION:
CC O04719; Q9LDI3: CIPK24; NbExp=4; IntAct=EBI-537680, EBI-537551;
CC O04719; O81439: PAP1; NbExp=5; IntAct=EBI-537680, EBI-962363;
CC O04719; Q8H1R0: PYL10; NbExp=3; IntAct=EBI-537680, EBI-2363213;
CC O04719; Q9FLB1: PYL5; NbExp=4; IntAct=EBI-537680, EBI-2363181;
CC O04719; Q8S8E3: PYL6; NbExp=4; IntAct=EBI-537680, EBI-2363192;
CC O04719; Q9FGM1: PYL8; NbExp=3; IntAct=EBI-537680, EBI-2429535;
CC O04719; Q84MC7: PYL9; NbExp=7; IntAct=EBI-537680, EBI-2349513;
CC O04719; O49686: PYR1; NbExp=3; IntAct=EBI-537680, EBI-2349590;
CC O04719; Q84JG2: SWI3B; NbExp=2; IntAct=EBI-537680, EBI-1102271;
CC O04719-1; Q8VZS8: PYL1; NbExp=2; IntAct=EBI-15803514, EBI-2363104;
CC O04719-1; O80992: PYL2; NbExp=3; IntAct=EBI-15803514, EBI-2363125;
CC O04719-1; Q9SSM7: PYL3; NbExp=2; IntAct=EBI-15803514, EBI-2363144;
CC O04719-1; O80920: PYL4; NbExp=2; IntAct=EBI-15803514, EBI-2349683;
CC O04719-1; Q9FLB1: PYL5; NbExp=2; IntAct=EBI-15803514, EBI-2363181;
CC O04719-1; Q8S8E3: PYL6; NbExp=2; IntAct=EBI-15803514, EBI-2363192;
CC O04719-1; O49686: PYR1; NbExp=2; IntAct=EBI-15803514, EBI-2349590;
CC O04719-1; Q39192: SRK2D; NbExp=2; IntAct=EBI-15803514, EBI-2363308;
CC O04719-1; Q940H6: SRK2E; NbExp=5; IntAct=EBI-15803514, EBI-782514;
CC O04719-1; Q39193: SRK2I; NbExp=2; IntAct=EBI-15803514, EBI-2620383;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O04719-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O04719-2; Sequence=VSP_034834;
CC -!- INDUCTION: Repressed by MYB44 and ERF4. Induced by salt stress and ABA.
CC {ECO:0000269|PubMed:14731256, ECO:0000269|PubMed:16021341,
CC ECO:0000269|PubMed:16998070, 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 -!- MISCELLANEOUS: The reduced form of ABI2 is converted to the oxidized
CC form by the addition of oxidized GPX3 or H(2)O(2).
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; Y08966; CAA70163.1; -; Genomic_DNA.
DR EMBL; Y08965; CAA70162.1; -; mRNA.
DR EMBL; Y11840; CAA72538.1; -; Genomic_DNA.
DR EMBL; AB024035; BAA97035.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96839.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96840.1; -; Genomic_DNA.
DR EMBL; AY136415; AAM97081.1; -; mRNA.
DR EMBL; BT008860; AAP68299.1; -; mRNA.
DR RefSeq; NP_001119448.1; NM_001125976.2. [O04719-2]
DR RefSeq; NP_200515.1; NM_125087.3. [O04719-1]
DR PDB; 3NMV; X-ray; 2.10 A; B=101-423.
DR PDB; 3UJK; X-ray; 1.90 A; A=101-423.
DR PDB; 3UJL; X-ray; 2.50 A; B=101-423.
DR PDBsum; 3NMV; -.
DR PDBsum; 3UJK; -.
DR PDBsum; 3UJL; -.
DR AlphaFoldDB; O04719; -.
DR SMR; O04719; -.
DR BioGRID; 21053; 40.
DR DIP; DIP-35025N; -.
DR IntAct; O04719; 19.
DR MINT; O04719; -.
DR STRING; 3702.AT5G57050.1; -.
DR iPTMnet; O04719; -.
DR PaxDb; O04719; -.
DR PRIDE; O04719; -.
DR ProteomicsDB; 250919; -. [O04719-1]
DR EnsemblPlants; AT5G57050.1; AT5G57050.1; AT5G57050. [O04719-1]
DR EnsemblPlants; AT5G57050.2; AT5G57050.2; AT5G57050. [O04719-2]
DR GeneID; 835809; -.
DR Gramene; AT5G57050.1; AT5G57050.1; AT5G57050. [O04719-1]
DR Gramene; AT5G57050.2; AT5G57050.2; AT5G57050. [O04719-2]
DR KEGG; ath:AT5G57050; -.
DR Araport; AT5G57050; -.
DR TAIR; locus:2164610; AT5G57050.
DR eggNOG; KOG0698; Eukaryota.
DR InParanoid; O04719; -.
DR OMA; LFELGNM; -.
DR PhylomeDB; O04719; -.
DR EvolutionaryTrace; O04719; -.
DR PRO; PR:O04719; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O04719; baseline and differential.
DR Genevisible; O04719; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004722; F:protein serine/threonine phosphatase activity; ISS:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:TAIR.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0010205; P:photoinhibition; IMP:TAIR.
DR GO; GO:1902456; P:regulation of stomatal opening; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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; Alternative splicing;
KW Disulfide bond; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..423
FT /note="Protein phosphatase 2C 77"
FT /id="PRO_0000057767"
FT DOMAIN 112..411
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20729862,
FT ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV,
FT ECO:0007744|PDB:3UJL"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20729862,
FT ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV,
FT ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20729862,
FT ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV,
FT ECO:0007744|PDB:3UJL"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20729862,
FT ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV,
FT ECO:0007744|PDB:3UJL"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20729862,
FT ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV,
FT ECO:0007744|PDB:3UJL"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20729862,
FT ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV,
FT ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL"
FT BINDING 402
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20729862,
FT ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV,
FT ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL"
FT SITE 290
FT /note="Lock"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT DISULFID 257..331
FT /evidence="ECO:0000269|PubMed:22116026,
FT ECO:0007744|PDB:3UJL"
FT VAR_SEQ 29..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034834"
FT MUTAGEN 168
FT /note="G->D: In abi2; reduced phosphatase activity, reduced
FT affinity with magnesium ions, loss of interaction with the
FT fibrillin precursor protein, impaired ABA-mediated binding
FT to PYR1, and reduced negative control on fibrillin
FT activity."
FT /evidence="ECO:0000269|PubMed:16571665,
FT ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:9165752"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 159..170
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 171..191
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 199..217
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:3UJK"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:3UJL"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:3UJK"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 345..361
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3UJK"
FT HELIX 382..397
FT /evidence="ECO:0007829|PDB:3UJK"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:3UJK"
SQ SEQUENCE 423 AA; 46306 MW; 67CAAC76DA531A71 CRC64;
MDEVSPAVAV PFRPFTDPHA GLRGYCNGES RVTLPESSCS GDGAMKDSSF EINTRQDSLT
SSSSAMAGVD ISAGDEINGS DEFDPRSMNQ SEKKVLSRTE SRSLFEFKCV PLYGVTSICG
RRPEMEDSVS TIPRFLQVSS SSLLDGRVTN GFNPHLSAHF FGVYDGHGGS QVANYCRERM
HLALTEEIVK EKPEFCDGDT WQEKWKKALF NSFMRVDSEI ETVAHAPETV GSTSVVAVVF
PTHIFVANCG DSRAVLCRGK TPLALSVDHK PDRDDEAARI EAAGGKVIRW NGARVFGVLA
MSRSIGDRYL KPSVIPDPEV TSVRRVKEDD CLILASDGLW DVMTNEEVCD LARKRILLWH
KKNAMAGEAL LPAEKRGEGK DPAAMSAAEY LSKMALQKGS KDNISVVVVD LKGIRKFKSK
SLN
