P2C37_ARATH
ID P2C37_ARATH Reviewed; 399 AA.
AC P49598;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein phosphatase 2C 37;
DE Short=AtPP2C37;
DE EC=3.1.3.16;
DE AltName: Full=Protein ABA-HYPERSENSITIVE GERMINATION 3;
DE AltName: Full=Protein phosphatase 2C A;
DE Short=PP2CA;
GN Name=PP2CA; Synonyms=AHG3; OrderedLocusNames=At3g11410; ORFNames=F24K9.8;
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;
RX PubMed=7816619; DOI=10.1093/nar/22.24.5296;
RA Kuromori T., Yamamoto M.;
RT "Cloning of cDNAs from Arabidopsis thaliana that encode putative protein
RT phosphatase 2C and a human Dr1-like protein by transformation of a fission
RT yeast mutant.";
RL Nucleic Acids Res. 22:5296-5301(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-139 AND GLY-145.
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 [6]
RP INTERACTION WITH AKT2/AKT3.
RX PubMed=11181729; DOI=10.1093/jxb/52.354.181;
RA Vranova E., Taehtiharju S., Sriprang R., Willekens H., Heino P.,
RA Palva E.T., Inze D., Van Camp W.;
RT "The AKT3 potassium channel protein interacts with the AtPP2CA protein
RT phosphatase 2C.";
RL J. Exp. Bot. 52:181-182(2001).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND 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 [8]
RP FUNCTION, MUTAGENESIS OF GLY-139, TISSUE SPECIFICITY, INDUCTION BY ABA, AND
RP INTERACTION WITH AKT2/AKT3.
RX PubMed=12034902; DOI=10.1105/tpc.000943;
RA Cherel I., Michard E., Platet N., Mouline K., Alcon C., Sentenac H.,
RA Thibaud J.-B.;
RT "Physical and functional interaction of the Arabidopsis K(+) channel AKT2
RT and phosphatase AtPP2CA.";
RL Plant Cell 14:1133-1146(2002).
RN [9]
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 [10]
RP INDUCTION BY COLD STRESS.
RX PubMed=16214899; DOI=10.1105/tpc.105.035568;
RA Lee B.-H., Henderson D.A., Zhu J.-K.;
RT "The Arabidopsis cold-responsive transcriptome and its regulation by
RT ICE1.";
RL Plant Cell 17:3155-3175(2005).
RN [11]
RP FUNCTION, INDUCTION BY ABA, MUTAGENESIS OF GLY-145 AND GLY-287, AND TISSUE
RP 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 [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=16361522; DOI=10.1104/pp.105.070318;
RA Kuhn J.M., Boisson-Dernier A., Dizon M.B., Maktabi M.H., Schroeder J.I.;
RT "The protein phosphatase AtPP2CA negatively regulates abscisic acid signal
RT transduction in Arabidopsis, and effects of abh1 on AtPP2CA mRNA.";
RL Plant Physiol. 140:127-139(2006).
RN [13]
RP FUNCTION, INDUCTION BY ABA, AND TISSUE SPECIFICITY.
RX PubMed=17461784; DOI=10.1111/j.1365-313x.2007.03107.x;
RA Nishimura N., Yoshida T., Kitahata N., Asami T., Shinozaki K., Hirayama T.;
RT "ABA-Hypersensitive Germination1 encodes a protein phosphatase 2C, an
RT essential component of abscisic acid signaling in Arabidopsis seed.";
RL Plant J. 50:935-949(2007).
RN [14]
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 [15]
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 [16]
RP FUNCTION, INTERACTION WITH SLAC1 AND SRK2E/OST1, AND MUTAGENESIS OF GLY-139
RP AND GLY-145.
RX PubMed=19955427; DOI=10.1073/pnas.0910601106;
RA Lee S.C., Lan W., Buchanan B.B., Luan S.;
RT "A protein kinase-phosphatase pair interacts with an ion channel to
RT regulate ABA signaling in plant guard cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21419-21424(2009).
RN [17]
RP INTERACTION WITH PYR1; PYL1; PYL2; PYL3; PYL4; PYL9 AND PYL12, AND ACTIVITY
RP 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 [18]
RP INTERACTION WITH CBL1; CBL2; CBL3; CBL4; CBL5; CBL6; CBL7 AND CBL9.
RX PubMed=21596690; DOI=10.1093/mp/ssr031;
RA Lan W.Z., Lee S.C., Che Y.F., Jiang Y.Q., Luan S.;
RT "Mechanistic analysis of AKT1 regulation by the CBL-CIPK-PP2CA
RT interactions.";
RL Mol. Plant 4:527-536(2011).
RN [19]
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 [20]
RP INTERACTION WITH RGLG1 AND RGLG5, AND UBIQUITINATION.
RX PubMed=27577789; DOI=10.1105/tpc.16.00364;
RA Wu Q., Zhang X., Peirats-Llobet M., Belda-Palazon B., Wang X., Cui S.,
RA Yu X., Rodriguez P.L., An C.;
RT "Ubiquitin ligases RGLG1 and RGLG5 regulate abscisic acid signaling by
RT controlling the turnover of phosphatase PP2CA.";
RL Plant Cell 28:2178-2196(2016).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 72-399 IN COMPLEX WITH MAGNESIUM
RP AND ZINC, AND 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).
CC -!- FUNCTION: Major negative regulator of abscisic acid (ABA) responses
CC during seed germination and cold acclimation. Confers insensitivity to
CC ABA. Modulates negatively the AKT2/3 activity, which mediates K(+)
CC transport and membrane polarization during stress situations, probably
CC by dephosphorylation. Prevents stomata closure by inactivating the S-
CC type anion efflux channel SLAC1 and its activator SRK2E. 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). {ECO:0000269|PubMed:11439132,
CC ECO:0000269|PubMed:12034902, ECO:0000269|PubMed:16339800,
CC ECO:0000269|PubMed:16361522, ECO:0000269|PubMed:17461784,
CC ECO:0000269|PubMed:19955427, ECO:0000269|PubMed:24179127,
CC ECO:0000269|PubMed:9448270}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24165892};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000269|PubMed:24165892};
CC -!- ACTIVITY REGULATION: Repressed by PYR/PYL/RCAR ABA receptors in an ABA-
CC dependent manner. {ECO:0000269|PubMed:19407142}.
CC -!- SUBUNIT: Interacts with AKT2/AKT3. Interacts with ABA-bounded PYR1,
CC PYL1, PYL2, PYL3, PYL4, PYL9 and PYL12, and with free PYL2, PYL3, PYL4
CC and PYL13. Binds to and inactivates SLAC1 and SRK2E. The inactivation
CC of SRK2E does not require phosphatase activity. Interacts with CBL1,
CC CBL2, CBL3, CBL5, and CBL7, but not CBL4, CBL6, and CBL9
CC (PubMed:11181729, PubMed:12034902, PubMed:19407142, PubMed:19955427,
CC PubMed:21596690, PubMed:24165892). Interacts with RGLG1 and RGLG5
CC (PubMed:27577789). Interacts with KIN10 (PubMed:24179127).
CC {ECO:0000269|PubMed:11181729, ECO:0000269|PubMed:12034902,
CC ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19955427,
CC ECO:0000269|PubMed:21596690, ECO:0000269|PubMed:24165892,
CC ECO:0000269|PubMed:24179127, ECO:0000269|PubMed:27577789}.
CC -!- INTERACTION:
CC P49598; Q38898: AKT2; NbExp=5; IntAct=EBI-1764934, EBI-1552774;
CC P49598; Q9LYL6: At3g56270; NbExp=3; IntAct=EBI-1764934, EBI-1238139;
CC P49598; A0A178V236: At4g37240; NbExp=3; IntAct=EBI-1764934, EBI-25521963;
CC P49598; Q9LFR7: CXE17; NbExp=3; IntAct=EBI-1764934, EBI-4456165;
CC P49598; A0SVK0: DOG1; NbExp=3; IntAct=EBI-1764934, EBI-25512274;
CC P49598; Q42510: GN; NbExp=3; IntAct=EBI-1764934, EBI-1998836;
CC P49598; Q9SZZ5: L73G19.50; NbExp=3; IntAct=EBI-1764934, EBI-25516330;
CC P49598; O22793: MORF2; NbExp=3; IntAct=EBI-1764934, EBI-1998046;
CC P49598; Q8H1R0: PYL10; NbExp=3; IntAct=EBI-1764934, EBI-2363213;
CC P49598; O80920: PYL4; NbExp=5; IntAct=EBI-1764934, EBI-2349683;
CC P49598; Q9FLB1: PYL5; NbExp=3; IntAct=EBI-1764934, EBI-2363181;
CC P49598; Q8S8E3: PYL6; NbExp=3; IntAct=EBI-1764934, EBI-2363192;
CC P49598; Q940H6: SRK2E; NbExp=2; IntAct=EBI-1764934, EBI-782514;
CC P49598; Q9SFT9: T1B9.26; NbExp=3; IntAct=EBI-1764934, EBI-4460083;
CC -!- TISSUE SPECIFICITY: Mostly expressed in seeds and leaves, and, to a
CC lower extent, in roots, stems, and flowers, particularly in siliques.
CC Essentially found in the phloem. {ECO:0000269|PubMed:11439132,
CC ECO:0000269|PubMed:12034902, ECO:0000269|PubMed:16339800,
CC ECO:0000269|PubMed:17461784}.
CC -!- INDUCTION: Repressed by MYB44. Induced by cold stress, drought, high
CC salt, and ABA. {ECO:0000269|PubMed:11439132,
CC ECO:0000269|PubMed:12034902, ECO:0000269|PubMed:16214899,
CC ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:16361522,
CC ECO:0000269|PubMed:17461784, 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}.
CC -!- PTM: Ubiquitinated by RGLG1 and RGLG5 in response to abscisic acid
CC (ABA). Ubiquitination of PP2CA leads to its degradation by the
CC proteasome. {ECO:0000269|PubMed:27577789}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; D38109; BAA07287.1; -; mRNA.
DR EMBL; AC008153; AAG51448.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75044.1; -; Genomic_DNA.
DR EMBL; AY074368; AAL67064.1; -; mRNA.
DR EMBL; AY091391; AAM14330.1; -; mRNA.
DR PIR; S55457; S55457.
DR RefSeq; NP_187748.1; NM_111974.4.
DR PDB; 4N0G; X-ray; 2.38 A; A/B=72-399.
DR PDBsum; 4N0G; -.
DR AlphaFoldDB; P49598; -.
DR SMR; P49598; -.
DR BioGRID; 5648; 59.
DR DIP; DIP-40197N; -.
DR IntAct; P49598; 30.
DR MINT; P49598; -.
DR STRING; 3702.AT3G11410.1; -.
DR iPTMnet; P49598; -.
DR PaxDb; P49598; -.
DR PRIDE; P49598; -.
DR ProteomicsDB; 248794; -.
DR EnsemblPlants; AT3G11410.1; AT3G11410.1; AT3G11410.
DR GeneID; 820314; -.
DR Gramene; AT3G11410.1; AT3G11410.1; AT3G11410.
DR KEGG; ath:AT3G11410; -.
DR Araport; AT3G11410; -.
DR TAIR; locus:2080787; AT3G11410.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_0_1; -.
DR InParanoid; P49598; -.
DR OMA; GCHFYGV; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; P49598; -.
DR PRO; PR:P49598; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P49598; baseline and differential.
DR Genevisible; P49598; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:TAIR.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0010360; P:negative regulation of anion channel activity; IDA:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
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; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP: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; SM00331; PP2C_SIG; 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; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Protein phosphatase; Reference proteome;
KW Ubl conjugation; Zinc.
FT CHAIN 1..399
FT /note="Protein phosphatase 2C 37"
FT /id="PRO_0000057769"
FT DOMAIN 104..389
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT BINDING 380
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24165892,
FT ECO:0007744|PDB:4N0G"
FT SITE 280
FT /note="Lock"
FT /evidence="ECO:0000250"
FT MUTAGEN 139
FT /note="G->D: Loss of phosphatase activity. Loss of kinase
FT activity but intact binding and repression of SRK2E; when
FT associated with D-145."
FT /evidence="ECO:0000269|PubMed:12034902,
FT ECO:0000269|PubMed:19955427, ECO:0000269|PubMed:9448270"
FT MUTAGEN 145
FT /note="G->D: Insensitive to ABA and loss of phosphatase
FT activity. Loss of kinase activity but intact binding and
FT repression of SRK2E; when associated with D-139."
FT /evidence="ECO:0000269|PubMed:16339800,
FT ECO:0000269|PubMed:19955427, ECO:0000269|PubMed:9448270"
FT MUTAGEN 287
FT /note="G->E: In ahg3-1; hypersensitivity to ABA during seed
FT germination, and loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:16339800"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 119..132
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 134..147
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 173..189
FT /evidence="ECO:0007829|PDB:4N0G"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:4N0G"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:4N0G"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:4N0G"
FT HELIX 361..375
FT /evidence="ECO:0007829|PDB:4N0G"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:4N0G"
SQ SEQUENCE 399 AA; 43350 MW; 83B82E32FEC71D4D CRC64;
MAGICCGVVG ETEPAAPVDS TSRASLRRRL DLLPSIKIVA DSAVAPPLEN CRKRQKRETV
VLSTLPGNLD LDSNVRSENK KARSAVTNSN SVTEAESFFS DVPKIGTTSV CGRRRDMEDA
VSIHPSFLQR NSENHHFYGV FDGHGCSHVA EKCRERLHDI VKKEVEVMAS DEWTETMVKS
FQKMDKEVSQ RECNLVVNGA TRSMKNSCRC ELQSPQCDAV GSTAVVSVVT PEKIIVSNCG
DSRAVLCRNG VAIPLSVDHK PDRPDELIRI QQAGGRVIYW DGARVLGVLA MSRAIGDNYL
KPYVIPDPEV TVTDRTDEDE CLILASDGLW DVVPNETACG VARMCLRGAG AGDDSDAAHN
ACSDAALLLT KLALARQSSD NVSVVVVDLR KRRNNQASS
