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 24-JAN-2024, entry version 174. 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; GN 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}. 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; 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.P49598; -. DR TCDB; 8.A.211.1.1; the pp2c,d phosphatase sal1 (sal1) family. DR iPTMnet; P49598; -. DR PaxDb; 3702-AT3G11410-1; -. 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; AT3G11410; PP2CA. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_20_0_1; -. DR InParanoid; P49598; -. DR OMA; VMASDEW; -. DR OrthoDB; 415067at2759; -. DR PhylomeDB; P49598; -. DR PRO; PR:P49598; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; P49598; baseline and differential. 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: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; 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:SF93; PROTEIN PHOSPHATASE 2C 37; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 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; P49598; AT. 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 //