| IED ID | IndEnz0018001297 |
| Enzyme Type ID | peroxidase001297 |
| Protein Name |
Protein phosphatase 2C 56 AtPP2C56 EC 3.1.3.16 Protein ABSCISIC ACID-INSENSITIVE 1 Protein phosphatase 2C ABI1 PP2C ABI1 |
| Gene Name | ABI1 At4g26080 F20B18.190 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MEEVSPAIAGPFRPFSETQMDFTGIRLGKGYCNNQYSNQDSENGDLMVSLPETSSCSVSGSHGSESRKVLISRINSPNLNMKESAAADIVVVDISAGDEINGSDITSEKKMISRTESRSLFEFKSVPLYGFTSICGRRPEMEDAVSTIPRFLQSSSGSMLDGRFDPQSAAHFFGVYDGHGGSQVANYCRERMHLALAEEIAKEKPMLCDGDTWLEKWKKALFNSFLRVDSEIESVAPETVGSTSVVAVVFPSHIFVANCGDSRAVLCRGKTALPLSVDHKPDREDEAARIEAAGGKVIQWNGARVFGVLAMSRSIGDRYLKPSIIPDPEVTAVKRVKEDDCLILASDGVWDVMTDEEACEMARKRILLWHKKNAVAGDASLLADERRKEGKDPAAMSAAEYLSKLAIQRGSKDNISVVVVDLKPRRKLKSKPLN |
| Enzyme Length | 434 |
| Uniprot Accession Number | P49597 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Phosphatase activity repressed by oxidized GPX3 and phosphatidic acid (PA). PA is produced by PLD alpha 1 in response to ABA. Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner. {ECO:0000269|PubMed:15197253, ECO:0000269|PubMed:16614222, ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19769575}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:10645425, ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9537523}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:10645425, ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9537523}; |
| DNA Binding | |
| EC Number | 3.1.3.16 |
| Enzyme Function | FUNCTION: Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1. Represses MAPKKK18 activity and promotes MAPKKK18 degradation by the proteasome pathway upon abscisic acid (ABA) treatment (PubMed:26443375). Represses KIN10 activity by the specific dephosphorylation of its T-loop Thr-198, leading to a poststress inactivation of SnRK1 signaling (PubMed:24179127). Restricts MAPKKK20 activity by dephosphorylation (PubMed:27913741). {ECO:0000269|PubMed:10488243, ECO:0000269|PubMed:10521520, ECO:0000269|PubMed:10645425, ECO:0000269|PubMed:10872217, ECO:0000269|PubMed:10950871, ECO:0000269|PubMed:11208021, ECO:0000269|PubMed:11289613, ECO:0000269|PubMed:11587514, ECO:0000269|PubMed:11701885, ECO:0000269|PubMed:11707572, ECO:0000269|PubMed:12047634, ECO:0000269|PubMed:12065416, ECO:0000269|PubMed:12194854, ECO:0000269|PubMed:12228349, ECO:0000269|PubMed:12232124, ECO:0000269|PubMed:12232276, ECO:0000269|PubMed:12432076, ECO:0000269|PubMed:12609042, ECO:0000269|PubMed:12713537, ECO:0000269|PubMed:14576281, ECO:0000269|PubMed:14596925, ECO:0000269|PubMed:15144382, ECO:0000269|PubMed:15197253, ECO:0000269|PubMed:15618419, ECO:0000269|PubMed:15923322, ECO:0000269|PubMed:16339784, ECO:0000269|PubMed:16365038, ECO:0000269|PubMed:16571665, ECO:0000269|PubMed:16614222, ECO:0000269|PubMed:16652949, ECO:0000269|PubMed:16798945, ECO:0000269|PubMed:17158582, ECO:0000269|PubMed:17304219, ECO:0000269|PubMed:18298671, ECO:0000269|PubMed:1834244, ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:24179127, ECO:0000269|PubMed:26443375, ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:7568166, ECO:0000269|PubMed:8492808, ECO:0000269|PubMed:8771791, ECO:0000269|PubMed:8898906, ECO:0000269|PubMed:9090884, ECO:0000269|PubMed:9108297, ECO:0000269|PubMed:9161030, ECO:0000269|PubMed:9165752, ECO:0000269|PubMed:9263461, ECO:0000269|PubMed:9276963, ECO:0000269|PubMed:9351242, ECO:0000269|PubMed:9448270, ECO:0000269|Ref.8}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:9537523}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (12); Chain (1); Domain (1); Helix (10); Metal binding (7); Motif (1); Mutagenesis (24); Sequence conflict (2); Site (1); Turn (3) |
| Keywords | 3D-structure;Abscisic acid signaling pathway;Cell membrane;Cytoplasm;Hydrolase;Magnesium;Manganese;Membrane;Metal-binding;Nucleus;Protein phosphatase;Reference proteome |
| Interact With | Q8VZS8; Q8H1R0; Q9FJ50; Q9FJ49; Q9SN51; O80992; Q9SSM7; O80920; Q9FLB1; Q8S8E3; Q1ECF1; Q9FGM1; Q84MC7; O49686; Q93ZY2; Q39192; Q940H6; Q39193; Q9LMA8 |
| Induction | INDUCTION: Repressed by MYB44. Induced by low temperature, drought, high salt, abscisic acid (ABA) and ethylene. {ECO:0000269|PubMed:11439132, ECO:0000269|PubMed:14731256, ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:16998070, ECO:0000269|PubMed:17158582, ECO:0000269|PubMed:18162593}. |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein. Note=Associated to the plasma membrane when in complex with PA, subsequently to ABA signaling. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3JRQ; 3KDJ; 3NMN; |
| Mapped Pubmed ID | 10441499; 10504578; 10527431; 10787063; 10899977; 10938371; 10972885; 11005831; 11115891; 11181729; 11459830; 11704678; 11779861; 11851911; 11882947; 12369629; 12427994; 12445125; 12446847; 12468729; 12514244; 12662310; 12857845; 12960166; 14504388; 15086800; 15356325; 15599761; 16280546; 16667813; 16805735; 17092320; 17261695; 17427804; 18028281; 18039663; 18088305; 18094993; 18365246; 18650403; 18775970; 19033529; 19240210; 19266168; 19458118; 19513806; 19624469; 19690149; 19705149; 19837818; 19847119; 19855047; 19880399; 19895399; 19924127; 20128877; 20164209; 20377695; 20490504; 20507936; 20519338; 20554531; 20639406; 20699393; 20803085; 20930557; 21172816; 21357183; 21371039; 21525137; 21556325; 21586729; 21610183; 21638061; 21666226; 21746700; 21778181; 21798944; 21821598; 21853252; 21885535; 22028934; 22090030; 22121246; 22156383; 22251383; 22350156; 22368268; 22652060; 22661072; 22705253; 22730405; 22968126; 22995285; 23007729; 23178483; 23268310; 23341337; 23370718; 23396828; 23437216; 23448237; 23452338; 23468926; 23483290; 23606412; 23630285; 23658427; 23660402; 23934343; 24078097; 24081610; 24098330; 24223981; 24279988; 24383079; 24492258; 24561249; 24637173; 24706923; 24828206; 25038254; 25074907; 25266633; 25268622; 25336569; 25795738; 25840086; 25976841; 26059040; 26063392; 26482222; 26491145; 26511514; 26625868; 26667153; 26724418; 26786013; 26852793; 26974851; 27192441; 27297076; 27474935; 27577789; 27923613; 28193765; 28494202; 28575641; 28716423; 28916739; 29288233; 29321786; 29444316; 29490615; 29618630; 29852366; 30014159; 30320882; 30730075; 30740122; 30886115; 31207493; 31357236; 31708935; 31713664; 31733960; 32326656; 32471862; 32490347; 32619606; 32625229; 32679718; 32933749; 32948668; 33048351; 33077597; 34099554; 8155877; 8761454; 8883386; 9112773; 9611170; 9765153; 9807815; 9862504; 9869399; |
| Motif | MOTIF 423..427; /note=Nuclear localization signal; /evidence=ECO:0000269|PubMed:18298671 |
| Gene Encoded By | |
| Mass | 47,506 |
| Kinetics | |
| Metal Binding | METAL 177; /note=Magnesium 1; /evidence=ECO:0007744|PDB:3NMN; METAL 177; /note=Magnesium 2; /evidence=ECO:0007744|PDB:3NMN; METAL 261; /note=Magnesium 1; /evidence=ECO:0007744|PDB:3NMN; METAL 262; /note=Magnesium 1; /evidence=ECO:0007744|PDB:3NMN; METAL 347; /note=Magnesium 1; /evidence=ECO:0007744|PDB:3NMN; METAL 347; /note=Magnesium 2; /evidence=ECO:0007744|PDB:3NMN; METAL 413; /note=Magnesium 2; /evidence=ECO:0007744|PDB:3NMN |
| Rhea ID | RHEA:20629; RHEA:47004 |
| Cross Reference Brenda | 3.1.3.16; |