P49598 · P2C37_ARATH
- ProteinProtein phosphatase 2C 37
- GenePP2CA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids399 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Major negative regulator of abscisic acid (ABA) responses during seed germination and cold acclimation. Confers insensitivity to ABA. Modulates negatively the AKT2/3 activity, which mediates K+ transport and membrane polarization during stress situations, probably by dephosphorylation. Prevents stomata closure by inactivating the S-type anion efflux channel SLAC1 and its activator SRK2E. Represses KIN10 activity by the specific dephosphorylation of its T-loop Thr-198, leading to a poststress inactivation of SnRK1 signaling (PubMed:24179127).
Catalytic activity
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 magnesium or manganese ions per subunit.
Activity regulation
Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 142 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 142 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 143 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 146 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 148 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 208 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 210 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 280 | Lock | ||||
Sequence: W | ||||||
Binding site | 327 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 327 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 331 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 380 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | kinase binding | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | phosphatase activity | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | protein kinase binding | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | abscisic acid-activated signaling pathway | |
Biological Process | defense response to virus | |
Biological Process | negative regulation of abscisic acid-activated signaling pathway | |
Biological Process | negative regulation of anion channel activity | |
Biological Process | regulation of stomatal movement | |
Biological Process | response to abscisic acid | |
Biological Process | response to cold | |
Biological Process | response to water deprivation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein phosphatase 2C 37
- EC number
- Short namesAtPP2C37
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP49598
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 139 | Loss of phosphatase activity. Loss of kinase activity but intact binding and repression of SRK2E; when associated with D-145. | ||||
Sequence: G → D | ||||||
Mutagenesis | 145 | Insensitive to ABA and loss of phosphatase activity. Loss of kinase activity but intact binding and repression of SRK2E; when associated with D-139. | ||||
Sequence: G → D | ||||||
Mutagenesis | 287 | In ahg3-1; hypersensitivity to ABA during seed germination, and loss of phosphatase activity. | ||||
Sequence: G → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 49 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000057769 | 1-399 | Protein phosphatase 2C 37 | |||
Sequence: MAGICCGVVGETEPAAPVDSTSRASLRRRLDLLPSIKIVADSAVAPPLENCRKRQKRETVVLSTLPGNLDLDSNVRSENKKARSAVTNSNSVTEAESFFSDVPKIGTTSVCGRRRDMEDAVSIHPSFLQRNSENHHFYGVFDGHGCSHVAEKCRERLHDIVKKEVEVMASDEWTETMVKSFQKMDKEVSQRECNLVVNGATRSMKNSCRCELQSPQCDAVGSTAVVSVVTPEKIIVSNCGDSRAVLCRNGVAIPLSVDHKPDRPDELIRIQQAGGRVIYWDGARVLGVLAMSRAIGDNYLKPYVIPDPEVTVTDRTDEDECLILASDGLWDVVPNETACGVARMCLRGAGAGDDSDAAHNACSDAALLLTKLALARQSSDNVSVVVVDLRKRRNNQASS |
Post-translational modification
Ubiquitinated by RGLG1 and RGLG5 in response to abscisic acid (ABA). Ubiquitination of PP2CA leads to its degradation by the proteasome.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Mostly expressed in seeds and leaves, and, to a lower extent, in roots, stems, and flowers, particularly in siliques. Essentially found in the phloem.
Induction
Repressed by MYB44. Induced by cold stress, drought, high salt, and ABA.
Gene expression databases
Interaction
Subunit
Interacts with AKT2/AKT3. Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL9 and PYL12, and with free PYL2, PYL3, PYL4 and PYL13. Binds to and inactivates SLAC1 and SRK2E. The inactivation of SRK2E does not require phosphatase activity. Interacts with CBL1, CBL2, CBL3, CBL5, and CBL7, but not CBL4, CBL6, and CBL9 (PubMed:11181729, PubMed:12034902, PubMed:19407142, PubMed:19955427, PubMed:21596690, PubMed:24165892).
Interacts with RGLG1 and RGLG5 (PubMed:27577789).
Interacts with KIN10 (PubMed:24179127).
Interacts with RGLG1 and RGLG5 (PubMed:27577789).
Interacts with KIN10 (PubMed:24179127).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P49598 | AKT2 Q38898 | 5 | EBI-1764934, EBI-1552774 | |
BINARY | P49598 | At3g56270 Q9LYL6 | 3 | EBI-1764934, EBI-1238139 | |
BINARY | P49598 | At4g37240 A0A178V236 | 3 | EBI-1764934, EBI-25521963 | |
BINARY | P49598 | CXE17 Q9LFR7 | 3 | EBI-1764934, EBI-4456165 | |
BINARY | P49598 | DOG1 A0SVK0 | 3 | EBI-1764934, EBI-25512274 | |
BINARY | P49598 | GN Q42510 | 3 | EBI-1764934, EBI-1998836 | |
BINARY | P49598 | L73G19.50 Q9SZZ5 | 3 | EBI-1764934, EBI-25516330 | |
BINARY | P49598 | MORF2 O22793 | 3 | EBI-1764934, EBI-1998046 | |
BINARY | P49598 | PYL10 Q8H1R0 | 3 | EBI-1764934, EBI-2363213 | |
BINARY | P49598 | PYL4 O80920 | 5 | EBI-1764934, EBI-2349683 | |
BINARY | P49598 | PYL5 Q9FLB1 | 3 | EBI-1764934, EBI-2363181 | |
BINARY | P49598 | PYL6 Q8S8E3 | 3 | EBI-1764934, EBI-2363192 | |
BINARY | P49598 | SRK2E Q940H6 | 2 | EBI-1764934, EBI-782514 | |
BINARY | P49598 | T1B9.26 Q9SFT9 | 3 | EBI-1764934, EBI-4460083 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 104-389 | PPM-type phosphatase | ||||
Sequence: KIGTTSVCGRRRDMEDAVSIHPSFLQRNSENHHFYGVFDGHGCSHVAEKCRERLHDIVKKEVEVMASDEWTETMVKSFQKMDKEVSQRECNLVVNGATRSMKNSCRCELQSPQCDAVGSTAVVSVVTPEKIIVSNCGDSRAVLCRNGVAIPLSVDHKPDRPDELIRIQQAGGRVIYWDGARVLGVLAMSRAIGDNYLKPYVIPDPEVTVTDRTDEDECLILASDGLWDVVPNETACGVARMCLRGAGAGDDSDAAHNACSDAALLLTKLALARQSSDNVSVVVVDL |
Domain
The 'lock' site stabilizes the complex made of PP2C, ABA and PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch' loops in closed positions.
Sequence similarities
Belongs to the PP2C family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length399
- Mass (Da)43,350
- Last updated1996-02-01 v1
- Checksum83B82E32FEC71D4D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D38109 EMBL· GenBank· DDBJ | BAA07287.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008153 EMBL· GenBank· DDBJ | AAG51448.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE75044.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY074368 EMBL· GenBank· DDBJ | AAL67064.1 EMBL· GenBank· DDBJ | mRNA | ||
AY091391 EMBL· GenBank· DDBJ | AAM14330.1 EMBL· GenBank· DDBJ | mRNA |