O04719 · P2C77_ARATH
- ProteinProtein phosphatase 2C 77
- GeneABI2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids423 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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), high light stress, response to glucose, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as H2O2 and oxidative burst in response to ABA and dehydration. Represses GHR1 and, to some extent, SRK2E/OST1, kinases involved in the regulation of SLAC1-dependent stomatal closure (PubMed:22730405).
Controls negatively fibrillin that is involved in mediating ABA-induced photoprotection. May be implicated in ABA content regulation. Involved in acquired thermotolerance of root growth and seedling survival. Required for the Erwinia amylovora harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic response
Controls negatively fibrillin that is involved in mediating ABA-induced photoprotection. May be implicated in ABA content regulation. Involved in acquired thermotolerance of root growth and seedling survival. Required for the Erwinia amylovora harpin-induced (HrpN) drought tolerance. Involved in the hydrotropic response
Miscellaneous
The reduced form of ABI2 is converted to the oxidized form by the addition of oxidized GPX3 or H2O2.
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
Phosphatase activity repressed by oxidized ATGPX3, free fatty acids (e.g. arachidonic acid (20:4) and Linolenic acid (18:3)) and by H2O2. Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner.
pH Dependence
Optimum pH is 8.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 165 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 165 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 251 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 252 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Site | 290 | Lock | ||||
Sequence: W | ||||||
Binding site | 337 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 337 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 402 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | abscisic acid-activated signaling pathway | |
Biological Process | negative regulation of protein kinase activity | |
Biological Process | photoinhibition | |
Biological Process | regulation of stomatal opening | |
Biological Process | response to abscisic acid | |
Biological Process | response to heat | |
Biological Process | response to osmotic stress | |
Biological Process | response to water deprivation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein phosphatase 2C 77
- EC number
- Short namesAtPP2C77
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO04719
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 168 | In abi2; reduced phosphatase activity, reduced affinity with magnesium ions, loss of interaction with the fibrillin precursor protein, impaired ABA-mediated binding to PYR1, and reduced negative control on fibrillin activity. | ||||
Sequence: G → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 40 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000057767 | 1-423 | Protein phosphatase 2C 77 | |||
Sequence: MDEVSPAVAVPFRPFTDPHAGLRGYCNGESRVTLPESSCSGDGAMKDSSFEINTRQDSLTSSSSAMAGVDISAGDEINGSDEFDPRSMNQSEKKVLSRTESRSLFEFKCVPLYGVTSICGRRPEMEDSVSTIPRFLQVSSSSLLDGRVTNGFNPHLSAHFFGVYDGHGGSQVANYCRERMHLALTEEIVKEKPEFCDGDTWQEKWKKALFNSFMRVDSEIETVAHAPETVGSTSVVAVVFPTHIFVANCGDSRAVLCRGKTPLALSVDHKPDRDDEAARIEAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEVTSVRRVKEDDCLILASDGLWDVMTNEEVCDLARKRILLWHKKNAMAGEALLPAEKRGEGKDPAAMSAAEYLSKMALQKGSKDNISVVVVDLKGIRKFKSKSLN | ||||||
Disulfide bond | 257↔331 | |||||
Sequence: CRGKTPLALSVDHKPDRDDEAARIEAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEVTSVRRVKEDDC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Repressed by MYB44 and ERF4. Induced by salt stress and ABA.
Gene expression databases
Interaction
Subunit
Interacts with SPK1, CIPK15/PKS3, GPX3, SCAR1, SCAR2, SCAR3 and SCARL. Interacts also with CIPK24/SOS2. Binds to the fibrillin precursor protein. Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL5, PYL6, PYL8 and PYL9, and with free PYL2, PYL3 and PYL4. Interacts with and represses GHR1, and, to a lesser extent, SRK2E/OST1 (PubMed:22730405).
Binary interactions
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 74-95 | Disordered | ||||
Sequence: GDEINGSDEFDPRSMNQSEKKV | ||||||
Compositional bias | 79-95 | Basic and acidic residues | ||||
Sequence: GSDEFDPRSMNQSEKKV | ||||||
Domain | 112-411 | PPM-type phosphatase | ||||
Sequence: LYGVTSICGRRPEMEDSVSTIPRFLQVSSSSLLDGRVTNGFNPHLSAHFFGVYDGHGGSQVANYCRERMHLALTEEIVKEKPEFCDGDTWQEKWKKALFNSFMRVDSEIETVAHAPETVGSTSVVAVVFPTHIFVANCGDSRAVLCRGKTPLALSVDHKPDRDDEAARIEAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEVTSVRRVKEDDCLILASDGLWDVMTNEEVCDLARKRILLWHKKNAMAGEALLPAEKRGEGKDPAAMSAAEYLSKMALQKGSKDNISVVVVDL |
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 & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O04719-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length423
- Mass (Da)46,306
- Last updated1997-07-01 v1
- Checksum67CAAC76DA531A71
O04719-2
- Name2
- Differences from canonical
- 29-68: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8BEK2 | A0A1P8BEK2_ARATH | ABI2 | 312 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_034834 | 29-68 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 79-95 | Basic and acidic residues | ||||
Sequence: GSDEFDPRSMNQSEKKV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y08966 EMBL· GenBank· DDBJ | CAA70163.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y08965 EMBL· GenBank· DDBJ | CAA70162.1 EMBL· GenBank· DDBJ | mRNA | ||
Y11840 EMBL· GenBank· DDBJ | CAA72538.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB024035 EMBL· GenBank· DDBJ | BAA97035.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED96839.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED96840.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY136415 EMBL· GenBank· DDBJ | AAM97081.1 EMBL· GenBank· DDBJ | mRNA | ||
BT008860 EMBL· GenBank· DDBJ | AAP68299.1 EMBL· GenBank· DDBJ | mRNA |