Q8GY31 · CDC25_ARATH
- ProteinDual specificity phosphatase Cdc25
- GeneCDC25
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids146 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity in vitro.
Arsenate reductase that plays a major role in the reduction of arsenate to arsenite and arsenic retention in roots (PubMed:16567632).
Has an in vitro and in vivo arsenate reductase activity (PubMed:16507083, PubMed:16766666, PubMed:22562211).
Plays no role in arsenic metabolism (PubMed:22879969, PubMed:25464340).
Has an in vitro and in vivo arsenate reductase activity (PubMed:16507083, PubMed:16766666, PubMed:22562211).
Plays no role in arsenic metabolism (PubMed:22879969, PubMed:25464340).
Miscellaneous
Binds 1 zinc ion which is not required for enzyme activity (PubMed:15329414).
Plants silencing ACR2 show increased sensitivity to arsenate but not arsenite (PubMed:16567632).
Plants silencing ACR2 show increased sensitivity to arsenate but not arsenite (PubMed:16567632).
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Activity regulation
Inhibited by NSC95397.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
50 mM | para-nitrophenyl phosphate |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 45-48 | substrate | ||||
Sequence: DEER | ||||||
Binding site | 53 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 68-71 | substrate | ||||
Sequence: KISH | ||||||
Active site | 86 | Cysteine persulfide intermediate | ||||
Sequence: C | ||||||
Binding site | 90-92 | substrate | ||||
Sequence: QVR | ||||||
Binding site | 134 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 136 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 141 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | arsenate reductase (glutaredoxin) activity | |
Molecular Function | metal ion binding | |
Molecular Function | protein tyrosine phosphatase activity | |
Biological Process | cell division | |
Biological Process | protein phosphorylation | |
Biological Process | response to arsenic-containing substance | |
Biological Process | sequestering of metal ion |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDual specificity phosphatase Cdc25
- EC number
- 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 accessionQ8GY31
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions, but plants show reduced root size when grown in presence of hydroxyurea (PubMed:20647223).
No visible phenotype, but decreased accumulation of total arsenic in shoots (PubMed:16507083).
No effect on arsenate sensitivity (PubMed:25099865).
No effect on the accumulation of arsenate in roots, efflux of arsenite or uptake of arsenate, or the total arsenic accumulation in shoots (PubMed:22879969, PubMed:25464340).
No visible phenotype, but decreased accumulation of total arsenic in shoots (PubMed:16507083).
No effect on arsenate sensitivity (PubMed:25099865).
No effect on the accumulation of arsenate in roots, efflux of arsenite or uptake of arsenate, or the total arsenic accumulation in shoots (PubMed:22879969, PubMed:25464340).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 86 | Loss of phosphatase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 145 | No major structural changes. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 18 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_0000198663 | 1-146 | Dual specificity phosphatase Cdc25 | |||
Sequence: MGRSIFSFFTKKKKMAMARSISYITSTQLLPLHRRPNIAIIDVRDEERNYDGHIAGSLHYASGSFDDKISHLVQNVKDKDTLVFHCALSQVRGPTCARRLVNYLDEKKEDTGIKNIMILERGFNGWEASGKPVCRCAEVPCKGDCA |
Proteomic databases
Expression
Tissue specificity
Expressed in roots and at lower levels in shoots (at protein level). Expressed in leaves, stems and flowers.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-135 | Rhodanese | ||||
Sequence: RRPNIAIIDVRDEERNYDGHIAGSLHYASGSFDDKISHLVQNVKDKDTLVFHCALSQVRGPTCARRLVNYLDEKKEDTGIKNIMILERGFNGWEASGKPVCR |
Sequence similarities
Belongs to the MPI phosphatase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length146
- Mass (Da)16,450
- Last updated2003-03-01 v1
- ChecksumEA2DD0E79784D538
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8BFF8 | A0A1P8BFF8_ARATH | CDC25 | 108 |
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL162751 EMBL· GenBank· DDBJ | CAB83305.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002688 EMBL· GenBank· DDBJ | AED90607.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK117898 EMBL· GenBank· DDBJ | BAC42537.1 EMBL· GenBank· DDBJ | mRNA | ||
BT003658 EMBL· GenBank· DDBJ | AAO39886.1 EMBL· GenBank· DDBJ | mRNA | ||
AY086729 EMBL· GenBank· DDBJ | AAM63780.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |