P38797 · PP2C7_YEAST
- ProteinProtein phosphatase 2C homolog 7, mitochondrial
- GenePTC7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids343 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein phosphatase which positively regulates biosynthesis of the ubiquinone, coenzyme Q (PubMed:12220683, PubMed:23940037, PubMed:28076776, PubMed:30267671).
Dephosphorylates and activates the ubiquinone biosynthesis protein CAT5/COQ7 (PubMed:23940037, PubMed:30267671).
Also dephosphorylates CIT1 on 'Ser-462', which leads to its activation (PubMed:28076776).
Dephosphorylates and activates the ubiquinone biosynthesis protein CAT5/COQ7 (PubMed:23940037, PubMed:30267671).
Also dephosphorylates CIT1 on 'Ser-462', which leads to its activation (PubMed:28076776).
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.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
155.7 μM | phosphorylated CIT1 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
218.6 μmol/min/ug |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nuclear envelope | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | peptidyl-serine dephosphorylation | |
Biological Process | regulation of ubiquinone biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein phosphatase 2C homolog 7, mitochondrial
- EC number
- Short namesPP2C-7
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38797
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Decreased growth in non-fermentable sugar mediums (PubMed:23940037, PubMed:28076776).
This is caused by a decrease in COQ6 levels, which results in a severe decrease in complex II, NADH-coenzyme Q dehydrogenase to complex III, and complex II to complex III activities in the electron transport chain (PubMed:23940037).
Impaired antioxidant defenses (PubMed:23940037).
Decreased phosphorylation of CAT5/COQ7 (PubMed:23940037).
Increased phosphorylation of CIT1 and decreased citrate synthase activity (PubMed:28076776).
This is caused by a decrease in COQ6 levels, which results in a severe decrease in complex II, NADH-coenzyme Q dehydrogenase to complex III, and complex II to complex III activities in the electron transport chain (PubMed:23940037).
Impaired antioxidant defenses (PubMed:23940037).
Decreased phosphorylation of CAT5/COQ7 (PubMed:23940037).
Increased phosphorylation of CIT1 and decreased citrate synthase activity (PubMed:28076776).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 109 | Loss of catalytic activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 265 | Loss of catalytic activity. | ||||
Sequence: D → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-39 | Mitochondrion | ||||
Sequence: MFANVGFRTLRVSRGPLYGSCSQIISFSKRTFYSSAKSG | ||||||
Chain | PRO_0000057779 | 40-343 | Protein phosphatase 2C homolog 7, mitochondrial | |||
Sequence: YQSNNSHGDAYSSGSQSGPFTYKTAVAFQPKDRDDLIYQKLKDSIRSPTGEDNYFVTSNNVHDIFAGVADGVGGWAEHGYDSSAISRELCKKMDEISTALAENSSKETLLTPKKIIGAAYAKIRDEKVVKVGGTTAIVAHFPSNGKLEVANLGDSWCGVFRDSKLVFQTKFQTVGFNAPYQLSIIPEEMLKEAERRGSKYILNTPRDADEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNAARTNDELQLLSQKFVDNVVSLSKDPNYPSVFAQEISKLTGKNYSGGKEDDITVVVVRVD |
Proteomic databases
Expression
Induction
By the presence of non-fermentable carbon sources and oxidative stress.
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P38797 | SEC14 P24280 | 5 | EBI-24588, EBI-16535 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 76-342 | PPM-type phosphatase | ||||
Sequence: IYQKLKDSIRSPTGEDNYFVTSNNVHDIFAGVADGVGGWAEHGYDSSAISRELCKKMDEISTALAENSSKETLLTPKKIIGAAYAKIRDEKVVKVGGTTAIVAHFPSNGKLEVANLGDSWCGVFRDSKLVFQTKFQTVGFNAPYQLSIIPEEMLKEAERRGSKYILNTPRDADEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNAARTNDELQLLSQKFVDNVVSLSKDPNYPSVFAQEISKLTGKNYSGGKEDDITVVVVRV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length343
- Mass (Da)37,782
- Last updated2007-06-26 v2
- ChecksumFCCC729800371B24
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U10556 EMBL· GenBank· DDBJ | AAB68888.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
EF123135 EMBL· GenBank· DDBJ | ABM97479.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ881450 EMBL· GenBank· DDBJ | ABI95877.1 EMBL· GenBank· DDBJ | mRNA | ||
BK006934 EMBL· GenBank· DDBJ | DAA06770.1 EMBL· GenBank· DDBJ | Genomic DNA |