P38797 · PP2C7_YEAST

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).

Caution

There are conflicting reports on the effect the deletion of PTC7 causes in cells (PubMed:23940037, PubMed:28076776).
In one report, deletion of PTC7 causes decreases in COQ6 levels, and mitochondrial defects observed are thought to be caused by disruption of the COQ6 pathway (PubMed:23940037).
In another report, deletion of PTC7 causes no change in COQ6 levels and mitochondrial defects observed in mutants are not thought to be caused by changes in the COQ6 pathway (PubMed:28076776).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 magnesium or manganese ions per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
155.7 μMphosphorylated CIT1
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
218.6 μmol/min/ug

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site109Mn2+ 1 (UniProtKB | ChEBI)
Binding site109Mn2+ 2 (UniProtKB | ChEBI)
Binding site110Mn2+ 1 (UniProtKB | ChEBI)
Binding site265Mn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnuclear envelope
Molecular Functionmetal ion binding
Molecular Functionmyosin phosphatase activity
Molecular Functionphosphoprotein phosphatase activity
Molecular Functionprotein serine/threonine phosphatase activity
Biological Processpeptidyl-serine dephosphorylation
Biological Processregulation of ubiquinone biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein phosphatase 2C homolog 7, mitochondrial
  • EC number
  • Short names
    PP2C-7

Gene names

    • Name
      PTC7
    • Ordered locus names
      YHR076W

Organism names

Accessions

  • Primary accession
    P38797
  • Secondary accessions
    • A2TBN2
    • D3DL26
    • Q06HN3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

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).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis109Loss of catalytic activity.
Mutagenesis265Loss of catalytic activity.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-39Mitochondrion
ChainPRO_000005777940-343Protein phosphatase 2C homolog 7, mitochondrial

Proteomic databases

Expression

Induction

By the presence of non-fermentable carbon sources and oxidative stress.

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P38797SEC14 P242805EBI-24588, EBI-16535

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain76-342PPM-type phosphatase

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    343
  • Mass (Da)
    37,782
  • Last updated
    2007-06-26 v2
  • Checksum
    FCCC729800371B24
MFANVGFRTLRVSRGPLYGSCSQIISFSKRTFYSSAKSGYQSNNSHGDAYSSGSQSGPFTYKTAVAFQPKDRDDLIYQKLKDSIRSPTGEDNYFVTSNNVHDIFAGVADGVGGWAEHGYDSSAISRELCKKMDEISTALAENSSKETLLTPKKIIGAAYAKIRDEKVVKVGGTTAIVAHFPSNGKLEVANLGDSWCGVFRDSKLVFQTKFQTVGFNAPYQLSIIPEEMLKEAERRGSKYILNTPRDADEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNAARTNDELQLLSQKFVDNVVSLSKDPNYPSVFAQEISKLTGKNYSGGKEDDITVVVVRVD

Sequence caution

The sequence AAB68888.1 differs from that shown. Reason: Erroneous gene model prediction

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp