Q6PE15 · ABHDA_MOUSE
- ProteinPalmitoyl-protein thioesterase ABHD10, mitochondrial
- GeneAbhd10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids297 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as an acyl-protein thioesterase that hydrolyzes fatty acids from acylated residues in proteins (PubMed:31740833).
Regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating mitochondrial antioxidant ability (PubMed:31740833).
Also catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate (By similarity).
Regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating mitochondrial antioxidant ability (PubMed:31740833).
Also catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate (By similarity).
Catalytic activity
- H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H+ + hexadecanoate + L-cysteinyl-[protein]This reaction proceeds in the forward direction.
Activity regulation
Inhibited by palmostatin-B.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 143 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 240 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 270 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | hydrolase activity, hydrolyzing O-glycosyl compounds | |
Molecular Function | mycophenolic acid acyl-glucuronide esterase activity | |
Molecular Function | palmitoyl-(protein) hydrolase activity | |
Biological Process | glucuronoside catabolic process | |
Biological Process | protein depalmitoylation |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePalmitoyl-protein thioesterase ABHD10, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6PE15
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 22 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-43 | Mitochondrion | ||||
Sequence: MAAWAPCRRWGWAAVSFGRHPGLSASLARKPPRAWWLSACRQK | ||||||
Chain | PRO_0000280734 | 44-297 | Palmitoyl-protein thioesterase ABHD10, mitochondrial | |||
Sequence: ASLSFLNRSELPNLAYKRLKGKTPGIIFIPGYLSNMNGIKAVAVEEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADGLVTQYHALPVETQKEIEMKGEWTLPSRYNKEGYFRIPYSFIKEAEHHCLLHSPIPVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQGDHRMKEKADIHLLICTIDDLIDKLSTVVP |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 69-196 | AB hydrolase-1 | ||||
Sequence: IIFIPGYLSNMNGIKAVAVEEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADGLVTQYHALPVETQKEIEMKGEWTL |
Sequence similarities
Belongs to the AB hydrolase superfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q6PE15-1
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
- Length297
- Mass (Da)33,040
- Last updated2004-07-05 v1
- Checksum7AE4AEBD214ED6CE
Q6PE15-2
- Name2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6X5P5 | F6X5P5_MOUSE | Abhd10 | 51 |
Features
Showing features for sequence conflict, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK052670 EMBL· GenBank· DDBJ | BAC35091.1 EMBL· GenBank· DDBJ | mRNA | ||
AK084998 EMBL· GenBank· DDBJ | BAC39335.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166025 EMBL· GenBank· DDBJ | BAE38528.1 EMBL· GenBank· DDBJ | mRNA | ||
BC027656 EMBL· GenBank· DDBJ | AAH27656.1 EMBL· GenBank· DDBJ | mRNA | ||
BC058347 EMBL· GenBank· DDBJ | AAH58347.1 EMBL· GenBank· DDBJ | mRNA |