Q9DC50 · OCTC_MOUSE
- ProteinPeroxisomal carnitine O-octanoyltransferase
- GeneCrot
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids612 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate.
Catalytic activity
- (R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine
- (R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-dimethylnonanoyl-(R)-carnitine
Pathway
Lipid metabolism; fatty acid beta-oxidation.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 327 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 406 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 410-417 | CoA (UniProtKB | ChEBI) | ||||
Sequence: KEEALHPD | ||||||
Binding site | 439 | (R)-carnitine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 441 | (R)-carnitine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 452 | (R)-carnitine (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | peroxisome | |
Molecular Function | carnitine O-octanoyltransferase activity | |
Biological Process | carnitine metabolic process | |
Biological Process | coenzyme A metabolic process | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | fatty acid metabolic process | |
Biological Process | fatty acid transport | |
Biological Process | generation of precursor metabolites and energy | |
Biological Process | medium-chain fatty acid metabolic process | |
Biological Process | response to xenobiotic stimulus |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxisomal carnitine O-octanoyltransferase
- EC number
- Short namesCOT
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 accessionQ9DC50
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 323 | Increases activity with octanoyl-CoA. | ||||
Sequence: C → M | ||||||
Mutagenesis | 335 | Slightly decreases activity with octanoyl-CoA. | ||||
Sequence: M → A | ||||||
Mutagenesis | 335 | Strongly decreases activity with octanoyl-CoA. | ||||
Sequence: M → A | ||||||
Mutagenesis | 553 | Loss of activity with octanoyl-CoA and myristoyl-CoA. | ||||
Sequence: G → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 39 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000210170 | 1-612 | Peroxisomal carnitine O-octanoyltransferase | |||
Sequence: MENQLTKSVEERTFQYQDSLPSLPVPALEESLKKYLESVKPFANEDEYKKTEEIVQKFQEGAGKRLHQKLLERARGKRNWLEEWWLNVAYLDVRIPSQLNVNFVGPCPHFEHYWPAREGTQLERGSMMLWHNLNYWQLLRREKLPVHKSGNTPLDMNQFRMLFSTCKVPGITRDSIMNYFKTESEGHCPTHIAVLCRGRAFVFDVLHEGCLITPPELLRQLTYIHKKCSNEPVGPSIAALTSEERTRWAKAREYLISLDPENLTLLEKIQTSLFVYSIEDSSPHATPEEYSQVFEMLLGGDPSVRWGDKSYNLISFANGIFGCCCDHAPYDAMVMVNIAHYVDERVLETEGRWKGSEKVRDIPLPEELVFTVDEKILNDVSQAKAQHLKAASDLQIAASTFTSFGKKLTKEEALHPDTFIQLALQLAYYRLHGRPGCCYETAMTRYFYHGRTETVRSCTVEAVRWCQSMQDPSASLLERQQKMLEAFAKHNKMMKDCSHGKGFDRHLLGLLLIAKEEGLPVPELFEDPLFSRSGGGGNFVLSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSSWRSCPETDAEKLVQMIFHAFHDMIQLMNTAHL | ||||||
Modified residue | 40 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 57 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 406 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 406 | N6-succinyllysine; alternate | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 610-612 | Microbody targeting signal | ||||
Sequence: AHL |
Sequence similarities
Belongs to the carnitine/choline acetyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length612
- Mass (Da)70,264
- Last updated2001-06-01 v1
- Checksum1C045A419A75C8B6
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 459 | in Ref. 2; AAH12308 | ||||
Sequence: T → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK004567 EMBL· GenBank· DDBJ | BAB23378.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006593 EMBL· GenBank· DDBJ | AAH06593.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012308 EMBL· GenBank· DDBJ | AAH12308.1 EMBL· GenBank· DDBJ | mRNA |