Q9DBK0 · ACO12_MOUSE

  • Protein
    Acetyl-coenzyme A thioesterase
  • Gene
    Acot12
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Preferentially hydrolyzes acetyl-CoA.

Catalytic activity

Activity regulation

Allosterically regulated by ATP (activator) and ADP (inhibitor) (By similarity).
Cold labile, it dissociates into inactive monomers at low temperature (By similarity).

Pathway

Lipid metabolism; fatty acid metabolism.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site54-56CoA (UniProtKB | ChEBI)
Binding site83-85CoA (UniProtKB | ChEBI)
Binding site145CoA (UniProtKB | ChEBI)
Binding site235-237CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentintercellular bridge
Cellular Componentnucleoplasm
Molecular Functionacetyl-CoA hydrolase activity
Molecular FunctionATP binding
Molecular Functioncarboxylic ester hydrolase activity
Molecular Functionidentical protein binding
Molecular Functionlipid binding
Biological Processacetyl-CoA metabolic process
Biological Processfatty acid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acetyl-coenzyme A thioesterase
  • EC number
  • Alternative names
    • Acyl-CoA thioester hydrolase 12
    • Acyl-coenzyme A thioesterase 12 (Acyl-CoA thioesterase 12)
    • Cytoplasmic acetyl-CoA hydrolase 1 (CACH-1; mCACH-1)

Gene names

    • Name
      Acot12
    • Synonyms
      Cach, Cach1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9DBK0
  • Secondary accessions
    • Q544M5
    • Q8R108

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000538101-556Acetyl-coenzyme A thioesterase
Modified residue34N6-succinyllysine
Modified residue97N6-succinyllysine
Modified residue160N6-succinyllysine
Modified residue229N6-succinyllysine

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homodimer or homotetramer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-118HotDog ACOT-type 1
Domain180-295HotDog ACOT-type 2
Domain327-536START

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    556
  • Mass (Da)
    61,762
  • Last updated
    2001-06-01 v1
  • Checksum
    9FE9C487BBCBB812
MESMVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKPVGKEKVHLKPVLLQTEQEQVEHNLASERRKVRLQHENTFNNIMKESSRFSDSICNEEEGTATTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENATPDGLKSVL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB078618
EMBL· GenBank· DDBJ
BAB84021.1
EMBL· GenBank· DDBJ
mRNA
AK004905
EMBL· GenBank· DDBJ
BAB23658.1
EMBL· GenBank· DDBJ
mRNA
AK034622
EMBL· GenBank· DDBJ
BAC28775.1
EMBL· GenBank· DDBJ
mRNA
BC025852
EMBL· GenBank· DDBJ
AAH25852.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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