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FLASH GENE
Symbol CRAT contributors: mct - updated : 14-03-2018
HGNC name carnitine acetyltransferase
HGNC id 2342
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • several potential MYOD binding sites
  • potential binding sites for members of HNF family
  • peroxisomal targeting signal
  • microbody targeting signal
  • mono polymer monomer
    HOMOLOGY
    interspecies homolog to murine Crat (90.4 pc)
    homolog to rattus Crat (90.7 pc)
    Homologene
    FAMILY
  • carnitine/choline acetyltransferase family
  • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,mitochondria,inner
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,peroxisome
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    text
  • matrix side of the mitochondrial inner membrane
  • basic FUNCTION
  • playing a role in the transesterification of short chain fatty acyl-CoA chains (C2-C4)
  • catalyzing the reversible transfer of acyl groups from an acyl-CoA thioester to carnitine
  • involved as well in the transport of acetyl-CoA into mitochondria
  • acting as a regulator of the ratio of acetyl-CoA/CoA in the subcellular compartments
  • its overexpression in primary skeletal myocytes increased glucose uptake and attenuated lipid-induced suppression of glucose oxidation, implicating carnitine insufficiency and reduced CRAT activity as reversible components of the metabolic syndrome
  • essential role for the mitochondrial matrix enzyme, carnitine acetyltransferase (CRAT), in regulating substrate switching and glucose tolerance
  • role of carnitine acetyl transferase in regulation of nitric oxide signaling in pulmonary arterial endothelial cells
  • catalyze the reversible conversion of acyl-CoAs into acylcarnitine esters
  • converts short- and medium-chain acyl-CoAs (C2 to C10-CoA), whereas no activity was observed with long-chain species
  • is a mitochondrial matrix enzyme that catalyzes the interconversion of acetyl-CoA and acetylcarnitine.
  • unlike muscle cells, substrate switch mechanisms that control macrophage energy metabolism and mitochondrial short-chain acyl-CoA pools during nutrient stress are controlled by pathways that are not solely reliant on CRAT
  • plays a crucial role in the transport of fatty acids for beta-oxidation
  • modulates mitochondrial acetyl-CoA/CoA (coenzyme A) ratios, thus regulating pyruvate dehydrogenase activity and glucose oxidation
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism energetic , lipid/lipoprotein
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule other,
  • coenzyme A
  • protein
  • lipid-induced antagonism of CRAT might contribute to decreased PDP1 activity and glucose disposal in the context of obesity and diabetes
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) CRATD
    related resource MITOP database
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional       loss of function
    decreased function in the brain of Alzeihmer patients
    constitutional        
    gene silencing disrupted mitochondrial bioenergetics resulting in reduced ATP generation and decreased NO signaling
    constitutional       loss of function
    has previously been shown to result in muscle insulin resistance due to accumulation of long-chain acylcarnitines
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS