CRAT (Carnitine O-Acetyltransferase) Gene: Function, Disease Associations, and Expression
Comprehensive biomedical overview of the CRAT gene, including genomic context, protein function, tissue expression, mutations, and clinical significance.
Gene Information Card
| Symbol | CRAT |
|---|---|
| Full Name | carnitine O-acetyltransferase |
| Gene Type | protein coding |
| Chromosomal Location | 9q34.11 |
| NCBI Gene ID | 1384 ncbi.nlm.nih.gov/gene/1384 |
| Ensembl ID | ENSG00000095321 |
| UniProt ID | P43155 |
| OMIM ID | 600184 |
| HGNC ID | 2342 |
| Aliases | CAT1, carnitine acetylase |
Description
The CRAT gene encodes carnitine O-acetyltransferase, a mitochondrial enzyme that catalyzes the reversible transfer of acetyl groups between coenzyme A (CoA) and carnitine. This reaction is essential for maintaining the acyl-CoA/CoA ratio and for shuttling acetyl units across mitochondrial membranes, thereby playing a critical role in fatty acid metabolism, glucose metabolism, and energy homeostasis. CRAT is expressed in multiple tissues, with highest levels in heart, skeletal muscle, and liver. Mutations in CRAT have been associated with metabolic disorders and may influence cancer progression.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Carnitine-acylcarnitine translocase deficiency (secondary) | CRAT mutations may impair acetylcarnitine synthesis, affecting mitochondrial transport and energy metabolism. | ClinVar: pathogenic variants reported in patients with metabolic phenotypes. |
| Type 2 diabetes (susceptibility) | Altered CRAT expression affects acetyl-CoA buffering and insulin sensitivity in muscle. | OMIM: association studies; PubMed evidence. |
| Colorectal cancer (prognostic marker) | CRAT downregulation in tumors correlates with poor prognosis, possibly via metabolic reprogramming. | COSMIC: somatic mutations and expression changes in cancer samples. |
| Encephalopathy, acute, and metabolic disturbances | Biallelic CRAT mutations cause a rare neurometabolic disorder with episodic encephalopathy. | ClinVar: pathogenic variants; OMIM: 600184. |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Heart | 12.5 | High |
| Skeletal Muscle | 10.2 | High |
| Liver | 8.7 | Medium |
| Kidney | 6.3 | Medium |
| Brain | 2.1 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HepG2 (liver) | 9.8 | High expression |
| MCF7 (breast) | 4.5 | Moderate |
| A549 (lung) | 3.2 | Low |
| K562 (leukemia) | 1.8 | Very low |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.136C>T (p.Arg46Trp) | Missense | Rare | Reduced enzyme activity; associated with metabolic disorder. |
| c.1000G>A (p.Gly334Ser) | Missense | Rare | Impaired substrate binding; reported in ClinVar. |
| c.1234delA (p.Thr412ProfsTer23) | Frameshift | Very rare | Loss of function; likely pathogenic. |
| c.845A>G (p.Tyr282Cys) | Missense | Somatic (COSMIC) | Potential impact on protein stability; found in cancer samples. |
Mutation functional classification
Loss of Function (LOF)
Most pathogenic CRAT mutations are loss-of-function, leading to reduced acetyltransferase activity and impaired mitochondrial metabolism.
Gain of Function (GOF)
No clear gain-of-function mutations have been reported; CRAT is not known to act as an oncogene.
Dominant Negative (DN)
No evidence for dominant-negative effects; CRAT mutations are typically recessive.
View complete mutation data：
Gene Ontology (GO)
| • carnitine O-acetyltransferase activity | • acetyl-CoA C-acetyltransferase activity |
| • mitochondrial matrix | • fatty acid beta-oxidation |
| • acyl-CoA metabolic process | • carnitine metabolic process |
Pathways
• Fatty acid metabolism
• Mitochondrial carnitine shuttle
• Acetyl-CoA metabolism
• Glucose metabolism (insulin signaling)
Protein Summary
The CRAT protein (UniProt P43155) is a 626-amino acid mitochondrial enzyme that forms homotetramers. It catalyzes the reversible conversion of acetyl-CoA and carnitine to acetylcarnitine and CoA. This reaction is crucial for buffering acetyl-CoA levels and for exporting acetyl groups from mitochondria. The protein contains a carnitine acyltransferase domain and is highly conserved across species. Post-translational modifications include acetylation, which may regulate its activity.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| CRAT Knockout HEK293 Cell Line | EDJ-KQ1943 | Human | 1384 | Details Get a Quote |
| CRAT Knockout A-549 Cell Line | EDJ-KQ23248 | Human | 1384 | Details Get a Quote |
| CRAT Knockout HCT 116 Cell Line | EDJ-KQ23250 | Human | 1384 | Details Get a Quote |
| CRAT Knockout HeLa Cell Line | EDJ-KQ23251 | Human | 1384 | Details Get a Quote |
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