CPT1A

A conformation change in the N-terminal region spanning the first 42 residues plays an important role in the regulation of enzyme activity by malonyl-CoA.

Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion (PubMed:11350182, PubMed:14517221, PubMed:16651524, PubMed:9691089). Possesses also a lysine succinyltransferase activity that can regulate enzymatic activity of substrate proteins such as ENO1 and metabolism independent of its classical carnitine O-palmitoyltransferase activity (PubMed:29425493). Plays an important role in hepatic triglyceride metabolism (By similarity). Plays also a role in inducible regulatory T-cell (iTreg) differentiation once activated by butyryl-CoA that antagonizes malonyl-CoA-mediated CPT1A repression (By similarity). Sustains the IFN-I response by recruiting ZDHCC4 to palmitoylate MAVS at the mitochondria leading to MAVS stabilization and activation (PubMed:38016475). Promotes ROS-induced oxidative stress in liver injury via modulation of NFE2L2 and NLRP3-mediated signaling pathways (By similarity).

Carnitine palmitoyltransferase 1A deficiency

CPT1AD

Rare autosomal recessive metabolic disorder of long-chain fatty acid oxidation characterized by severe episodes of hypoketotic hypoglycemia usually occurring after fasting or illness. Onset is in infancy or early childhood.

None

The disease is caused by variants affecting the gene represented in this entry.

Lipid metabolism; fatty acid beta-oxidation.

Belongs to the carnitine/choline acetyltransferase family.

Strong expression in kidney and heart, and lower in liver and skeletal muscle.

• Mitochondrion outer membrane
• Multi-pass membrane protein

CPT1, CPT1A, CPT1-L, Carnitine palmitoyltransferase 1A, Succinyltransferase CPT1A, CPT I, CPTI-L

• entrezGene:1374
• omim:600528
• swissprot:P50416

Proteins

Immunology & Infectious Disease

88368Da