Fatty acid hydroxylase domain-containing protein 2 (FAXDC2)

Fatty acid hydroxylase domain-containing protein 2 (FAXDC2) is an enzyme that participates in the modulation of cholesterol and sphingolipid biosynthesis. It acts as a C4-methyl sterol oxidase—catalyzing the demethylation step of specific intermediates (such as lophenol and dihydro-T-MAS) within the downstream 'Kandutsch-Russell' arm of the cholesterol biosynthetic pathway. FAXDC2 is structurally related to MSMO1 and is conserved across animals and plants. Functionally, it influences the abundance of bioactive sterols which serve as signaling molecules, and it regulates major cellular pathways (notably Wnt/β-catenin and MAPK/ERK signaling). FAXDC2 expression is significantly altered in several cancers, often being repressed in tumors with high Wnt signaling and associated with unfavorable prognosis in liver cancer; overexpression can suppress tumor cell proliferation and invasion through S-phase cell cycle arrest and attenuation of ERK phosphorylation. No targeted therapeutic drugs or specific inhibitors are known as of this writing. Key enzyme activities of FAXDC2 include oxidoreductase function (iron-binding, monooxygenase-type), and its aberrant regulation may play a role in oncogenesis and progression, particularly in cancers with altered lipid/cholesterol metabolism.

Other names

C5orf4FLJ13758fatty acid hydroxylase domain containing 2

Not applicable (for drugs), but FAXDC2’s own enzymatic mechanism involves C4-demethylation of sterol intermediates as part of cholesterol biosynthesis.