A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and their oxygenated derivatives (oxylipins) (PubMed:15364545, PubMed:18065749, PubMed:24138531, PubMed:37373382). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:15364545, PubMed:18065749, PubMed:24138531, PubMed:37373382). Catalyzes with high efficiency the oxidation of the terminal carbon (omega-oxidation) of 3-hydroxy fatty acids, such as 3- hydroxyhexadecanoic and 3-hydroxyoctadecanoic acids, likely participating in the biosynthesis of long-chain 3-hydroxydicarboxylic acids (PubMed:18065749, PubMed:19932081). Omega-hydroxylates and inactivates phylloquinone (vitamin K1), and menaquinone-4 (MK-4, a form of vitamin K2), both acting as cofactors in blood coagulation (PubMed:24138531). Metabolizes with low efficiciency fatty acids, including (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) and its oxygenated metabolite 8-hydroxyeicosatetraenoic acid (8-HETE) (PubMed:15364545, PubMed:19932081). Catalyzes N- and O-demethylation of drugs such as erythromycin, benzphetamine, ethylmorphine, chlorpromazine, imipramine and verapamil (PubMed:15364545). Catalyzes the oxidation of dialkylresorcinol 2 (PubMed:36565673). {ECO:0000269|PubMed:15364545, ECO:0000269|PubMed:18065749, ECO:0000269|PubMed:19932081, ECO:0000269|PubMed:24138531, ECO:0000269|PubMed:36565673, ECO:0000269|PubMed:37373382}. This is the function of CYP4F11 (cytochrome P450 family 4 subfamily F member 11, ENSG00000171903).