A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins) (PubMed:7679927, PubMed:1739747, PubMed:8914854, PubMed:10553002, PubMed:10660572, PubMed:15611369). 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:7679927, PubMed:1739747, PubMed:8914854, PubMed:10553002, PubMed:10660572, PubMed:15611369). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids, the catalytic efficiency decreasing in the following order: dodecanoic > tetradecanoic > (9Z)-octadecenoic > (9Z,12Z)-octadecadienoic > hexadecanoic acid (PubMed:10553002, PubMed:10660572). Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver (PubMed:7679927, PubMed:1739747, PubMed:8914854, PubMed:15611369). Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (PubMed:10620324, PubMed:10660572, PubMed:15611369). Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency (PubMed:7679927). May contribute to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acid, thereby initiating chain shortening (PubMed:18182499). Omega-hydroxylates (9R,10S)-epoxy-octadecanoate stereoisomer (PubMed:15145985). Plays a minor role in omega-oxidation of long-chain 3-hydroxy fatty acids (PubMed:18065749). Has little activity toward prostaglandins A1 and E1 (PubMed:7679927). an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 14-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 22-hydroxydocosanoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-oxodocosanoate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] 22-oxodocosanoate + O2 + reduced [NADPH--hemoprotein reductase] = docosanedioate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (9R,10S)-epoxy-octadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(9R,10S)-epoxy-octadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 3-hydroxyhexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 3,16-dihydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] Activated by cytochrome b5. kcat is 42 min(-1) with dodecanoic acid as substrate. kcat is 50 min(-1) with tetradecanoic acid as substrate. kcat is 10 min(-1) with hexadecanoic acid as substrate. kcat is 0.4 min(-1) with (9Z)-octadecenoic acid as substrate. kcat is 0.4 min(-1) with (5Z,8Z,11Z,14Z)-eicosatetraenoic acid as substrate. Lipid metabolism; arachidonate metabolism. Lipid metabolism; oxylipin biosynthesis. Expressed in liver (PubMed:7679927). Expressed in S2 and S3 segments of proximal tubules in cortex and outer medulla of kidney (PubMed:7679927, PubMed:10660572). CYP4A11v seems to be a rare allelic variant of CYP4A11, it seems to be unstable and not to metabolize lauric acid. Belongs to the cytochrome P450 family. CYP4A11 alleles