FAR1 (fatty acyl-CoA reductase 1) catalyzes the reduction of saturated and unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols, functioning as the rate-limiting enzyme in ether lipid biosynthesis 1. These fatty alcohols are essential substrates for the synthesis of plasmalogens and ether-linked phospholipids, which are incorporated into cellular membranes across multiple tissues 2. FAR1 also supports wax monoester production through the same fatty alcohol intermediates 3. The enzyme localizes primarily to peroxisomes but can adopt alternative membrane topologies and relocalize to lipid droplets under conditions of elevated triglyceride synthesis 4. FAR1 has emerged as a critical mediator of ferroptosis, a form of iron-dependent cell death. A peroxisome-driven ether-lipid biosynthetic axis involving FAR1 controls ferroptosis sensitivity, particularly in response to saturated fatty acids 5. This function has clinical relevance to acute kidney injury (AKI), where reduced FAR1 expression in renal tissue correlates with increased ferroptosis markers and cell death; conversely, FAR1 overexpression in kidney cells suppresses ferroptosis-related phenotypes 6. Pathogenic variants in FAR1 cause distinct neurological disease. Heterozygous de novo variants at position 480 cause autosomal dominant spastic paraparesis, bilateral cataracts, and developmental delay through gain-of-function mechanisms that disrupt plasmalogen-dependent feedback regulation, leading to uncontrolled ether lipid synthesis 2. In contrast, biallelic loss-of-function variants result in plasmalogen deficiency. FAR1 represents a potential therapeutic target for ferroptosis-related disorders including cancer and ischemic stroke.