GDPD1 (glycerophosphodiester phosphodiesterase domain containing 1) is a lipid-metabolizing enzyme that hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and corresponding amines 12. The enzyme shows substrate preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE), and lysophosphatidylcholine (lyso-PC), and participates in bioactive N-acylethanolamine biosynthesis 12. GDPD1 expression is predominantly localized to the ovary and small intestine 3. Mechanistically, GDPD1 mRNA stability is regulated by the RNA-binding protein hnRNP Q1; viral infection can destabilize GDPD1 mRNA through hnRNP Q1 degradation, promoting aerobic glycolysis in cancer contexts 4. Clinically, structural variants affecting GDPD1 regulatory elements cause autosomal dominant retinitis pigmentosa type 17 (RP17). These variants create neo-topologically associating domains (neo-TADs) enabling ectopic contact between retinal enhancers and the GDPD1 promoter, resulting in increased retinal GDPD1 expression through a dominant gain-of-function mechanism 56. Notably, GDPD1 knockout mice remain fertile, suggesting non-essential roles in reproductive fertility 7.