EBPL (EBP-like) is a 23.2 kDa protein encoded on human chromosome 13.2 that localizes to the endoplasmic reticulum 1. Despite 31% amino acid identity to emopamil-binding protein (EBP), EBPL lacks sterol delta8-delta7 isomerase activity and does not bind sigma ligands, distinguishing it functionally from EBP 1. The protein is ubiquitously expressed with highest abundance in liver, lung, and kidney tissues 1. EBPL undergoes homodimerization and is evolutionarily conserved in animals but absent from plants 1. Notably, EBPL expression is not coordinated with cholesterol biosynthesis regulation, unlike EBP, suggesting a distinct cellular function 1. In disease contexts, EBPL shows relevance to rheumatoid arthritis susceptibility through transcriptome-wide association studies, with expression changes detected across multiple tissue types and involvement in endoplasmic reticulum organization and immune response pathways 2. Additionally, computational studies indicate EBPL is a binding target for environmental toxicants including chlorinated polyfluoroalkyl ether sulfonates 3, though the functional significance of these interactions requires experimental validation. The precise biological function of EBPL remains unknown 1.