The adzuki bean borer moth, Ostrinia scapulalis, uses a mixture of (E)-11- and (Z)-11-tetradecenyl acetates as a sex pheromone. At a step in the pheromone biosynthetic pathway, fatty-acyl precursors are converted to corresponding alcohols by an enzyme, fatty-acyl reductase (FAR). Here we report the cloning of FAR-like genes expressed in the pheromone gland of female O. scapulalis, and the characterization of a single pheromone-gland-specific FAR (pgFAR) and its functional assay using an insect cell expression system. As many as thirteen FAR-like genes (FAR-I-FAR-XIII) were expressed in the pheromone gland of O. scapulalis; however, only one (FAR-XIII) was pheromone-gland-specific. The deduced amino acid sequence of FAR-XIII predicted a 462-aa protein with a conserved NAD(P)H-binding motif in the N-terminal region, showing overall identity of 34% with the pgFAR of Bombyx mori. A functional assay using Sf9 cells transfected with an expression vector containing the open reading frame of the FAR-XIII gene has proven that FAR-XIII protein has the ability to convert a natural substrate, (Z)-11-tetradecenoic acid, to a corresponding alcohol, (Z)-11-tetradecenol.