Abstract: The study investigates the structure and expression features of Pomacea canaliculata cytochrome P450, and explores the correlation of metaldehyde treatment and cytochrome P450 expression level. A full-length cDNA of CYP3192A1 from P.canaliculata with total length of 2 523 bp was obtained by RACE, including an open reading frame (ORF) encoding 517 amino acids, which had a heme-binding domain F**G*** C*G, helix K(E**R), helix I(AG*ET), helix C(W***R) and trans-membrane helix(12~34 amino acids).Blast and phylogenetic analyses suggest P.canaliculata CYP3192A1 is a member of a novel CYP450 family, with high similarity with CYP3A subfamily. The RT-qPCR suggests that CYP3192A1 has gender-specific and tissue specific expression(P < 0.05). Expression in female P.canaliculata was higher than in males; expression amounts in intestinal and gill were the highest, followed by those in liver and stomach, and were the lowest in heart and pleopod. The influence of metaldehyde to CYP3192A1 expression shows a trend of induction at low concentration, shortened and advanced induction period at high concentration. It is demonstrated that there is close correlation between CYP3192A1 expression and metaldehyde treatment, and the induced expression of CYP3192A1 might play an important role in metaldehyde metalbolism.