GANC (glucosidase alpha, neutral C) is a member of glycosyl hydrolase family 31 that exhibits alpha-glucosidase activity, capable of releasing terminal glucose from maltotriose and glycogen at neutral pH 1. The enzyme evolved from the α-subunit of GANAB in early vertebrates and localizes to the nucleoplasm and cytoplasm, where it colocalizes with actin filaments 2. GANC demonstrates alpha-1,4-glucosidase activity and participates in N-glycan processing, suggesting roles in carbohydrate metabolism and protein modification. The gene maps to chromosome 15, a region associated with diabetes susceptibility, and exhibits multiple allelic variants including a null allele 1. Functionally, GANC promotes influenza virus replication by inhibiting proteasome-dependent degradation of viral hemagglutinin (HA) protein 3. GANC knockdown facilitates HA degradation through promoting direct binding with proteasome subunits PSMD1 and PSMD2, while genetic variants reduce the enzyme's ability to promote viral replication 3. This dual role in carbohydrate metabolism and viral pathogenesis suggests GANC may serve as both a metabolic enzyme and a host factor influencing influenza A virus infections across multiple strains including H7N9, H9N2, and H1N1.