Interferon-induced dynamin-like GTPase with antiviral activity against influenza A virus, (IAV). Inhibits IAV replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Homooligomer. Oligomerizes into multimeric filamentous or ring-like structures by virtue of its stalk domain. Oligomerization is critical for GTPase activity, protein stability, and recognition of viral target structures (By similarity). Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7 (By similarity). Interacts with HSPA5 (By similarity). Interacts with TUBB/TUBB5 (By similarity). Interacts with DDX39A and DDX39B (By similarity). Binds preferentially to negatively charged phospholipids. By type I and type III interferons. The C-terminal GTPase effector domain (GED) is involved in oligomerization and viral target recognition. The middle domain mediates self-assembly and oligomerization. ISGylated. Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.