Severs actin filaments and accelerates their polymerization and depolymerization. Phosphate inhibits both the depolymerization and severing activities. Interacts with actin at the FH2 domain. Interacts with DAAM2 (PubMed:33232676). Widely expressed. In the kidney, expression is apparent in podocytes and some tubule cells. The WH2 domain acts as the DAD (diaphanous autoregulatory) domain and binds to actin monomers. Regulated by autoinhibition due to intramolecular GBD-DAD binding. The severing activity is dependent on covalent attachment of the FH2 domain to the C-terminus. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the formin homology family. Extended N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated C-terminus.