| Description | Formins participate in the assembly of the actin and microtubule cytoskeletons in processes like cell division, migration, and development. Diaphanous-related formins (DRF) contain an N-terminal GTPase-binding domain (GBD) and a C-terminal diaphanous autoregulatory domain (DAD). DRFs are regulated by an autoinhibitory interaction of the C-terminal DAD with the DRF N-terminal armadillo repeat-like region (see ) in the DID or GBD/FH3 domain [ , , ]. This autoinhibition is released upon competitive binding of an activated Rho GTPase to the GBD. The release of DAD allows the catalytical formin homology 2 (FH2) domain to then nucleate and elongate nonbranched actin filaments.The DAD domain is a ~32 amino acid autoinhibitory domain, which facilitates intramolecular binding. The DAD core forms an α-helical structure and the C-terminal part of the domain contains several basic residues that form a basic region [ , , , ].Proteins known to contain a DAD domain include:Fruit fly protein diaphanous, which plays an important role during cytokinesis.Mammalian diaphanous-related formins (DRF) 1-3, which act as Rho GTPase effectors during cytoskeletal remodelling.Saccharomyces cerevisiae (Baker's yeast) proteins BNI1 and BNI1-related protein 1 (BNR1).Emericella nidulans (Aspergillus nidulans) cytokinesis protein sepA, which participates in two actin-mediated processes, septum formation and polarized growth.Mammalian disheveled-associated activator of morphogenesis (DAAM) proteins.Mammalian formin-like 1 protein (Fmnl1) or formin-related protein gene in leukocytes (FRL). | Name | Diaphanous autoregulatory (DAD) domain |
| Short Name | DAD_dom | Type | Domain |
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