Diaphanous autoregulatory (DAD) domain (IPR014767)

Short name: DAD_dom

Overlapping homologous superfamilies


Domain relationships


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 IPR000225) in the DID or GBD/FH3 domain [PMID: 15950879, PMID: 15740615, PMID: 16292343]. 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 alpha-helical structure and the C-terminal part of the domain contains several basic residues that form a basic region [PMID: 16292343, PMID: 16472745, PMID: 11035012, PMID: 16361707].

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).

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles