mDia12

mDia12 is not a widely recognized or independently validated gene or protein in major public databases. In most contemporary references, the mammalian diaphanous-related formin (mDia) family is represented by DIAPH1, DIAPH2, and DIAPH3, corresponding to mDia1, mDia2, and mDia3. If the label mDia12 appears in some literature, it is often an informal alias, a localized nomenclature, or a reference to a particular splice variant or cross-species annotation rather than a universally accepted separate gene.

Proteins in the diaphanous-related formin family are actin nucleators and elongation factors that regulate the assembly and organization of the actin cytoskeleton. They typically share a conserved domain structure that includes a GTPase-binding domain (GBD) at the N terminus, a diaphanous inhibitory domain (DID), a coiled-coil region, and the actin-regulating FH1 and FH2 domains, with some isoforms also featuring additional motifs. Activity is tightly controlled by autoinhibition, which can be relieved by binding to Rho family GTPases, enabling interaction with profilin and other actin regulators to promote filament formation and processive elongation.

Biologically, mDia family proteins influence processes such as cell shape changes, polarity, cytokinesis, and directed cell migration, as well as vesicle trafficking and neurite outgrowth in certain contexts. Given the ambiguity around the term mDia12, researchers are advised to verify the intended gene or isoform in the relevant organism and to consult established databases (such as NCBI Gene or UniProt) for precise nomenclature and annotations.