Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). Associates with F-actin (PubMed:9867483). Interacts with NEB (PubMed:18639526). Interacts with MYH9 (By similarity). Interacts with MYLK (By similarity). Interacts with TASOR (By similarity). Interacts with TRIP6 (By similarity). Interacts with DYNLT1 (By similarity). Interacts with KIF14; at midbody during cytokinesis (By similarity). Tightly associated with both actin filaments and plasma membranes. Expressed in many tissues. Most abundant in muscle, bone marrow, thyroid gland and salivary gland. Isoform 1 (archvillin) is muscle specific. As opposed to other villin-type headpiece domains, supervillin HP (SVHP) doesn't bind F-actin due to the absence of a conformationally flexible region (V-loop). The disease is caused by variants affecting the gene represented in this entry. Belongs to the villin/gelsolin family.