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. 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. 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 (By similarity). Interacts with NEB (By similarity). Interacts with MYH9 (By similarity). Interacts with MYLK (By similarity). Interacts with TASOR (PubMed:31112734). 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 the heart, tongue and granular cells within the cerebellum. 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). Belongs to the villin/gelsolin family.