fascin-like domain, beta-trefoil fold, found in the hisactophilin subfamily
Hisactophilin is a histidine-rich actin-binding protein from Dictyostelium discoideum. It exists in two isoforms, hisactophilin-1 (HatA, also called HS I) and hisactophilin-2 (HatB, also called HS II), which are both myristoylated and distributed between plasma membrane and cytoplasm. Hisactophilin may act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. Hisactophilin contains a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.
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