Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. May be involved in the remodeling of the actin cytoskeleton. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activating protein on Rho. Genetic variation in MYO9B is the cause of susceptibility to celiac disease type 4 (CELIAC4). It is a multifactorial disorder of the small intestine that is influenced by both environmental and genetic factors. It is characterized by malabsorption resulting from inflammatory injury to the mucosa of the small intestine after the ingestion of wheat gluten or related rye and barley proteins. In its classic form, celiac disease is characterized in children by malabsorption and failure to thrive. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Actin-binding; GAP; GAP, Rac/Rho; Motility/polarity/chemotaxis; Motor
Cellular Component: actin filament; cell cortex; cytoplasm; cytoskeleton; cytosol; filopodium tip; lamellipodium; membrane; myosin complex; perinuclear region of cytoplasm; ruffle
Molecular Function: actin binding; actin filament binding; actin-dependent ATPase activity; ADP binding; ATP binding; ATP-dependent protein binding; ATPase activity; calmodulin binding; GTPase activator activity; metal ion binding; microfilament motor activity; motor activity; nucleotide binding; Rho GTPase binding; Roundabout binding; zinc ion binding
Biological Process: actin filament-based movement; actin-myosin filament sliding; establishment of cell polarity; macrophage chemotaxis; monocyte chemotaxis; positive regulation of GTPase activity; regulation of Rho protein signal transduction; Rho protein signal transduction; signal transduction