Predicted to react with Mouse and Rat samples.
The protein encoded by this gene belongs to the myosin superfamily. Myosins are molecular motors that, upon interaction with actin filaments, utilize energy from ATP hydrolysis to generate mechanical force. Each myosin has a conserved N-terminal motor domain that contains both ATP-binding and actin-binding sequences. Following the motor domain is a light-chain-binding 'neck' region containing 1-6 copies of a repeat element, the IQ motif, that serves as a binding site for calmodulin or other members of the EF-hand superfamily of calcium-binding proteins. At the C-terminus, each myosin class has a distinct tail domain that serves in dimerization, membrane binding, protein binding, and/or enzymatic activities and targets each myosin to its particular subcellular location. The kidney epithelial cell line, LLC-PK1-CL4 (CL4), forms a well ordered brush border (BB) on its apical surface. Experiments indicate that the brush border population of the encoded protein turns over rapidly, while its head and tail domains interact transiently with the core actin and plasma membrane, respectively. A rapidly exchanging pool of the protein encoded by this gene envelops an actin core bundle that, by comparison, is static in structure.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: BBM-I; BBMI; brush border myosin 1; Brush border myosin I; brush border myosin-I; MIHC; myosin heavy polypeptide 1 skeletal muscle adult; Myosin I heavy chain; myosin, heavy polypeptide-like (100kD); myosin, heavy polypeptide-like (110kD); myosin-Ia; Unconventional myosin-Ia
Gene Aliases: BBM-I; BBMI; DFNA48; MIHC; Myh1; MYHL; MYO1A
Molecular Function: actin binding motor protein