|Ref Sequence Id||NP_001039942.1|
|Amino Acid Lenth||577|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||bovine uterus smooth muscle cells, microvilli, filopodia, uropods, ruffling membranes, retraction fibers, the cleavage furrow of dividing cells, and adhesion sites where actin filaments are associated with the plasma membrane|
|Protein Function||heparin-binding protein; interacted with CD43; increased expression is necessary during epithelial-mesenchymal transition for efficient actin filament remodeling, and for cortical relocalization of adhesion and contractile elements|
|Biochemical Properties||an N-terminal membrane binding domain (FERM domain), which can bind the membrane via phosphatidylinositol (4,5)-bisphosphate (PIP2), a α-helical linker region and a C-terminal actin-binding domain; Moesin and ezrin show similar affinities for PIP2; both ezrin and moesin were more rapidly degraded by chymotrypsin after binding to PIP2-LUVs|
|Significance in milk||Ezrin-radixin-moeisin binding phosphoprotein is required for the development of lactating mammary glands|
|Additional Comments||high degree of homology among ERM members; tissue distribution and primary structures are different for the ERM proteins; of all ERM proteins, moesin is the only one present in platelets|
|Bibliography||1. Franck, Z., Gary, R., & Bretscher, A. (1993). Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable. Journal of Cell Science, 105(1). |
2. Bretscher, A., Gary, R., & Berryman, M. (1995). Soluble Ezrin Purified from Placenta Exists as Stable Monomers and Elongated Dimers with Masked C-Terminal Ezrin-Radixin-Moesin Association Domains. Biochemistry, 34(51), 16830–16837. https://doi.org/10.1021/bi00051a034.
3. Sato, N., Funayama, N., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S. (1992). A gene family consisting of ezrin, radixin and moesin. Journal of Cell Science, 103, 131–143.