Search by BoMiProt ID - Bomi26

Primary Information

BoMiProt ID Bomi26
Protein Name Moesin
Organism Bos taurus
Uniprot IDQ2HJ49
Milk FractionWhey
Ref Sequence ID NP_001039942.1
Aminoacid Length 577
Molecular Weight 67975
FASTA Sequence Download
Gene Name MSN
Gene ID 540426
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

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
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions 375-409,466-518
DisProt Annotation
TM Helix Prediction No TM helices
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.