Primary Information |
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| BoMiProt ID | Bomi26 |
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| Protein Name | Moesin |
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| Organism | Bos taurus |
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| Uniprot Id | Q2HJ49 |
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| Milk Fraction | Whey |
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| Ref Sequence Id | NP_001039942.1 |
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| Amino Acid Lenth | 577 |
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| Molecular Weight | 67975 |
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| Fasta Sequence | https://www.uniprot.org/uniprot/Q2HJ49.fasta |
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| Gene Name | MSN |
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| Gene Id | 540426 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondry Information |
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| 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 |
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| 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 |
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| 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 |
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| Significance in milk | Ezrin-radixin-moeisin binding phosphoprotein is required for the development of lactating mammary glands |
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| 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 |
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| 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. |
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