Primary Information
BoMiProt ID	Bomi17
Protein Name	Ezrin
Organism	Bos taurus
Uniprot ID	P31976
Milk Fraction	Whey
Ref Sequence ID	NP_776642.1
Aminoacid Length	581
Molecular Weight	68760
FASTA Sequence	Download
Gene Name	EZR
Gene ID	281574
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Presence in other biological fluids/tissue/cells	localized at the plasma membrane in actin-rich surface structures such as microvilli, membrane ruffles, and lamellipodia in gut cells, lymphocytes, hepatocytes, spermatozoids, fibroblasts and in a variety of other cell types
Protein Function	Member of ERM proteins; morphogenesis, cancer metastasis and virus infection; establishment of cell polarity, cell motility and cell signaling; linkers between the plasma membrane and the cortical actin cytoskeleton; crucial molecule in the dissemination of two pediatric tumors, rhabdomyosarcoma and osteosarcoma; overexpression increased migration of metastatic melanoma; interaction with podocalyxin increase the invasiveness of cancer cells; involved in the functional localization of PKA; regulates the structure of the cortical cytoskeleton to control cell surface topography
Biochemical Properties	N-terminal domain of ezrin associates with the membrane, whereas the C-terminal half links it to the cytoskeleton; substrates for certain tyrosine kinases;ezrin in soluble extracts of intestinal or placental tissues is monomeric; presence of polyproline stretch
Significance in milk	maintainence of 3 dimensional structure of matrix which is required in both cell survival and differentiation has been well documented for mammary gland epithelial cells
PTMs	Phosphorylated; C-terminal threonine phosphorylation
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	(471-499)
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	Phosphorylation of ezrin is required for both conformational activation and for signaling to downstream events
Additional Comments	originally purified from the microfilament bundle of isolated intestinal microvilli, yet the native protein possessed no convincing F-actin binding activity
Bibliography	1. Algrain, M., Turunen, O., Vaheri, A., Louvard, D., & Arpin, M. (1993). Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. The Journal of Cell Biology, 120(1), 129–139. https://doi.org/10.1083/jcb.120.1.129. 2. Dransfield, D. T., Bradford, A. J., Smith, J., Martin, M., Roy, C., Mangeat, P. H., & Goldenring, J. R. (1997). Ezrin is a cyclic AMP-dependent protein kinase anchoring protein. EMBO Journal, 16(1), 35–43. https://doi.org/10.1093/emboj/16.1.35. 3. Bretscher, A. (1983). Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. The Journal of Cell Biology, 97(2), 425–432. https://doi.org/10.1083/jcb.97.2.425. 4. Gautreau, A., Poullet, P., Louvard, D., & Arpin, M. (1999). Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway. Proceedings of the National Academy of Sciences of the United States of America, 96(13), 7300–7305. https://doi.org/10.1073/pnas.96.13.7300. 5. Srivastava, J., Elliott, B. E., Louvard, D., & Arpin, M. (2005). Src-dependent ezrin phosphorylation in adhesion-mediated signaling. Molecular Biology of the Cell, 16(3), 1481–1490. https://doi.org/10.1091/mbc.e04-08-0721