Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch. May regulate the EFNA5-EPHA3 signaling.
Specificity
Natural and recombinant Bovine Disintegrin and metalloproteinase domain-containing protein 10
Subcellular Location
Golgi apparatus membrane Single-pass type I membrane protein Cell membrane Single-pass type I membrane protein The protealytically actived form is localized mainly in the plasma membrane whereas the proenzyme is found intracellularly in the Golgi.
Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts with EPHA2.
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Reviews of ELISA Kit for Bovine Disintegrin and metalloproteinase domain-containing protein 10