InterPro domain: IPR013111

A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown [ 1 , 2 , 3 , 4 ] to be present, in a moreor less conserved form, in a large number of other, mostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However, a common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.

This entry contains EGF domains found in a variety of extracellular and membrane proteins

1. Structure and function of epidermal growth factor-like regions in proteins. FEBS Lett. 231, 1-4
2. Computer-based characterization of epidermal growth factor precursor. Nature 307, 558-60
3. The many faces of epidermal growth factor repeats. New Biol. 2, 410-9
4. Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors. Proc. Natl. Acad. Sci. U.S.A. 81, 7363-7