Epidermal growth factor (EGF) is a small mitogenic protein that is thought to be involved in mechanisms such as normal cell growth, oncogenesis, and wound healing. This protein shows both strong sequential and functional homology with human type-alpha transforming growth factor (hTGF alpha), which is a competitor for EGF receptor sites. EGF receptors are expressed in almost all types of tissues. Parietal endoderm, mature skeletal muscles, and hematopoietic tissues do not express the receptor. The EGF receptor, designated HER1, is a 170 kDa transmembrane glycoprotein with a length of 1186 amino acids. It is identical with a previously described glycoprotein called SA-7 (species antigen 7). The extracellular receptor domain has a length of 621 amino acids, including 11 glycosylated asparagine residues and 51 cysteine residues. This domain contains the EGF binding site and also binds mammalian TGF-alpha.