| Primary Identifier | IPR041161 | Type | Domain |
| Short Name | EGF_Tenascin |
| description | This entry represents the EGF-like domains found in Tenascin and Reelin proteins. A common feature of all EGF-like domains is that they are found in theextracellular domain of membrane-bound proteins or in proteins known to besecreted (exception: prostaglandin G/H synthase). The EGF-like domain includessix cysteine residues which have been shown to be involved in disulfide bonds.The structure of several EGF-like domains has been solved. The fold consistsof two-stranded β-sheet followed by a loop to a C-terminal shorttwo-stranded sheet []. Tenascins are extracellular matrix glycoproteins that act both as integrin ligands and as modifiers of fibronectin-integrin interactions to regulate cell adhesion, migration, proliferation and differentiation. Tenascins are usually composed of repeated epidermal growth factor (EGF)-like domains, fibronectin-type III (FNIII) domains and a C-terminal fibrinogen related domain (FReD) [].Reelin is an extracellular matrix serine protease that regulates neuronal migration during embryonic development and acts as a modulator of synaptic transmission in the adult brain []. Reelin acts on its receptors, VLDLR and ApoER2, acting on cytoskeleton, controlling migration and subsequently positioning and stabilizing the cortical neurons [, , ]. In the adult brain, reelin stabilizes the actin cytoskeleton by inducing cofilin phosphorylation. Decreased Reelin expression causes destabilization of neurons, which could have implications for brain disorders, such as epilepsy and schizophrenia []. |
