Protein Domain : Trappin protein transglutaminase-binding repeat IPR019541

Type	Repeat
Description	Trappin-2,a protease inhibitor, has a unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase [ ]. This domain contains several repeated motifs (rpresented by this entry) with the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalysed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyse the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond []. Cementoin is associated with the WAP family, , at the C terminus.
Short Name	Trappin_transglut-bd_rpt