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Trappin protein transglutaminase binding domain. Trappin-2, itself a protease inhibitor, has this unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the 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-catalyzed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyze the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond. Cementoin is associated with the WAP family, pfam00095, at the C-terminus.
No pairwise interactions found for the domain Cementoin
Tips:  If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position. The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs. Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below. Range on the Protein: Protein ID Protein Position Domain Position:  No Conserved Features/Sites Found for Cementoin
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