Pathways & interactions
Protein-glutamine gamma-glutamyltransferase, animal (IPR023608)
Short name: Transglutaminase_animal
Overlapping homologous superfamilies
- Transglutaminase-like superfamily (IPR036985)
- Protein-glutamine gamma-glutamyltransferase, animal (IPR023608)
- Coagulation factor XIII A chain (IPR034810)
This entry includes a group of transglutaminases from animals.
Transglutaminases catalyse the post-translational modification of proteins at glutamine residues, with formation of isopeptide bonds. Members of the transglutaminase family usually have three domains: N-terminal, middle and C-terminal. The middle domain is usually well conserved, but family members can display major differences in their N- and C-terminal domains, although their overall structure is conserved [PMID: 10411627].
The best known transglutaminase is blood coagulation factor XIII, a plasma tetrameric protein composed of two catalytic A subunits and two non-catalytic B subunits. Factor XIII is responsible for cross-linking fibrin chains, thus stabilising the fibrin clot. Protein-glutamine gamma-glutamyltransferases (EC:184.108.40.206) are calcium-dependent enzymes that catalyse the cross-linking of proteins by promoting the formation of isopeptide bonds between the gamma-carboxyl group of a glutamine in one polypeptide chain and the epsilon-amino group of a lysine in a second polypeptide chain. TGases also catalyse the conjugation of polyamines to proteins [PMID: 1683845, PMID: 1974250].
- PIRSF000459 (TGM_EBP42)