Transglutaminase 7 (TGM7)

Transglutaminases (TGM; EC 2.3.2.13) are a family of structurally and functionally related enzymes that stabilize protein assemblies through the formation of gamma-glutamyl-epsilon lysine crosslinks.

Grenard et al. (2001) cloned a novel TGM cDNA, designated TGM7, by RT-PCR and anchored PCR of human prostate carcinoma tissues and cells, using degenerate primers based on the conserved active site sequence. The deduced 710-amino acid protein has a calculated molecular mass of about 80 kD. TGM7 contains a conserved cys-his-asp catalytic triad and a calcium-binding domain. Its core domain shares 50% sequence identity with other TGMs. Northern dot blot analysis detected ubiquitous low level expression of TGM7, with highest levels in testis and lung.