TGM7

TGM7 (transglutaminase 7, TG7; also known as transglutaminase Z) belongs to the transglutaminase family of protein cross-linking enzymes that catalyze the formation of protein cross-links and the conjugation of polyamines to proteins^[1][2]. As a member of the transglutaminase superfamily, TGM7 is associated with the conserved biochemical process of protein stabilization through transamidation reactions, a core mechanism shared across transglutaminase family members^[2][1]. Genomic analyses identified TGM7 as a distinct transglutaminase gene located within a gene cluster on chromosome 15q15.2 together with TGM5 and EPB42, supporting its evolutionary origin through local gene duplication events^[1]. A full-length TGM7 cDNA encodes a protein of approximately 710 amino acids with a predicted molecular mass of about 80 kDa, and transcript analyses demonstrated differential expression across human tissues^[1]. Unlike the better-characterized transglutaminase isoforms such as TGM2, TGM5, and TGM6, the biological functions, signaling mechanisms, and disease-associated roles of TGM7 remain comparatively underexplored^[2]. Available expression data indicate that TGM7 exhibits tissue-specific distribution, including expression in lung and testicular tissues, suggesting specialized physiological functions distinct from related transglutaminase family members^[1][3]. Current literature provides limited mechanistic evidence linking TGM7 directly to defined pathological pathways or validated experimental disease models, highlighting the need for further functional studies to clarify its biological significance and potential research applications^[2].