TGM3

Protein-glutamine gamma-glutamyltransferase E is an enzyme that in humans is encoded by the TGM3 gene.[5][6][7]

TGM3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1L9M, 1L9N, 1NUD, 1NUF, 1NUG
Identifiers
Aliases	TGM3, TGE, transglutaminase 3, UHS2
External IDs	OMIM: 600238 MGI: 98732 HomoloGene: 20690 GeneCards: TGM3
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20p13 Start 2,296,001 bp[1] End 2,341,079 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 F1 Start 130,012,349 bp[2] End 130,050,399 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • metal ion binding • calcium ion binding • catalytic activity • protein-glutamine gamma-glutamyltransferase activity • transferase activity • transferase activity, transferring acyl groups Cellular component • extrinsic component of cytoplasmic side of plasma membrane • extracellular exosome • cytoplasm Biological process • keratinization • protein tetramerization • hair follicle morphogenesis • cell envelope organization • peptide cross-linking • cellular protein modification process • keratinocyte differentiation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7053	21818
Ensembl	ENSG00000125780	ENSMUSG00000027401
UniProt	Q08188	Q08189
RefSeq (mRNA)	NM_003245	NM_009374
RefSeq (protein)	NP_003236	NP_033400
Location (UCSC)	Chr 20: 2.3 – 2.34 Mb	Chr 2: 130.01 – 130.05 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

For the Tetris game, see Tetris: The Grand Master.

Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene consists of two polypeptide chains activated from a single precursor protein by proteolysis. The encoded protein is involved the later stages of cell envelope formation in the epidermis and hair follicle.[7]

See also

• Proximal promoter

References

1. GRCh38: Ensembl release 89: ENSG00000125780 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027401 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Wang M, Kim IG, Steinert PM, McBride OW (Mar 1995). "Assignment of the human transglutaminase 2 (TGM2) and transglutaminase 3 (TGM3) genes to chromosome 20q11.2". Genomics. 23 (3): 721–2. doi:10.1006/geno.1994.1571. PMID 7851911.
6. Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF (Mar 1998). "Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers". J Biol Chem. 273 (6): 3452–60. doi:10.1074/jbc.273.6.3452. PMID 9452468.
7. "Entrez Gene: TGM3 transglutaminase 3 (E polypeptide, protein-glutamine-gamma-glutamyltransferase)".

Further reading

• Ahvazi B, Boeshans KM, Rastinejad F (2005). "The emerging structural understanding of transglutaminase 3". J. Struct. Biol. 147 (2): 200–7. doi:10.1016/j.jsb.2004.03.009. PMID 15193648.
• Rice RH, Green H (1978). "Relation of protein synthesis and transglutaminase activity to formation of the cross-linked envelope during terminal differentiation of the cultured human epidermal keratinocyte". J. Cell Biol. 76 (3): 705–11. doi:10.1083/jcb.76.3.705. PMC 2110014. PMID 24643.
• Steck TL (1972). "Cross-linking the major proteins of the isolated erythrocyte membrane". J. Mol. Biol. 66 (2): 295–305. doi:10.1016/0022-2836(72)90481-0. PMID 5038456.
• Mariniello L, Esposito C, Di Pierro P, et al. (1993). "Human-immunodeficiency-virus transmembrane glycoprotein gp41 is an amino acceptor and donor substrate for transglutaminase in vitro". Eur. J. Biochem. 215 (1): 99–104. doi:10.1111/j.1432-1033.1993.tb18011.x. PMID 7688299.
• Amendola A, Lombardi G, Oliverio S, et al. (1994). "HIV-1 gp120-dependent induction of apoptosis in antigen-specific human T cell clones is characterized by 'tissue' transglutaminase expression and prevented by cyclosporin A". FEBS Lett. 339 (3): 258–64. doi:10.1016/0014-5793(94)80427-3. PMID 7906657.
• Kim IG, Lee SC, Lee JH, et al. (1994). "Structure and organization of the human transglutaminase 3 gene: evolutionary relationship to the transglutaminase family". J. Invest. Dermatol. 103 (2): 137–42. doi:10.1111/1523-1747.ep12392470. PMID 7913719.
• Kim IG, Gorman JJ, Park SC, et al. (1993). "The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse". J. Biol. Chem. 268 (17): 12682–90. PMID 8099584.
• Lee JH, Jang SI, Yang JM, et al. (1996). "The proximal promoter of the human transglutaminase 3 gene. Stratified squamous epithelial-specific expression in cultured cells is mediated by binding of Sp1 and ets transcription factors to a proximal promoter element". J. Biol. Chem. 271 (8): 4561–8. doi:10.1074/jbc.271.8.4561. PMID 8626812.
• Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
• Kim SY, Grant P, Lee JH, et al. (1999). "Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease". J. Biol. Chem. 274 (43): 30715–21. doi:10.1074/jbc.274.43.30715. PMID 10521460.
• Méhul B, Bernard D, Simonetti L, et al. (2000). "Identification and cloning of a new calmodulin-like protein from human epidermis". J. Biol. Chem. 275 (17): 12841–7. doi:10.1074/jbc.275.17.12841. PMID 10777582.
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Sárdy M, Kárpáti S, Merkl B, et al. (2002). "Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis". J. Exp. Med. 195 (6): 747–57. doi:10.1084/jem.20011299. PMC 2193738. PMID 11901200.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ahvazi B, Boeshans KM, Idler W, et al. (2003). "Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme". J. Biol. Chem. 278 (26): 23834–41. doi:10.1074/jbc.M301162200. PMID 12679341.
• Hitomi K, Presland RB, Nakayama T, et al. (2004). "Analysis of epidermal-type transglutaminase (transglutaminase 3) in human stratified epithelia and cultured keratinocytes using monoclonal antibodies". J. Dermatol. Sci. 32 (2): 95–103. doi:10.1016/S0923-1811(03)00091-4. PMID 12850301.
• Gonzalez HE, Gujrati M, Frederick M, et al. (2003). "Identification of 9 genes differentially expressed in head and neck squamous cell carcinoma". Arch. Otolaryngol. Head Neck Surg. 129 (7): 754–9. doi:10.1001/archotol.129.7.754. PMID 12874078.
• Ahvazi B, Boeshans KM, Idler W, et al. (2004). "Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium". J. Biol. Chem. 279 (8): 7180–92. doi:10.1074/jbc.M312310200. PMID 14645372.