TGM3

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 129,854,269 bp [2] End 129,892,319 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of abdomen right uterine tube thymus minor salivary gland vagina gallbladder blood right coronary artery fundus right lobe of liver Top expressed in esophagus left colon lip superior surface of tongue hair follicle skin of back skin of abdomen trachea pretectal area condyle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding calcium ion binding catalytic activity protein-glutamine gamma-glutamyltransferase activity transferase activity acyltransferase activity 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 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: 129.85 – 129.89 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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

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. S2CID   39872629.
• 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. doi: 10.1016/S0021-9258(18)31442-X . 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. Bibcode:2001Natur.414..865D. 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. Bibcode:2002PNAS...9916899M. 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.