TGM3

TGM3

Identifiers

TGM3, TGE, transglutaminase 3, UHS2

External IDs

OMIM: 600238; MGI: 98732; GeneCards: TGM3

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1L9M, 1L9N, 1NUD, 1NUF, 1NUG

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
2.3.2.13	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 20 (human)

Band	20p13	Start	2,296,001 bp
Band	20p13	End	2,341,079 bp

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)

Band	2\|2 F1	Start	129,854,269 bp
Band	2\|2 F1	End	129,892,319 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

skin of leg

skin of abdomen

right uterine tube

tonsil

minor salivary glands

vagina

ectocervix

gallbladder

blood

granulocyte

Top expressed in

esophagus

left colon

lip

superior surface of tongue

granulocyte

hair follicle

skin of back

skin of abdomen

trachea

pretectal area

More reference expression data


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

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


7053


21818


ENSG00000125780


ENSMUSG00000027401


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

View/Edit Human

View/Edit Mouse

Protein-glutamine gamma-glutamyltransferase E is an enzyme that in humans is encoded by the TGM3 gene.

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.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000125780 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027401 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "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.

PDB gallery

1l9m: Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
1l9n: Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
1nud: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme (3 calciums, active form)
1nuf: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme
1nug: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme (2 calciums, 1 Mg, inactive form)
1rle: Structural Basis for the Coordinated Regulation of Transglutaminase 3 by Guanine Nucleotides and Calcium/Magnesium
1sgx: Crystal Structure of Transglutaminase 3 in Complex with Bound GMP: Structural Basis for Alteration in Nucleotide Specificity
1vjj: Structural Basis for the Coordinated Regulation of Transglutaminase 3 by Guanine Nucleotides and Calcium/Magnesium

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