B3GAT3

From Wikipedia, the free encyclopedia

Beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I)

PDB rendering based on 1fgg.

Available structures: 1fgg, 1kws

Identifiers

Symbol(s)

B3GAT3; GLCATI; GlcAT-I

External IDs

OMIM: 606374 MGI: 1919977 HomoloGene: 56554

Gene ontology
Molecular Function:	• galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity • transferase activity • manganese ion binding • metal ion binding
Cellular Component:	• Golgi membrane • membrane • integral to membrane
Biological Process:	• glycosaminoglycan biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012200 (mRNA)
NP_036332 (protein)

NM_024256 (mRNA)
NP_077218 (protein)

Location

Chr 11: 62.14 - 62.15 Mb

Chr 19: 8.99 - 8.99 Mb

Pubmed search

[1]

[2]

Beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I), also known as B3GAT3, is a human gene.^[1]

The protein encoded by this gene is a member of the glucuronyltransferase gene family, enzymes that exhibit strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. This gene product catalyzes the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans.^[1]

[edit] References

^ ^a ^b Entrez Gene: B3GAT3 beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I).

[edit] Further reading

Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514.
Venkatesan N, Barré L, Benani A, et al. (2005). "Stimulation of proteoglycan synthesis by glucuronosyltransferase-I gene delivery: a strategy to promote cartilage repair.". Proc. Natl. Acad. Sci. U.S.A. 101 (52): 18087-92. doi:10.1073/pnas.0404504102. PMID 15601778.
Gulberti S, Lattard V, Fondeur M, et al. (2005). "Phosphorylation and sulfation of oligosaccharide substrates critically influence the activity of human beta1,4-galactosyltransferase 7 (GalT-I) and beta1,3-glucuronosyltransferase I (GlcAT-I) involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans.". J. Biol. Chem. 280 (2): 1417-25. doi:10.1074/jbc.M411552200. PMID 15522873.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Gulberti S, Fournel-Gigleux S, Mulliert G, et al. (2003). "The functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif.". J. Biol. Chem. 278 (34): 32219-26. doi:10.1074/jbc.M207899200. PMID 12794088.
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. PMID 12477932.
Kitagawa H, Taoka M, Tone Y, Sugahara K (2001). "Human glycosaminoglycan glucuronyltransferase I gene and a related processed pseudogene: genomic structure, chromosomal mapping and characterization.". Biochem. J. 358 (Pt 3): 539-46. PMID 11535117.
Pedersen LC, Tsuchida K, Kitagawa H, et al. (2000). "Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I.". J. Biol. Chem. 275 (44): 34580-5. doi:10.1074/jbc.M007399200. PMID 10946001.
Ouzzine M, Gulberti S, Netter P, et al. (2000). "Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues.". J. Biol. Chem. 275 (36): 28254-60. doi:10.1074/jbc.M002182200. PMID 10842173.
Tone Y, Kitagawa H, Imiya K, et al. (1999). "Characterization of recombinant human glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans.". FEBS Lett. 459 (3): 415-20. PMID 10526176.
Herman T, Horvitz HR (1999). "Three proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathway.". Proc. Natl. Acad. Sci. U.S.A. 96 (3): 974-9. PMID 9927678.
Kitagawa H, Tone Y, Tamura J, et al. (1998). "Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans.". J. Biol. Chem. 273 (12): 6615-8. PMID 9506957.