Post Translational Modifications | N-glycosylated. |
Function | Glycosaminoglycans biosynthesis. Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation. |
Protein Name | Galactosylgalactosylxylosylprotein 3-Beta-Glucuronosyltransferase 3Beta-1 -3-Glucuronyltransferase 3Glucuronosyltransferase IGlcat-IUdp-Glcua -Gal Beta-1 -3-Gal-R GlucuronyltransferaseGlcuat-I |
Database Links | Reactome: R-HSA-1971475Reactome: R-HSA-3560801 |
Cellular Localisation | Golgi Apparatus MembraneSingle-Pass Type Ii Membrane ProteinGolgi ApparatusCis-Golgi Network |
Alternative Protein Names | Galactosylgalactosylxylosylprotein 3-Beta-Glucuronosyltransferase 3 proteinBeta-1 -3-Glucuronyltransferase 3 proteinGlucuronosyltransferase I proteinGlcat-I proteinUdp-Glcua -Gal Beta-1 -3-Gal-R Glucuronyltransferase proteinGlcuat-I proteinB3GAT3 protein |
Information sourced from Uniprot.org