Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate ( ). Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis . Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response (By similarity). Required for the exosomal release of SDCBP, CD63 and syndecan .
Lacks both N-deacetylase and N-sulfotransferase activities. Acts as a dominant negative on isoform 1, likely by changing the composition of enzyme complexes responsible for elongation and modification of heparan sulfates.
Subcellular locations: Golgi apparatus, Trans-Golgi network membrane, Golgi apparatus, Cis-Golgi network membrane
Subcellular locations: Golgi apparatus, Cis-Golgi network membrane
Widely expressed. Expression is most abundant in heart, liver and pancreas.