Heparan sulfate sulfotransferase
IPR037359
Definition
Seven 3-O-sulfotransferase isoforms in the human genome are involved in the biosynthesis of 3-O-sulfated heparan sulfate PMID:17131147. These enzymes catalyze the transfer of a sulfo group from the sulfo donor, 3'-phosphoadenosine-5'-phosphosulfate (PAPS), to the 3-OH position of a glucosamine unit of heparin sulfate (HS). 3-O-sulfation is critically important for anticoagulant activity PMID:6935668. The key control of anticoagulant HS synthesis is regulation of the expression of 3-O-sulfotransferase isoforms 1 and 5 (3-OST-1 and 3-OST-5). 3-O-sulfation is also involved in the regulation of neural development [[cite:PMID:26731579], [cite:PMID:15452147], [cite:PMID:23451335]]. 3-OST proteins exhibit similarity with the heparan biosynthetic enzyme NST (bifunctional HS N-deacetylase/N-sulfotransferase). It appears that a common sulfotransferase structure is shared by these two types of heparan biosynthetic enzyme PMID:9346953. The bifunctional enzyme catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in HS PMID:10758005.
11 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
Loading the interactive Seroatlas explorer...