CHST5

The carbohydrates of glycoconjugates are highly diverse structures with variation in monosaccharide composition, glycosidic linkage positions, and branching of chains. Further diversity is added by the covalent addition of sulfate moieties to particular hydroxyl groups and amino groups of saccharides. The sulfate modifications of glycoproteins can be extensive in amount and frequently occur at high density. They can have a profound effect on the physiochemical properties of the glycoconjugates, at least in part through the addition of negative charge. Carbohydrate sulfation plays a critical role in many biologic processes. CHST5 belongs to the GST family of sulfotransferases, which also includes CHST1 (MIM 603797), CHST2 (MIM 603798), CHST3 (MIM 603799), and LSST. These enzymes are 6-O-sulfotransferases, which add sulfate to C6 of galactose (Gal), N-acetylgalactosamine (GalNAc), or N-acetylglucosamine (GlcNAc) (Lee et al., 1999 [PubMed 10491328]).[supplied by OMIM

carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 5

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues and O-linked sugars of mucin-type acceptors. Acts on the non-reducing terminal GlcNAc of short carbohydrate substrates. However, it does not transfer sulfate to longer carbohydrate substrates that have poly-N-acetyllactosamine structures. Has no activity toward keratan. Not involved in generating HEV-expressed ligands for SELL. Its substrate specificity may be influenced by its subcellular location.

Carbohydrate metabolic process Source: UniProtKB-KW
Keratan sulfate biosynthetic process Source: GO_Central
N-acetylglucosamine metabolic process Source: UniProtKB
Protein sulfation Source: ProtInc
Sulfur compound metabolic process Source: UniProtKB

Golgi apparatus membrane. Golgi membrane, early secretory pathway.

Cytoplasmic: 1-30
Helical: 31-48
Lumenal: 49-411