Polypeptide N-acetylgalactosaminyltransferase 10
Domain
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Function
Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates.
Pathway
Protein modification; protein glycosylation.
Sequence Similarities
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
Tissue Specificity
Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues.
Cellular localization
- Golgi apparatus membrane
- Single-pass type II membrane protein
Alternative names
Polypeptide N-acetylgalactosaminyltransferase 10, Polypeptide GalNAc transferase 10, Protein-UDP acetylgalactosaminyltransferase 10, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, GalNAc-T10, pp-GaNTase 10, GALNT10