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.
Catalytic activity: UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1
Cofactor: Manganese
By similarity.Calcium
By similarity.
Pathway: Protein modification; protein glycosylation.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein
By similarity.
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. Ref.1
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
By similarity.The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity
By similarity.
Sequence similarities: Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.Contains 1 ricin B-type lectin domain.
Caution: According to experiments made in rat, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.
Sequence caution: The sequence BAB14676.1 differs from that shown. Reason: Erroneous initiation.
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