GALNT14
GALNT14 (polypeptide N-acetylgalactosaminyltransferase 14, also known as GalNAc-T14 or GalNac-T10) is a Golgi-resident enzyme that starts mucin-type O-linked glycosylation by attaching N-acetylgalactosamine to serine and threonine residues on target proteins. Browse Assay Genie's current range of GALNT14 research reagents below, or read on for the biology behind the target.
GALNT14 catalyses the initial reaction in O-linked oligosaccharide biosynthesis: the transfer of an N-acetyl-D-galactosamine (GalNAc) residue to the hydroxyl group of a serine or threonine on the protein receptor. This committed first step creates the GalNAc-O-Ser/Thr linkage on which longer O-glycan structures are then built. The enzyme shows activity toward mucin-derived peptide substrates, including Muc2, Muc5AC, Muc7 and Muc13, and has been shown to transfer GalNAc to large proteins such as mucins. It may also contribute to O-glycosylation in the kidney.
The GALNT14 gene encodes a Golgi protein that localises to the Golgi apparatus membrane. It belongs to the glycosyltransferase 2 family, GalNAc-T subfamily, and is a member of the polypeptide N-acetylgalactosaminyltransferase (ppGalNAc-T) family, the HGNC gene group that also includes GALNT3 and GALNT7. Members of this family act on the hydroxyl groups of serines and threonines in target peptides, and each shows its own substrate preferences.
The protein has been catalogued under several names, including UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 14, GalNAc-T14, GalNac-T10 and FLJ12691. Alterations in the GALNT14 gene may play a role in cancer progression and response to chemotherapy, which makes it of interest to researchers studying glycosylation changes in disease. A mouse ortholog, Galnt14, is recognised.
GALNT14 catalyses the first step of mucin-type O-linked glycan synthesis, making it a useful enzyme for studying how GalNAc is added to serine and threonine residues.
The enzyme acts on mucin-derived peptides including Muc2, Muc5AC, Muc7 and Muc13, linking it to studies of mucin glycosylation.
Alterations in the GALNT14 gene may play a role in cancer progression and response to chemotherapy.
GALNT14 may be involved in O-glycosylation in the kidney, pointing to a role in renal glycoprotein biology.
GALNT14 is a Golgi enzyme that catalyses the first step of O-linked oligosaccharide biosynthesis. It transfers N-acetyl-D-galactosamine to serine or threonine residues on protein substrates, and it shows activity toward mucin-derived peptides such as Muc2, Muc5AC, Muc7 and Muc13.
GALNT14 is also called GalNAc-T14, GalNac-T10 and FLJ12691. Its full name is polypeptide N-acetylgalactosaminyltransferase 14, and an earlier name was UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 14. It is classed under EC 2.4.1.41.
The NCBI Gene summary states that alterations in GALNT14 may play a role in cancer progression and response to chemotherapy. UniProt also notes a possible role in kidney O-glycosylation. A mouse ortholog, Galnt14, exists; check the datasheet of any product for its validated reactivity.
Other polypeptide N-acetylgalactosaminyltransferases that initiate mucin-type O-glycosylation, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q96FL9; product specifications from Assay Genie datasheets.