Aliases for GALNT7 Gene
- Polypeptide N-Acetylgalactosaminyltransferase 7 2 3 5
- Polypeptide GalNAc Transferase 7 2 3 4
- UDP-N-Acetyl-Alpha-D-Galactosamine:Polypeptide N-Acetylgalactosaminyltransferase 7 (GalNAc-T7) 2 3
- UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase 7 3 4
- Protein-UDP Acetylgalactosaminyltransferase 7 3 4
- Pp-GaNTase 7 3 4
- GALNAC-T7 3 4
External Ids for GALNT7 Gene
Previous GeneCards Identifiers for GALNT7 Gene
This gene encodes GalNAc transferase 7, a member of the GalNAc-transferase family. The enzyme encoded by this gene controls the initiation step of mucin-type O-linked protein glycosylation and transfer of N-acetylgalactosamine to serine and threonine amino acid residues. This enzyme is a type II transmembrane protein and shares common sequence motifs with other family members. Unlike other family members, this enzyme shows exclusive specificity for partially GalNAc-glycosylated acceptor substrates and shows no activity with non-glycosylated peptides. This protein may function as a follow-up enzyme in the initiation step of O-glycosylation. [provided by RefSeq, Jul 2008]
GeneCards Summary for GALNT7 Gene
GALNT7 (Polypeptide N-Acetylgalactosaminyltransferase 7) is a Protein Coding gene. Among its related pathways are Transport to the Golgi and subsequent modification and O-linked glycosylation. GO annotations related to this gene include carbohydrate binding and polypeptide N-acetylgalactosaminyltransferase activity. An important paralog of this gene is GALNT10.
UniProtKB/Swiss-Prot for GALNT7 Gene
Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers 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. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.