The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T5 (Polypeptide N-acetylgalactosaminyltransferase 5), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, is a 940 amino acid protein that displays enzymatic activity toward EA2 peptide substrate with weaker activity toward Muc2 or Muc 1b substrates. Its N-terminal domain is involved in substrate binding and manganese coordination, while the SLCterminal domain is involved in UDP-Gal binding and catalytic reaction. EXT2 directly interacts with GalNAc-T5, suggesting that these proteins may corroborate in glycosaminoglycan synthesis.
Function:
GALNT5 can catalyze 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. GALNT5 has activity toward EA2 peptide substrate, but it has a weak activity toward Muc2 or Muc1b substrates.
Subunit:
Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3.
Subcellular Location:
Cell Membrane and Golgi Apparatus
Similarity:
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
Contains 1 ricin B-type lectin domain.
SWISS:
Q7Z7M9
Gene ID:
11227
Database links:
Entrez Gene: 11227 Human
Entrez Gene: 241391 Mouse
Entrez Gene: 83627 Rat
SwissProt: Q7Z7M9 Human
SwissProt: Q8C102 Mouse
SwissProt: O88422 Rat
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