DAD1 cDNA Clone – Defender Against Cell Death 1 (Human)

DAD1, the defender against apoptotic cell death, was initially identified as a negative regulator of programmed cell death in the temperature sensitive tsBN7 cell line. The DAD1 protein disappeared in temperature-sensitive cells following a shift to the nonpermissive temperature, suggesting that loss of the DAD1 protein triggered apoptosis. DAD1 is believed to be a tightly associated subunit of oligosaccharyltransferase both in the intact membrane and in the purified enzyme, thus reflecting the essential nature of N-linked glycosylation in eukaryotes. [provided by RefSeq, Jul 2008]

DAD1: Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis. Belongs to the DAD/OST2 family.

Protein type: EC 2.4.99.18; Transferase; Apoptosis; Membrane protein, integral; Endoplasmic reticulum; Membrane protein, multi-pass; Glycan Metabolism - N-glycan biosynthesis

Chromosomal Location of Human Ortholog: 14q11.2

Cellular Component: endoplasmic reticulum membrane; membrane; oligosaccharyl transferase complex

Molecular Function: dolichyl-diphosphooligosaccharide-protein glycotransferase activity; oligosaccharyl transferase activity

Biological Process: protein amino acid glycosylation; protein amino acid N-linked glycosylation via asparagine