Description
Product Characteristics:
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.
Subcellular location: Cytoplasm, Cell membrane
Synonyms: DAD 1, DAD-1, dad1, DAD1_HUMAN, Defender against cell death 1, Dolichyl diphosphooligosaccharide protein glycosyltransferase subunit DAD1, Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1, Oligosaccharyl transferase subunit DAD1, OST 2, OST2.
Target Information: 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]