basic FUNCTION
| transfering a high mannose oligosaccharide from a lipid-linked oligosaccharide donor onto asparagine accaptor sites within an Asn-X-Ser/Thr consensus motif in newly synthesized proteins |
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facilitate the N-glycosylation of certain precursors during their biogenesis at the endoplasmic reticulum |
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can regulate the delivery of precursor proteins to the oligosaccharyltransferase complex by capturing substrates and presenting them to the catalytic core |
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acts as a substrate-specific facilitator of N-glycosylation |
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involved in asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum |
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distinct and complementary roles for the RPN1 isoforms STT3A, STT3B allowing sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation |
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having a novel chaperone activity that is a consequence of N-glycosylation-dependent direct interaction with OPRM1 |
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RPN1 functions as a chaperone inside the cell |
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may play a central role in the selective association between MLEC and misfolded glycoproteins |
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may function as a chaperone that recognizes misfolded proteins inside cells |