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貨期:
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用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. 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). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets. STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation. Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation.
基因功能參考文獻:
Study reports that STT3B-oligosaccharyltransferase, but not STT3A-oligosaccharyltransferase, is a lipid-linked oligosaccharide hydrolase. PMID: 30181269
These results reveal that the oxidoreductase activity of the STT3B-containing oligosaccharyltransferase is necessary for dengue virus infection. PMID: 28720733
STT3B was significantly upregulated in hip osteoarthritis with affected versus intact cartilage, particularly in the analysis of hypertrophic and normotrophic compared with atrophic bone remodelling pattern. PMID: 27974301
Post-translational modification of cotranslationally skipped sites by STT3B is hindered by the middle X residue, resulting in hypoglycosylation of consensus sites containing large hydrophobic and negatively charged side chains. PMID: 25029371
Results show homozygous mutation in STT3A and in STT3B causes congenital disorders of glycosylation. PMID: 23842455
Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST. PMID: 23530066
Data show that prolonged transthyretin (TTR) unfolding induces externalization of cryptic N-glycosylation site and triggers STT3B-dependent posttranslational N-glycosylation. PMID: 22607976
The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein. PMID: 19167329
STT3 proteins are the catalytic subunits of the oligosaccharyltransferase. Vertebrate, plant and insect genomes have an STT3A gene and a STT3B gene. SIMP is a member of the STT3B subfamily of STT3 proteins. PMID: 12887896