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Catalytic Activity
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Dolichyl diphosphooligosaccharide + [protein]- L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
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Domain
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The cytoplasmic C-terminal domain contains a functional dilysine-retrieval motif, which is involved in the retrograde Golgi-to-ER transport of the protein.
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Function
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Essential subunit of the N-oligosaccharyl transferase (OST) complex 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). All subunits are required for a maximal enzyme activity.
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Interaction
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P53622:COP1; NbExp=3; IntAct=EBI-12658, EBI-4860; P52870:SBH1; NbExp=2; IntAct=EBI-12658, EBI-16410; P32915:SEC61; NbExp=2; IntAct=EBI-12658, EBI-16400; P35179:SSS1; NbExp=2; IntAct=EBI-12658, EBI-16406; P39007:STT3; NbExp=3; IntAct=EBI-12658, EBI-18447; Q02795:SWP1; NbExp=4; IntAct=EBI-12658, EBI-12666;
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Miscellaneous
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Present with 14900 molecules/cell in log phase SD medium
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Miscellaneous
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Present with 14900 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
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Pathway
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Protein modification; protein glycosylation.
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Similarity
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Belongs to the DDOST 48 kDa subunit family
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Similarity
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Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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Subcellular Location
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Endoplasmic reticulum membrane; Single-pass type I membrane protein.
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Subunit
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Component of the oligosaccharyltransferase (OST) complex, which appears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6. WBP1, SWP1 and OST2 probably form a subcomplex. May interact directly with OST2, OST3, OST5, OST6, WBP1 AND SWP1. Interacts with SEC61, SBH1 and SSS1. {ECO:0000269|PubMed:15831493, ECO:0000269|PubMed:15886282, ECO:0000269|PubMed:8175708, ECO:0000269|PubMed:9405463}.
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