The yeast oligosaccharyl transferase catalyzes the glycosylation of asparagine residues in secreted, vesicular, and membrane proteins. A complex of at least four membrane-bound polypeptides is responsible for oligosaccharyl transferase activity. Amino acid sequences from the 64 kDa glycoprotein subunit of the complex were used to clone the essential NLT1 (N-linked oligosaccharyl transferase) gene. The Nlt1p gene product is a processed, multiply glycosylated type I membrane protein; it has an extensive amino-terminal soluble domain, a potential hydrophobic transmembrane domain, and a short carboxy-terminal soluble domain. The Nlt1p is significantly similar than the mammalian ribophorin I, a component of the mammalian oligosaccharyl transferase complex, and the enzyme is conserved throughout eukaryotic evolution.
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| rdf:type | |
| rdfs:comment |
The yeast oligosaccharyl transferase catalyzes the glycosylation of asparagine residues in secreted, vesicular, and membrane proteins. A complex of at least four membrane-bound polypeptides is responsible for oligosaccharyl transferase activity. Amino acid sequences from the 64 kDa glycoprotein subunit of the complex were used to clone the essential NLT1 (N-linked oligosaccharyl transferase) gene. The Nlt1p gene product is a processed, multiply glycosylated type I membrane protein; it has an extensive amino-terminal soluble domain, a potential hydrophobic transmembrane domain, and a short carboxy-terminal soluble domain. The Nlt1p is significantly similar than the mammalian ribophorin I, a component of the mammalian oligosaccharyl transferase complex, and the enzyme is conserved throughout eukaryotic evolution.
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| skos:exactMatch | |
| uniprot:name |
FEBS Lett.
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| uniprot:author |
Imperiali B.,
Parker C.S.,
Pathak R.
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| uniprot:date |
1995
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| uniprot:pages |
229-234
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| uniprot:title |
The essential yeast NLT1 gene encodes the 64 kDa glycoprotein subunit of the oligosaccharyl transferase.
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| uniprot:volume |
362
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| dc-term:identifier |
doi:10.1016/0014-5793(95)00253-6
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