National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory
Protein Information |
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|---|---|
| Protein Name | Transmembrane protein 258 |
| Accession Code | Q9VVA8 |
| Gene | kud |
| Organism | Drosophila melanogaster (Taxonomy: 7227) |
| Part of Reference Proteome? | Yes |
| Sequence (Length: 78) |
Description |
Position in the Nuclear Envelope |
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|---|---|---|
| Location | Location ID | Description |
| Nuclear Envelope | SL-0178 | The nuclear envelope is a membrane system which surrounds the nucleoplasm of eukaryotic cells. It is composed of the nuclear lamina, nuclear pore complexes and two nuclear membranes. The space between the two membranes is called the nuclear intermembrane space. |
| Nuclear Membrane | SL-0182 | The membrane surrounding the nucleus. This term is used when it is not known if the protein is found in or associated with the inner or outer nuclear membrane. |
| Nuclear Outer Membrane | SL-0183 | The outer membrane of the nucleus is the membrane facing the cytoplasm. In mammals, the outer nuclear membrane is continuous in many places with the rough endoplasmic reticulum and is dotted with ribosomes. | Membrane Topology |
| Topology | Source | Annotation Type |
| Transmembrane | UniProt | Sequence Analysis {ECO:0000255} | Assigned Ontology terms |
Description |
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|---|---|
| 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 (By similarity). In addition may regulates nuclear envelope (NE) architecture and nuclear positioning through the linker of nucleoskeleton and cytoskeleton (LINC)-dependent and -independent mechanisms (PubMed:28716842). {By SimilarityUniProtKB:P61165, Experimental EvidencePubMed:28716842}. | Assigned Ontology terms |
Interactions with other proteins (1 interactors) |
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National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory