| Gene Name | EIF3D |
| HF Protein Name | Eukaryotic translation initiation factor 3 subunit D |
| HF Function | It plays role in translation initiation complex recruitment |
| Uniprot ID | O15371 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 8664 |
| Host Factor (HF) Name in Paper | EIF3D |
| Gene synonyms | EIF3S7 |
| Ensemble Gene ID | ENSG00000100353 |
| Ensemble Transcript | ENST00000216190 [O15371-1];ENST00000405442 [O15371-1] |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0001732, GO:0002191, GO:0003723, GO:0003743, GO:0005829, GO:0005852, GO:0006413, GO:0016020, GO:0045727, GO:0071541, GO:0075522, GO:0075525, GO:0098808, GO:1902416, |
| MINT ID | O15371 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 603915 |
| PANTHER ID | PTHR12399 |
| PDB ID(s) | N.A., |
| pfam ID | PF05091, |
| Drug Bank ID | N.A., |
| ChEMBL ID | N.A. |
| Organism | Homo sapiens (Human) |
| Virus Name | Norwalk virus |
| Virus Short Name | NLV |
| Order | Nidovirales |
| Virus Family | Caliciviridae |
| Virus Subfamily | N.A. |
| Genus | Norovirus |
| Species | Norwalk virus |
| Host | Human, mammals |
| Cell Tropism | Intestinal epithelium |
| Associated Disease | Gastroenteritis |
| Mode of Transmission | Fecal-oral route from contaminated water and food |
| VIPR DB link | https://www.viprbrc.org/brc/home.spg?decorator=calici |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/positive-sense-rna-viruses-2011/w/posrna_viruses/253/caliciviridae |
| Virus Host DB link | N.A. |
| Paper Title | The genome-linked protein VPg of the Norwalk virus binds eIF3, suggesting its role in translation initiation complex recruitment |
| Author's Name | Katie F.Daughenbaugh, Chris S.Fraser1, John W.B.Hershey1 and Michele E.Hardy |
| Journal Name | The EMBO Journal |
| Pubmed ID | 12773399 |
| Abstract | The positive-strand RNA genomes of caliciviruses are not capped, but are instead covalently linked at their 5 ends to a viral proteincalled VPg. The lack of a cap structure typical of eukaryotic mRNA and absence of an internal ribosomal entry site suggest that VPgmay function in translation initiation on calicivirus RNA. This hypothesis was tested by analyzing binding of Norwalk virus VPg to translation initiation factors. The eIF3d subunit of eIF3 was identified as a binding partner of VPg by yeast two-hybrid analysis. VPgbound to purified mammalian eIF3 and to eIF3 in mammalian cell lysates. To test the effects of the VPg- eIF3 interaction on translation, VPg was added to cell-free translation reactions programmed with either capped reporter RNA, an RNA containing an EMCV internal ribosomal entry site (IRES) or an RNA with a cricket paralysis virus IRES. VPg inhibited translation of all reporter RNAs in a dose-dependent manner. Together, the data suggest that VPg may play a role in initiating translation on calicivirus RNA through unique protein-protein interactions with the translation machinery. |
| Used Model | CaCo-2 cells |
| DOI | 10.1093/emboj/cdg251 |
