Eukaryotic translation initiation factor 3 subunit D (EIF3D)
The protein contains 548 amino acids for an estimated molecular weight of 63973 Da.
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs (PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:18599441, PubMed:25849773). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs (PubMed:27462815).', '(Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs745920273 |
Biological Process
Cap-dependent translational initiation
Formation of cytoplasmic translation initiation complex
IRES-dependent viral translational initiation
Positive regulation of mRNA binding
Positive regulation of translation
Translational initiation
Viral translational termination-reinitiation
The reference OMIM entry for this protein is 603915
Eukaryotic translation initiation factor 3, subunit d; eif3d
Eif3-p66
Eukaryotic translation initiation factor 3, subunit 7, formerly; eif3s7, formerly
DESCRIPTION
Eukaryotic initiation factor-3 (eIF3), the largest of the eIFs, is a multiprotein complex of approximately 600 kD that binds to the 40S ribosome and helps maintain the 40S and 60S ribosomal subunits in a dissociated state. It is also thought to play a role in the formation of the 40S initiation complex by interacting with the ternary complex of eIF2/GTP/methionyl-tRNA, and by promoting mRNA binding. Mammalian eIF3 consists of at least 10 nonidentical subunits: p170 (602039), p116 (603917), p110 (603916), p66 (EIF3D), p48 (602210), p47 (603914), p44 (603913), p40 (603912), p36 (603911), and p35 (603910). The p170, p110, p116, p36, and p44 subunits are homologous to S. cerevisiae proteins, suggesting that they represent a core complex capable of the RNA-protein and protein-protein interactions required to stimulate the translation initiation reactions dependent on eIF3. The remaining subunits may have been acquired later in eukaryotic evolution to provide additional means of translational control (summary by Asano et al., 1997).CLONING
By searching EST databases with the partial protein sequences of rabbit p66, p47, and p40, Asano et al. (1997) identified cDNAs encoding the human homologs. The predicted 548-amino acid human p66 protein contains an RNA-binding domain within an arginine- and lysine-rich N-terminal hydrophilic segment. Northern blot analysis revealed that p66 is expressed as a 1.9-kb mRNA.GENE FUNCTION
Asano et al. (1997) showed that recombinant human p66 bound radiolabeled RNA in vitro. Mutation analysis revealed that the RNA-binding domain of p66 is located between residues 86 and 118.MAPPING
Hartz (2012) mapped the EIF3D gene to chromosome 22q12.3 based on an alignment of the EIF3D sequence (GenBank GENBANK BC014912) with the genomic sequence (GRCh37). ... More on the omim web site
Nov. 17, 2018: Protein entry updated
Automatic update: OMIM entry 603915 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).