Eukaryotic translation initiation factor 3 subunit M (EIF3M)
The protein contains 374 amino acids for an estimated molecular weight of 42503 Da.
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17403899, PubMed:25849773, 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:17403899). 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).', '(Microbial infection) May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2). (updated: Oct. 25, 2017)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- 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:rs11557143 | |
| a breast cancer sample; somatic mutation | |
| dbSNP:rs1802363 |
Biological Process
Cytoplasmic translational initiation
Formation of cytoplasmic translation initiation complex
Formation of translation preinitiation complex
Regulation of translational initiation
Translational initiation
Viral process
The reference OMIM entry for this protein is 609641
Eukaryotic translation initiation factor 3, subunit m; eif3m
Pci domain-containing protein 1; pcid1
Human fetal lung protein b5; hflb5; b5
Dendritic cell protein ga17; ga17
DESCRIPTION
HFLB5 encodes a broadly expressed protein containing putative membrane fusion domains that acts as a receptor or coreceptor for entry of herpes simplex virus (HSV) (Perez et al., 2005).CLONING
By searching for genes in a region of chromosome 11 associated with WAGR syndrome (194072), Gawin et al. (1999) identified and cloned EIF3M, which they called GA17. Northern blot analysis detected a 1.5-kb transcript in all human tissues examined. Variable Ga17 expression was detected in all adult tissues examined, and Ga17 expression was also detected at all stages of mouse embryonic development. In situ hybridization of mouse embryos showed expression mainly in lung, thymus, and developing kidney, with lower levels in muscle and neuronal tissues. By screening a fetal lung cDNA library for sequences that transferred HSV susceptibility to entry-defective, replication-competent porcine kidney cells, Perez et al. (2005) obtained a cDNA encoding HFLB5. The predicted 374-amino acid type II membrane protein contains 2 N-glycosylation sites and a C-terminal heptad repeat that forms a coiled-coil structure. HFLB5 lacks a signal peptide. Microscopic, immunoprecipitation, Western blot, and FACS analyses demonstrated that the HFLB5 C terminus is exposed extracellularly on the cell surface. Northern blot and RT-PCR analyses of human tissues and cell lines revealed broad expression of a 1.3-kb HFLB5 transcript.GENE FUNCTION
Perez et al. (2005) determined that expression of HFLB5 in entry-defective, replication-competent porcine kidney cells transferred susceptibility to both HSV-1 and HSV-2. Entry of HSV into HFLB5-expressing porcine and human cells could be blocked by a 30-mer peptide identical to the HFLB5 C-terminal coiled-coil region. Using mutagenesis and synthetic peptides, Perez-Romero and Fuller (2005) showed that only the wildtype B5 C-terminal coiled-coil sequence or the B5 C terminus with nondisruptive mutations blocked HSV entry. They concluded that the C terminus of B5 contains a functional region important for B5 to mediate HSV entry. Chew et al. (2009) presented a highly validated set of targets that is necessary for apoptosis provoked by several stimuli in Drosophila. Among these, Tango7, whose human homolog is PCID1, was identified as a new effector. Cells depleted for this gene resisted apoptosis at a step before the induction of effector caspase activity, and the directed silencing of Tango7 in Drosophila prevented caspase-dependent programmed cell death. Unlike known apoptosis regulators in this model system, Tango7 activity did not influence stimulus-dependent loss of Drosophila DIAP1 (human homolog DIAPH1, 602121), but instead regulated levels of the apical caspase Dronc (human homolog CASP9, 602234). Similarly, Chew et al. (2009) found that human PCID1 impinged on CASP9, revealing a novel regulatory axis affecting the apoptosome.MAPPING
By analyzing a PAC contig covering chromosome 11p14.1-p13, Gawin et al. (1999) mapped the EIF3M gene to chromosome 11p13, centromeric to the WT1 gene (607102) and telomeric to the TR2 gene (DEPDC7; 612294). ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609641 was added.