Eukaryotic translation initiation factor 3 subunit C (EIF3C)

The protein contains 913 amino acids for an estimated molecular weight of 105344 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:17581632, 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:17581632). 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). (updated: Oct. 25, 2017)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. 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.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. 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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 61%
Model score: 0
No model available.

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The reference OMIM entry for this protein is 603916

Eukaryotic translation initiation factor 3, subunit c; eif3c
Eif3-p110
Eukaryotic translation initiation factor 3, subunit 8, formerly; eif3s8, formerly

DESCRIPTION

Eukaryotic initiation factor-3 (eIF3) is the largest of the eIFs and consists of at least 10 nonidentical subunits, including EIF2C (Asano et al., 1997).

CLONING

Asano et al. (1997) demonstrated that the 115-kD component of HeLa cell eIF3 is actually composed of 2 proteins, p116 (PRT1; 603917) and p110. By screening a HeLa cell expression library with antibodies against the 115-kD band, these authors identified cDNAs encoding p110. The predicted 913-amino acid p110 protein has a pI of 5.8 and is unrelated to p116. p110 shares 31% identity to the S. cerevisiae Nip1 protein, which is thought to be involved in nuclear import and the initiation phase of protein synthesis. Asano et al. (1997) found that the p116, p110, and p36 (603911) subunits localize on 40S ribosomes in cells active in translation and coimmunoprecipitate with p170 (602039), indicating that these proteins are integral components of eIF3. Northern blot analysis revealed that p110 is expressed as a 3-kb mRNA.

GENE FUNCTION

By reciprocal yeast 2-hybrid and coimmunoprecipitation analyses of the human STS26T malignant schwannoma cell line, Scoles et al. (2006) showed that isoforms 1 and 2 of schwannomin (NF2; 607379) interacted with EIF3C. Mutation analysis revealed that the FERM domain of schwannomin interacted with the C-terminal half of EIF3C. Immunofluorescence microscopy of STS26T cells showed that the 2 proteins partly colocalized at punctate perinuclear structures and at some membranous structures. Overexpression of EIF3C in STS26T cells elevated cell proliferation, and schwannomin countered this effect. Western blot analysis revealed an inverse abundance of schwannomin and EIF3C in human meningiomas.

MAPPING

Gross (2011) mapped the EIF3C gene to chromosome 16p11.2 based on an alignment of the EIF3C sequence (GenBank GENBANK BC000533) with the genomic sequence (GRCh37). A nearly identical copy of EIF3C, designated EIF3CL, also maps to chromosome 16p11.2. ... More on the omim web site

Subscribe to this protein entry history

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 25, 2017: Additional information
No protein expression data in P. Mayeux work for EIF3C

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603916 was added.