Enhancer of mRNA-decapping protein 4 (EDC4)
The protein contains 1401 amino acids for an estimated molecular weight of 151661 Da.
In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
- 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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Biological Process
Deadenylation-independent decapping of nuclear-transcribed mRNA
Exonucleolytic catabolism of deadenylated mRNA
Cellular Component
Cytoplasm
Cytoplasmic ribonucleoprotein granule
Cytosol
Membrane
Nucleoplasm
Nucleus
P-body
Molecular Function
The reference OMIM entry for this protein is 606030
Enhancer of mrna decapping 4; edc4
Autoantigen rcd8; rcd8
Ge1
Human enhancer of decapping, large subunit; hedls
CLONING
Antibodies directed against nuclear and cytoplasmic components are a characteristic feature of autoimmune disease. By screening a hepatocellular carcinoma cDNA expression library with serum from a patient (GE) with Sjogren syndrome (270150), followed by probing an endothelial cell cDNA library, Bloch et al. (1994) identified a cDNA encoding GE1. The deduced 1,215-amino acid protein contains a central serine-rich region and a putative nuclear localization sequence (NLS) near its C terminus; however, it lacks zinc finger, leucine zipper, and RNA-binding motifs, which are found in other autoantigens. Immunoblot analysis indicated that GE1 is expressed as a 160-kD protein. Epitope mapping analysis suggested that the functional NLS-containing hydrophilic region of GE1 is the site recognized by patient serum. Immunofluorescence microscopy using rat antisera to the recombinant protein demonstrated speckled, mostly nuclear expression. Using human RCD serum, which recognizes strictly cytoplasmic components, to screen an expression cDNA library, Garcia-Lozano et al. (1997) obtained a cDNA encoding RCD8. Sequence analysis predicted that the 968-amino acid RCD8 protein is nearly identical to the GE1 protein identified by Bloch et al. (1994). However, due to a nucleotide insertion at position 2341, RCD8 is 186 amino acids longer at the C-terminal end than GE1, whereas GE1 is 433 amino acids longer at the N-terminal end. Immunoblot analysis showed expression of a 160-kD protein. Immunofluorescence microscopy demonstrated cytoplasmic expression. Garcia-Lozano et al. (1997) mapped the immunoreactive region to an area between amino acids 435 and 500, identical to the area identified by Bloch et al. (1994).GENE FUNCTION
Using mass spectroscopy, Fenger-Gron et al. (2005) found that EDC3 (609842), RCK (DDX6; 600326), and EDC4, which they called HEDLS, coimmunopurified with the mRNA-decapping enzymes DCP1A and DCP2 (609844) from HEK293 cell lysates. RCD8 promoted the association of DCP1A and DCP2, and overexpressed DCP1A and DCP2 did not associate in its absence. RCD8 associated with DCP2 and stimulated its decapping activity in vitro. Overexpression of RCD8 caused accumulation of deadenylated mRNA and formation of multiple enlarged cytoplasmic processing body-like structures containing EDC4, DCP1 and XRN1 (607994).MAPPING
The International Radiation Hybrid Mapping Consortium mapped the EDC4 gene to chromosome 16 (TMAP stSG43158). ... More on the omim web site
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 606030 was added.