Eukaryotic peptide chain release factor subunit 1 (ETF1)
The protein contains 437 amino acids for an estimated molecular weight of 49031 Da.
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA (PubMed:7990965, PubMed:24486019). Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Required for SHFL-mediated translation termination which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and cellular genes (PubMed:30682371). (updated: Sept. 18, 2019)
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.
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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The reference OMIM entry for this protein is 600285
Eukaryotic translation termination factor 1; etf1
Release factor 1; rf1
Erf1
DESCRIPTION
Termination of protein biosynthesis and release of the nascent polypeptide chain are signaled by the presence of an in-frame stop codon at the aminoacyl site of the ribosome. The process of translation termination is universal and is mediated by protein release factors (RFs) and GTP. A class 1 RF recognizes the stop codon and promotes the hydrolysis of the ester bond linking the polypeptide chain with the peptidyl site tRNA, a reaction catalyzed at the peptidyl transferase center of the ribosome. Class 2 RFs, which are not codon specific and do not recognize codons, stimulate class 1 RF activity and confer GTP dependency upon the process. In prokaryotes, both class 1 RFs, RF1 and RF2, recognize UAA; however, UAG and UGA are decoded specifically by RF1 and RF2, respectively. In eukaryotes, eRF1, or ETF1, the functional counterpart of RF1 and RF2, functions as an omnipotent RF, decoding all 3 stop codons (Frolova et al., 1994).CLONING
Frolova et al. (1994) characterized a family of tightly related proteins from lower and higher eukaryotes that are structurally and functionally similar to rabbit RF. Two of these proteins, one from human and the other from Xenopus laevis, were expressed in yeast and Escherichia coli, respectively, purified, and shown to be active in the in vitro RF assay. Another protein of this family, sup45 (sup1) of Saccharomyces cerevisiae, is involved in omnipotent suppression during translation. The amino acid sequence of the RF1 family is highly conserved. Frolova et al. (1994) concluded that the RF1 proteins are directly implicated in the termination of translation in eukaryotes.GENE FUNCTION
Eukaryotic RF1 and RF3 (see GSPT1; 139259) are involved in translation termination. In vitro, RF1 catalyzes the release of the polypeptide chain without any stop codon specificity; the GTP-binding protein RF3 confers GTP dependence to the termination process and stimulates RF1 activity. Le Goff et al. (1997) used tRNA-mediated nonsense suppression of different stop codons in a CAT reporter gene to analyze the polypeptide chain release factor activities of recombinant human RF1 and RF3 proteins overexpressed in human cells. Using a CAT assay, they measured the competition between the suppressor tRNA and the release factors when a stop codon was present in the ribosomal A site. Regardless of which of the 3 stop codons was present in the CAT open reading frame, the overexpression of RF1 alone markedly decreased translational read-through by suppressor tRNA. Thus, Le Goff et al. (1997) concluded that RF1 has intrinsic antisuppressor activity. The levels of antisuppression when both RF1 and RF3 were overexpressed were almost the same as those when RF1 was overexpressed alone, suggesting that RF1-RF3 complex-mediated termination may be controlled by the expression level of RF1. Overexpression of RF3 alone had an inhibitory effect on CAT gene expression. CAT mRNA stability studies suggested that RF3 inhibits gene expression at the transcriptional level. Le Goff et al. (1997) suggested that RF3 may perform other functions, including the stimulation of RF1 activity, in vivo. Alkalaeva et al. (2006) reconstituted eukaryotic translation initiation, elongation, and termination processes in vitro on a model mRNA encoding a tetrapeptide followed by a UAA stop codon using individual 40S and 60S ribosomal subunits and the complete set of individual initiation, elongation, and release factors. They ... More on the omim web site
Sept. 22, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Jan. 21, 2019: 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 600285 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed