Protein pelota homolog (PELO)
The protein contains 385 amino acids for an estimated molecular weight of 43359 Da.
Cotranslational quality control factor involved in the No-Go Decay (NGD) pathway (PubMed:21448132, PubMed:29861391). In the presence of ABCE1 and HBS1L, is required for 48S complex formation from 80S ribosomes and dissociation of vacant 80S ribosomes (PubMed:21448132). Together with HBS1L and in presence of ABCE1, recognizes stalled ribosomes and promotes dissociation of elongation complexes assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and to degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway (PubMed:21448132). As part of the PINK1-regulated signaling, upon mitochondrial damage is recruited to the ribosome/mRNA-ribonucleoprotein complex associated to mitochondrial outer membrane thereby enabling the recruitment of autophagy receptors and induction of mitophagy (PubMed:29861391). (updated: Feb. 10, 2021)
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.
- 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.
- 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:rs1499280 |
Biological Process
Cell cycle
Cell division
Cell population proliferation
Chromosome organization
Endoderm development
Inner cell mass cell proliferation
Mesenchymal to epithelial transition
Nonfunctional rRNA decay
Nuclear-transcribed mRNA catabolic process, no-go decay
Nuclear-transcribed mRNA catabolic process, non-stop decay
Positive regulation of BMP signaling pathway
Regulation of translation
Ribosome disassembly
RNA surveillance
Stem cell population maintenance
Translation
The reference OMIM entry for this protein is 605757
Pelota, drosophila, homolog of; pelo
CLONING
Using degenerate primers designed to the Drosophila pelota gene sequence, Shamsadin et al. (2000) cloned a human PELO cDNA from a testis cDNA library. Lai et al. (2000) also identified human PELO, which they called CGI-17, by EST database searching against the C. elegans proteome sequence. The PELO cDNA encodes a 385-amino acid protein with a conserved nuclear localization signal. It shares 70%, 57%, and 36% sequence identity with Drosophila pelota protein, C. elegans R74.6, and yeast DOM34, respectively. By Northern blot analysis, Shamsadin et al. (2000) detected a 1.6-kb PELO transcript in all tissues tested as well as a 2.0-kb testis-specific transcript. By dot blot analysis, Lai et al. (2000) detected PELO expression most abundantly in fetal kidney, spleen, and lung, and in placenta, lung, spleen, kidney, and adrenal gland.GENE FUNCTION
Shamsadin et al. (2000) noted that studies of the Drosophila pelota gene indicate a role in spermatogenesis, mitotic division, and patterning, and that mutations in the related yeast DOM34 gene result in disturbances in the cell cycle and in meiotic cell division.MAPPING
Shamsadin et al. (2000) mapped the PELO gene to 5q11.2 by fluorescence in situ hybridization.ANIMAL MODEL
Adham et al. (2003) developed mice deficient in Pelo and found that homozygous deletion was embryonic lethal. Homozygous Pelo null embryos failed to develop past embryonic day 7.5 (E7.5). In culture, mitotic inactive trophoplasts survived, while mitotic active inner cell mass of null blastocysts failed to expand in growth, indicating that the lethality of Pelo null embryos was due to a defect in cell proliferation. Analysis of the cellular DNA content revealed a significant increase of aneuploid cells in Pelo null embryos at E7.5. Adham et al. (2003) hypothesized that an increase in aneuploid cells at E7.5 caused arrested development, suggesting that Pelo is required to maintain genomic stability. ... More on the omim web site
Feb. 16, 2021: 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605757 was added.