Protein argonaute-3 (AGO3)
The protein contains 860 amino acids for an estimated molecular weight of 97360 Da.
Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Proposed to be involved in stabilization of small RNA derivates (siRNA) derived from processed RNA polymerase III-transcribed Alu repeats containing a DR2 retinoic acid response element (RARE) in stem cells and in the subsequent siRNA-dependent degradation of a subset of RNA polymerase II-transcribed coding mRNAs by recruiting a mRNA decapping complex involving EDC4. Possesses RNA slicer activity but only on select RNAs bearing 5'- and 3'-flanking sequences to the region of guide-target complementarity (PubMed:29040713). (updated: April 22, 2020)
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.
- 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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Biological Process
Intracellular receptor signaling pathway
MiRNA loading onto RISC involved in gene silencing by miRNA
MiRNA mediated inhibition of translation
MRNA catabolic process
Negative regulation of gene expression
Positive regulation of gene expression
Positive regulation of NIK/NF-kappaB signaling
Post-transcriptional gene silencing by RNA
Pre-miRNA processing
Production of miRNAs involved in gene silencing by miRNA
Regulation of megakaryocyte differentiation
Regulation of stem cell proliferation
Regulation of transcription initiation from RNA polymerase II promoter
RNA secondary structure unwinding
Wnt signaling pathway, calcium modulating pathway
The reference OMIM entry for this protein is 607355
Eukaryotic translation initiation factor 2c, subunit 3; eif2c3
Argonaute 3; ago3
DESCRIPTION
Members of the argonaute protein family are involved in RNA silencing phenomena. Among their biologic roles are regulation of development and determination of stem cell character. These proteins are evolutionarily conserved from bacteria and plants to higher organisms. They contain an approximately 130-amino acid PAZ domain thought to be involved in protein-protein interactions and a C-terminal 300-amino acid PIWI domain. For a review of argonaute proteins, see Carmell et al. (2002).GENE FUNCTION
Azuma-Mukai et al. (2008) found that most small RNAs immunopurified with endogenous AGO2 (606229) and AGO3 from human Jurkat cell lysates were microRNAs (miRNAs), and that the miRNAs associated with AGO2 and AGO3 largely overlapped. Immunohistochemical analysis showed that both AGO2 and AGO3 localized in processing (P) bodies, suggesting that both are involved in the miRNA pathway. Endogenous AGO2 showed slicer activity, but AGO3 did not. Azuma-Mukai et al. (2008) hypothesized that AGO3 may function as an inhibitor of RNA interference activity.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the AGO3 gene to chromosome 1 (TMAP stSG53925). Carmell et al. (2002) stated that the AGO3 gene resides in tandem with the AGO1 (EIF2C1; 606228) and AGO4 (607356) genes on chromosome 1p35-p34. The orthologous genes in mouse are in the same orientation on chromosome 4. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 607355 was added.
April 25, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).