RNA-binding protein 3 (RBM3)
The protein contains 157 amino acids for an estimated molecular weight of 17170 Da.
Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation (By similarity). (updated: March 4, 2015)
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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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
Positive regulation of mRNA splicing, via spliceosome
Positive regulation of translation
Production of miRNAs involved in gene silencing by miRNA
Regulation of RNA metabolic process
Regulation of translation
Response to cold
RNA processing
Translation
Cellular Component
Cytoplasm
Dendrite
Nucleolus
Nucleoplasm
Nucleus
Ribonucleoprotein complex
Spliceosomal complex
The reference OMIM entry for this protein is 300027
Rna-binding motif protein 3; rbm3
CLONING
Using cDNA selection with a YAC from the Xp11.2 region, Derry et al. (1995) identified a novel gene, which they designated RBM3 (for 'RNA-binding motif protein 3'), that encodes a polypeptide with high sequence similarity to a group of proteins that bind to RNA; see also the Y-chromosome genes RBM1 (400006) and RBM2. The RBM3 gene gave rise to alternatively spliced transcripts in a variety of human tissues. The longest open reading frame encodes a 157-amino acid protein with a predicted molecular weight of 17 kD. Its putative RNA-binding domain most closely resembles that of 2 previously characterized human RNA-binding proteins, YRRM and a glycoprotein identified as an autoantigen. The authors noted that homology of RBM3 in both sequence and size to an RNA-binding protein from maize, AAIP, suggested it functions in a fundamental pathway conserved from plants to mammals.GENE FUNCTION
Peretti et al. (2015) demonstrated that synapse regeneration is impaired in mouse models of neurodegenerative disease, in association with failure to induce Rbm3. In both prion-infected and 5XFAD (Alzheimer-type) mice, the capacity to regenerate synapses after cooling declined in parallel with the loss of induction of Rbm3. Enhanced expression of Rbm3 in the hippocampus prevented this deficit and restored the capacity for synapse reassembly after cooling. Rbm3 overexpression, achieved either by boosting endogenous levels through hypothermia before the loss of the Rbm3 response or by lentiviral delivery, resulted in sustained synaptic protection in 5XFAD mice and throughout the course of prion disease, preventing behavioral deficits and neuronal loss and significantly prolonging survival. In contrast, knockdown of Rbm3 exacerbated synapse loss in both models and accelerated disease and prevented the neuroprotective effects of cooling. Peretti et al. (2015) concluded that deficient synapse regeneration, mediated at least in part by failure of the RBM3 stress response, contributes to synapse loss throughout the course of neurodegenerative disease. The authors also stated that their data supported enhancing cold-shock pathways as potential protective therapies in neurodegenerative disorders.MAPPING
On a YAC contig map, RBM3 was found by Derry et al. (1995) to be located between OATL1 (311240) and GATA1 (305371)/TFE3 (314310) in subband Xp11.23. ... More on the omim web site
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 300027 was added.