Ras-related protein R-Ras (RRAS)
The protein contains 218 amino acids for an estimated molecular weight of 23480 Da.
Regulates the organization of the actin cytoskeleton (PubMed:16537651, PubMed:18270267). With OSPBL3, modulates integrin beta-1 (ITGB1) activity (PubMed:18270267). (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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Biological Process
Face morphogenesis
Leukocyte differentiation
Negative regulation of cell migration
Positive regulation of angiogenesis
Positive regulation of endothelial cell migration
Positive regulation of endothelial cell-matrix adhesion via fibronectin
Positive regulation of vasculogenesis
Ras protein signal transduction
Regulation of ERK1 and ERK2 cascade
Regulation of protein kinase B signaling
The reference OMIM entry for this protein is 165090
Related ras viral oncogene homolog; rras
Oncogene rras
CLONING
Lowe et al. (1987) isolated the human RRAS gene by low-stringency hybridization with a Harvey-ras probe. They found that the predicted 218-amino acid RRAS protein has an amino-terminal extension of 26 residues compared with HRAS p21 (190020) and shares 55% sequence identity with it. The cloned mouse Rras cDNA encodes a predicted protein sharing 94.5% sequence identity with the human protein. By immunostaining several mouse tissues, Komatsu and Ruoslahti (2005) found that Rras was primarily expressed in vascular smooth muscle cells in small arterioles and major arteries and in endothelial cells of lung capillaries. Lower Rras levels were found in smooth muscle cells of veins, renal glomeruli, and venous endothelium of spleen. In smooth muscle cells, Rras was distributed along the plasma membrane.GENE FUNCTION
Oinuma et al. (2004) reported that the semaphorin-4D (SEMA4D; 601866) receptor plexin B1 (601053) directly stimulates the intrinsic GTPase activity of RRAS, a member of the Ras superfamily of small GTP-binding proteins that has been implicated in promoting cell adhesion and neurite outgrowth. This activity required the interaction of plexin B1 with RND1 (609038), a small GTP-binding protein of the Rho family. Downregulation of RRAS activity by the plexin B1/RND1 complex was essential for the SEMA4D-induced growth cone collapse in hippocampal neurons. Oinuma et al. (2004) concluded that plexin B1 mediates SEMA4D-induced repulsive axon guidance signaling by acting as a GTPase-activating protein for RRAS.GENE STRUCTURE
Lowe et al. (1987) determined that the RRAS gene has at least 6 exons.ANIMAL MODEL
Komatsu and Ruoslahti (2005) found that Rras-null mice were viable and fertile with no obvious abnormalities and normal tissues upon histologic examination. However, Rras-null mice showed exaggerated neointimal thickening in response to arterial injury and increased angiogenesis in implanted tumors. In wildtype mice, Rras expression was greatly reduced in hyperplastic neointimal smooth muscle cells and in angiogenic endothelial cells. Overexpression of activated Rras suppressed mitogenic and invasive activities of growth factor-stimulated vascular cells.MAPPING
By means of a panel of mouse-human somatic cell hybrids, Lowe et al. (1987) mapped the human RRAS gene to chromosome 19. By means of a panel of mouse-hamster somatic cell hybrids, they mapped the mouse homolog to chromosome 7. ... More on the omim web site
July 5, 2019: Protein entry updated
Automatic update: OMIM entry 165090 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).