Rab GDP dissociation inhibitor beta (GDI2)
The protein contains 445 amino acids for an estimated molecular weight of 50663 Da.
Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. (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.
- 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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Biological Process
Neutrophil degranulation
Positive regulation of GTPase activity
Protein transport
Regulation of small GTPase mediated signal transduction
Signal transduction
Small GTPase mediated signal transduction
Vesicle-mediated transport
The reference OMIM entry for this protein is 600767
Gdp-dissociation inhibitor 2; gdi2
Rab gdp-dissociation inhibitor, beta; rabgdib
Rab gdi-beta
DESCRIPTION
GDI-beta (GDI2) is a member of the GDP-dissociation inhibitor family, which includes GDI-alpha (GDI1; 300104). The rab GDIs modulate the activity of G proteins of the rab family and play a role in the regulation of vesicle-mediated cellular transport (summary by Sedlacek et al., 1998).CLONING
Shisheva et al. (1994) cloned mouse RABGDIB (which they referred to as 'smg p25A GDI') and reported the sequence. Sedlacek et al. (1994) found that the human RABGDIB sequence is 86.5% similar to RABGDIA, which they referred to as 'XAP-4.' Bachner et al. (1995) studied expression patterns of the 2 human genes. They showed that the 2.5-kb mRNA for RABGDIB is ubiquitously expressed, in contrast to RABGDIA, which is expressed primarily in neural and sensory tissues. Rak et al. (2003) used a combination of chemical synthesis and protein engineering to generate and crystallize the monoprenylated YPT1-RABGDI complex. The structure of this complex was determined to 1.5-angstrom resolution and provided a structural basis for the ability of RABGDI to inhibit nucleotide release by RAB proteins. Isoprenoid binding requires a conformational change that opens a cavity in the hydrophobic core of its domain II. Analysis of the structure provided a molecular basis for understanding a RABGDI mutant that causes mental retardation.GENE STRUCTURE
The GDI-beta gene contains 11 exons (Sedlacek et al., 1998).MAPPING
By in situ hybridization, Sedlacek et al. (1998) demonstrated that the GDI2 gene maps to 10p15; a processed pseudogene maps to 7p13-p11. ... 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 600767 was added.