Rho GDP-dissociation inhibitor 2 (ARHGDIB)

The protein contains 201 amino acids for an estimated molecular weight of 22988 Da.

 

Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them (PubMed:8356058, PubMed:7512369). Regulates reorganization of the actin cytoskeleton mediated by Rho family members (PubMed:8262133). (updated: Nov. 22, 2017)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. 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.
  3. 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.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. 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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 100%
Model score: 67
MODL_MODELLER-9.18
MODL_I-TASSER-3.0

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No binding partner found

The reference OMIM entry for this protein is 602843

Rho gdp-dissociation inhibitor beta; arhgdib
Gdp-dissociation inhibitor d4; gdid4; d4
Lygdi

DESCRIPTION

Members of the Rho (or ARH) protein family (see 165390) and other Ras-related small GTP-binding proteins (see 179520) are involved in diverse cellular events, including cell signaling, proliferation, cytoskeletal organization, and secretion. The GTP-binding proteins are active only in the GTP-bound state. At least 3 classes of proteins tightly regulate cycling between the GTP-bound and GDP-bound states: GTPase-activating proteins (GAPs), guanine nucleotide-releasing factors (GRFs), and GDP-dissociation inhibitors (GDIs). The GDIs, including ARHGDIB, decrease the rate of GDP dissociation from Ras-like GTPases (summary by Scherle et al., 1993).

CLONING

By using a subtractive hybridization approach, Scherle et al. (1993) identified a B-cell cDNA encoding ARHGDIB, which shares homology to RhoGDI (ARHGDIA; 601925). They designated the gene LyGDI for 'lymphoid-specific GDI.' Northern blot analysis revealed that LyGDI is expressed as a 1.4-kb transcript only in hematopoietic tissues. Antibodies against LyGDI recognized a 27-kD protein on Western blots of B- and T-cell line lysates. Scherle et al. (1993) found that LyGDI bound RhoA and, in vitro, inhibited GDP dissociation from RhoA. Stimulation of T lymphocytes with phorbol ester led to phosphorylation of LyGDI. Independently, Lelias et al. (1993) cloned the LyGDI gene from human and from mouse, and designated it GDP-dissociation inhibitor D4. The sequence of the predicted 201-amino acid human protein was 67% identical to that of bovine RhoGDI. Mouse and human D4 shared 89% amino acid sequence identity. Leffers et al. (1993) identified 3 human proteins related to bovine RhoGDI and found that they corresponded to 3 proteins in the keratinocyte 2-dimensional-gel protein database, called IEF (for 'isoelectric focusing') 8120, IEF8118, and IEF1120. By screening an embryonic lung fibroblast library with an oligonucleotide based on the protein sequence of IEF8120, Leffers et al. (1993) isolated cDNAs encoding ARHGDIB. They reported that ARHGDIB had a pI of 4.79. Northern blot analysis revealed that ARHGDIB was expressed abundantly in lung, and at lower levels in several other tissues. Overexpression of ARHGDIB in mammalian cells caused them to 'round up' and disrupted the actin cytoskeleton, mimicking the phenotypic changes associated with inactivation of Rho proteins.

MAPPING

By fluorescence in situ hybridization, Adra et al. (1994) mapped the ARHGDIB gene to chromosome 12p12.3. ... More on the omim web site

Subscribe to this protein entry history

Feb. 10, 2018: 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 602843 was added.

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed