Summary: RHO protein GDP dissociation inhibitor
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RHO protein GDP dissociation inhibitor Edit Wikipedia article
| RHO protein GDP dissociation inhibitor | |||||||||
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| Structure of RHO guanine nucleotide dissociation inhibitor.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Rho_GDI | ||||||||
| Pfam | PF02115 | ||||||||
| InterPro | IPR000406 | ||||||||
| SCOP | 1rho | ||||||||
| SUPERFAMILY | 1rho | ||||||||
| OPM superfamily | 99 | ||||||||
| OPM protein | 1qvy | ||||||||
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RHO protein GDP dissociation inhibitor of Rho proteins (rho GDI), regulates GDP/GTP exchange.
The protein plays an important role in the activation of the oxygen superoxide-generating NADPH oxidase of phagocytes. This process requires the interaction of membrane-associated cytochrome b559 with 3 cytosolic components: p47-phox, p67-phox and a heterodimer of the small G-protein p21Rac1 and rho GDI.[2] The association of p21rac and GDI inhibits dissociation of GDP from p21rac, thereby maintaining it in an inactive form. The proteins are attached via a lipid tail on p21rac that binds to the hydrophobic region of GDI.[3] Dissociation of these proteins might be mediated by the release of lipids (e.g., arachidonate and phosphatidate) from membranes through the action of phospholipases.[3] The lipids may then compete with the lipid tail on p21rac for the hydrophobic pocket on GDI.
[edit] Human proteins containing this domain
[edit] References
- ^ Keep NH, Barnes M, Barsukov I, et al. (May 1997). "A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm". Structure 5 (5): 623–33. doi:10.1016/S0969-2126(97)00218-9. PMID 9195882.
- ^ Pick E, Gorzalczany Y, Engel S (1993). "Role of the rac1 p21-GDP-dissociation inhibitor for rho heterodimer in the activation of the superoxide-forming NADPH oxidase of macrophages". Eur. J. Biochem. 217 (1): 441–455. doi:10.1111/j.1432-1033.1993.tb18264.x. PMID 8223583.
- ^ a b Segal AW (1996). "The NADPH oxidase and chronic granulomatous disease". Mol. Med. Today (Regul. Ed.) 2 (3): 129–135. doi:10.1016/1357-4310(96)88723-5. PMID 8796870.
[edit] References
This article incorporates text from the public domain Pfam and InterPro IPR000406
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No Pfam abstract.
External database links
| HOMSTRAD: | Rho_GDI |
| PANDIT: | PF02115 |
| PRINTS: | PR00492 |
| Pseudofam: | PF02115 |
| SCOP: | 1rho |
| SYSTERS: | Rho_GDI |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000406
The GDP dissociation inhibitor for rho proteins, rho GDI, regulates GDP/GTP exchange by inhibiting the dissociation of GDP from them. The protein contains 204 amino acids, with a calculated Mr value of 23,421. Hydropathy analysis shows it to be largely hydrophilic, with a single hydrophobic region. Results of database searches suggest rho GDI is a novel protein, currently with no known homologue. The protein plays an important role in the activation of the superoxide (O2-)-generating NADPH oxidase of phagocytes. This process requires the interaction of membrane-associated cytochrome b559 with 3 cytosolic components: p47-phox, p67-phox and a heterodimer of the small G-protein p21rac1 and rho GDI [PUBMED:8223583]. The association of p21rac and GDI inhibits dissociation of GDP from p21rac, thereby maintaining it in an inactive form. The proteins are attached via a lipid tail on p21rac that binds to the hydrophobic region of GDI [PUBMED:8796870]. Dissociation of these proteins might be mediated by the release of lipids (e.g., arachidonate and phosphatidate) from membranes through the action of phospholipases [PUBMED:8796870]. The lipids may then compete with the lipid tail on p21rac for the hydrophobic pocket on GDI.Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | cytoplasm (GO:0005737) |
| Molecular function | Rho GDP-dissociation inhibitor activity (GO:0005094) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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| Seed (16) |
Full (507) |
Representative proteomes | NCBI (499) |
Meta (3) |
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| RP15 (79) |
RP35 (153) |
RP55 (234) |
RP75 (308) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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| Seed (16) |
Full (507) |
Representative proteomes | NCBI (499) |
Meta (3) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (79) |
RP35 (153) |
RP55 (234) |
RP75 (308) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | IPR000406 |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Mian N, Bateman A |
| Number in seed: | 16 |
| Number in full: | 507 |
| Average length of the domain: | 181.80 aa |
| Average identity of full alignment: | 38 % |
| Average coverage of the sequence by the domain: | 87.83 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 200 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
RasStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Rho_GDI domain has been found. There are 48 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence