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48  structures 274  species 1  interaction 507  sequences 6  architectures

Family: Rho_GDI (PF02115)

Summary: RHO protein GDP dissociation inhibitor

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This is the Wikipedia entry entitled "RHO protein GDP dissociation inhibitor". More...

RHO protein GDP dissociation inhibitor Edit Wikipedia article

RHO protein GDP dissociation inhibitor
PDB 1rho EBI.jpg
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

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.

Human proteins containing this domain[edit]

ARHGDIA; ARHGDIB; ARHGDIG;

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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. 

References[edit]

This article incorporates text from the public domain Pfam and InterPro IPR000406


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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External database links

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

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Domain organisation

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Alignments

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  Seed
(16)
Full
(507)
Representative proteomes NCBI
(499)
Meta
(3)
RP15
(79)
RP35
(153)
RP55
(234)
RP75
(308)
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  Seed
(16)
Full
(507)
Representative proteomes NCBI
(499)
Meta
(3)
RP15
(79)
RP35
(153)
RP55
(234)
RP75
(308)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.7 22.7
Trusted cut-off 22.9 22.8
Noise cut-off 21.9 21.7
Model length: 200
Family (HMM) version: 12
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Interactions

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Ras

Structures

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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