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{
"metadata": {
"accession": "IPR001895",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0005085",
"name": "guanyl-nucleotide exchange factor activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0007264",
"name": "small GTPase-mediated signal transduction",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd00155": "RasGEF"
},
"profile": {
"PS50009": "Ras guanine-nucleotide exchange factors catalytic domain profile"
},
"smart": {
"SM00147": "Guanine nucleotide exchange factor for Ras-like small GTPases"
},
"pfam": {
"PF00617": "RasGEF domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR001895",
"name": "Ras guanine-nucleotide exchange factors catalytic domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Ras guanine-nucleotide exchange factors catalytic domain",
"short": "RASGEF_cat_dom"
},
"description": [
{
"text": "<p>This entry represents the catalytic domain of the Ras guanine-nucleotide exchange factors.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP [[cite:PUB00004087]] in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP [[cite:PUB00004162], [cite:PUB00001017]]. The latter proteins are known as guanine-nucleotide exchange (or releasing) factors (GEFs or GRFs) (or also as guanine-nucleotide dissociation stimulators (GDSs)). GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors [[cite:PUB00081668], [cite:PUB00000728]].</p>\n\n<p><P>The crystal structure of the GEF region of human Sos1 complexes with Ras has been solved [[cite:PUB00001237]]. The structure consists of two distinct α helical structural domains: the N-terminal domain which seems to have a purely structural role and the C-terminal domain which is sufficient for catalytic activity and contains all residues that interact with Ras. A main feature of the catalytic domain is the protrusion of a helical hairpin important for the nucleotide-exchange mechanism. The N-terminal domain is likely to be important for the stability and correct placement of the hairpin structure.</P></p>\n\n<p>Some proteins known to contain a Ras-GEF domain are listed below:</p>\n\n<ul>\n<li>Cdc25 from yeast.</li>\n<li>Scd25 from yeast.</li>\n<li>Ste6 from fission yeast.</li>\n<li>Son of sevenless (gene sos) from Drosophila and mammals.</li>\n<li>p140-RAS GRF (cdc25Mm) from mammals. This protein possesses both a domain belonging to the CDC25 family and one belonging to the CDC24 family.</li>\n<li>Bud5 from yeast, that may interact with the ras-like protein RSR1/BUD1.</li>\n<li>Lte1 from yeast, whose target protein is not yet known.</li>\n<li>ralGDS from mammals, which interacts with the ras-like proteins ralA and ralB [[cite:PUB00001237]].</li>\n</ul>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00004087": {
"PMID": 1898771,
"ISBN": null,
"volume": "349",
"issue": "6305",
"year": 1991,
"title": "The GTPase superfamily: conserved structure and molecular mechanism.",
"URL": null,
"raw_pages": "117-27",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Bourne HR",
"Sanders DA",
"McCormick F."
],
"DOI_URL": "http://dx.doi.org/10.1038/349117a0"
},
"PUB00081668": {
"PMID": 9438849,
"ISBN": null,
"volume": "279",
"issue": "5350",
"year": 1998,
"title": "Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos.",
"URL": null,
"raw_pages": "560-3",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Nimnual AS",
"Yatsula BA",
"Bar-Sagi D."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.279.5350.560"
},
"PUB00001017": {
"PMID": 15335949,
"ISBN": null,
"volume": "2",
"issue": "6",
"year": 1992,
"title": "Ras regulation: putting back the GTP.",
"URL": null,
"raw_pages": "329-31",
"medline_journal": "Curr Biol",
"ISO_journal": "Curr. Biol.",
"authors": [
"Downward J."
],
"DOI_URL": "http://dx.doi.org/10.1016/0960-9822(92)90897-J"
},
"PUB00001237": {
"PMID": 8094051,
"ISBN": null,
"volume": "12",
"issue": "1",
"year": 1993,
"title": "Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase.",
"URL": null,
"raw_pages": "339-47",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Albright CF",
"Giddings BW",
"Liu J",
"Vito M",
"Weinberg RA."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8094051&action=stream&blobtype=pdf"
},
"PUB00004162": {
"PMID": 8259209,
"ISBN": null,
"volume": "366",
"issue": "6456",
"year": 1993,
"title": "Proteins regulating Ras and its relatives.",
"URL": null,
"raw_pages": "643-54",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Boguski MS",
"McCormick F."
],
"DOI_URL": "http://dx.doi.org/10.1038/366643a0"
},
"PUB00000728": {
"PMID": 7786285,
"ISBN": null,
"volume": "17",
"issue": "5",
"year": 1995,
"title": "Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins.",
"URL": null,
"raw_pages": "395-404",
"medline_journal": "Bioessays",
"ISO_journal": "Bioessays",
"authors": [
"Quilliam LA",
"Khosravi-Far R",
"Huff SY",
"Der CJ."
],
"DOI_URL": "http://dx.doi.org/10.1002/bies.950170507"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR023578",
"name": "Ras guanine nucleotide exchange factor domain superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR036964",
"name": "Ras guanine-nucleotide exchange factor, catalytic domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 931,
"interactions": 0,
"matches": 64239,
"pathways": 231,
"proteins": 64128,
"proteomes": 2923,
"sets": 0,
"structural_models": {
"alphafold": 44771,
"bfvd": 7
},
"structures": 116,
"taxa": 8163
},
"entry_annotations": {
"alignment:seed": 577,
"alignment:full": 44517
},
"cross_references": {
"prositedoc": {
"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC00594",
"url": "http://prosite.expasy.org/PDOC00594"
}
]
},
"gp": {
"displayName": "Genome Properties",
"description": "Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.",
"rank": 45,
"accessions": [
{
"accession": "GenProp1548",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1548"
},
{
"accession": "GenProp1511",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1511"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "6v9n",
"name": "Expanding the Chemical Landscape of SOS1 Activators Using Fragment Based Methods"
}
}
}
