HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "PS50238",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR000198",
"hierarchy": null,
"name": {
"name": "Rho GTPase-activating proteins domain profile",
"short": "RHOGAP"
},
"description": [
{
"text": "<p>Small G proteins of the Rho family, which includes Rho, Rac and Cdc42,\nregulate phosphorylation pathways that control a range of biological functions\nincluding cytoskeleton formation and cell proliferation. Rho proteins act as\nmolecular switches, with an active GTP-bound form and an inactive GDP-bound\nform. The inactive GDP bound form is promoted by GTPase-activating proteins\n(GAPs). GAP proteins specific for Rho contain a conserved region of around 200\namino-acid residues, the Rho-GAP domain. This domain can accelerate the GTP\nhydrolysis activity of Rho by five orders of magnitude [[cite:PUB00018225]]. RhoGAP domains are\nusually associated with other signaling modules like SH2,\nSH3 or PH.\n\nLike other GAP domains Rho-GAP is exclusively helical (nine helices) [[cite:PUB00004251]]. The core of the domain forms a four-helix bundle. The most\nconserved residues across the family are located on the bundle face that\ninteracts with the G protein [[cite:PUB00004258]]. Rho-GAP domain like Ras-GAP supplies an\narginine residue in trans into the active site of the G protein which confers\na self-stimulatory GAP activity through homophilic interaction [[cite:PUB00018226]].\n\nSome of the proteins containing a RhoGAP domain are listed below:\n\n - Mammalian ARAP 1,2 and 3 proteins, a family of GTPase activating proteins\n that contains both a RhoGAP and a ARFGAP domains. They\n can regulate Rho or ARF G proteins according to their localization in the\n cell.\n - Vertebrate Beta-chimaerin protein, a GTPase activating protein for the Rho-\n like GTPase Rac.\n - Mammalian Nadrin protein, a neuron-specific GTPase-activating protein\n involved in regulated exocytosis.\n - Mammalian unconventional myosin-9b.\n - Mammalian breakpoint cluster region protein (BCR) and Drosophila Rotund\n protein, GTPase-activating proteins for Rac and Cdc42.\n - Mammalian Rho-GAP hematopoietic protein C1.\n - Mammalian Rho-GTPase-activating protein 6. It promotes continuous\n elongation of cytoplasmic processes during cell motility and simultaneous\n retraction of the cell body changing the cell morphology.\n - Mammalian phosphatidylinositol 3-kinase regulatory alpha subunit, an\n adapter subunit of the phosphatidylinositol 3-kinase (PI3K). It has a\n critical role in signal transduction pathways originating from a variety of\n membrane-bound receptors.\n - Mammalian Inositol polyphosphate 5-phosphatase OCRL-1 (EC 3.1.3.-). It may\n function in lysosomal membrane trafficking by regulating the specific pool\n of phosphatidylinositol 4,5-bisphosphate that is associated with lysosomes.\n - Mammalian type II inositol-1,4,5-trisphosphate 5-phosphatase involved in\n signal-terminating reaction (EC 3.1.3.56.).\n - Yeast LRG1 and SAC7 proteins, the two major Rho GTPase-activating proteins.\n The SAC7 protein is involved in assembly of actin.\n - Yeast BEM2 protein, a GTPase activating protein involved in the control of\n cellular morphogenesis.\n\nThe profile we developed covers the whole domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00018225": {
"PMID": 9631293,
"ISBN": null,
"volume": "8",
"issue": "2",
"year": 1998,
"title": "GTPase-activating proteins and their complexes.",
"URL": null,
"raw_pages": "195-201",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Gamblin SJ",
"Smerdon SJ."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0959-440X(98)80038-9"
},
"PUB00004251": {
"PMID": 9009196,
"ISBN": null,
"volume": "385",
"issue": "6615",
"year": 1997,
"title": "The structure of the GTPase-activating domain from p50rhoGAP.",
"URL": null,
"raw_pages": "458-61",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Barrett T",
"Xiao B",
"Dodson EJ",
"Dodson G",
"Ludbrook SB",
"Nurmahomed K",
"Gamblin SJ",
"Musacchio A",
"Smerdon SJ",
"Eccleston JF."
],
"DOI_URL": "http://dx.doi.org/10.1038/385458a0"
},
"PUB00004258": {
"PMID": 9262406,
"ISBN": null,
"volume": "388",
"issue": "6643",
"year": 1997,
"title": "Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP.",
"URL": null,
"raw_pages": "693-7",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Rittinger K",
"Walker PA",
"Eccleston JF",
"Nurmahomed K",
"Owen D",
"Laue E",
"Gamblin SJ",
"Smerdon SJ."
],
"DOI_URL": "http://dx.doi.org/10.1038/41805"
},
"PUB00018226": {
"PMID": 9338791,
"ISBN": null,
"volume": "389",
"issue": "6652",
"year": 1997,
"title": "Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue.",
"URL": null,
"raw_pages": "758-62",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Rittinger K",
"Walker PA",
"Eccleston JF",
"Smerdon SJ",
"Gamblin SJ."
],
"DOI_URL": "http://dx.doi.org/10.1038/39651"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 149345,
"pathways": 0,
"proteins": 148881,
"proteomes": 3622,
"sets": 0,
"structural_models": {
"alphafold": 112448,
"bfvd": 0
},
"structures": 66,
"taxa": 10307
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2osa",
"name": "The Rho-GAP domain of human N-chimaerin"
}
}
}
