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{
"metadata": {
"accession": "PS51741",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR031160",
"hierarchy": null,
"name": {
"name": "F-BAR domain profile",
"short": "F_BAR"
},
"description": [
{
"text": "<p>All eukaryotic cells are surrounded by a plasma membrane, and they also\ncontain multiple membrane-based organelles and structures inside cells. Thus\nmembrane remodeling is likely to be important for most cellular activities and\ndevelopment. The Bin-Amphiphysin-Rvs (BAR) domain superfamily of proteins has\nbeen found to play a major role in remodeling cellular membranes linked with\norganelle biogenesis, membrane trafficking, cell division, cell morphology and\ncell migration. The BAR domain superfamily of proteins is evolutionarily\nconserved with representative members present from yeast to man. Currently\nthere are three distinct families of BAR domain proteins: classical BAR, F-BAR (FCH-BAR e.g., Fes/CIP4 homology BAR e.g., Toca-1) and I-\nBAR (inverse-BAR e.g., IRSp53). The classical BAR, F-BAR, and I-BAR domains\nare structurally similar homodimeric modules with antiparallel arrangement of\nmonomers [[cite:PUB00074815]][[cite:PUB00043263]].\n\nThe F-BAR domain is emerging as an important player in membrane remodeling\npathways. F-BAR domain proteins couple membrane remodeling with actin dynamics\nassociated with endocytic pathways and filopodium formation. F-BAR domain\ncontaining proteins can be categorized into five sub-families based on their\nphylogeny which is consistent with the additional protein domains they\npossess, for example, RhoGAP domains, Cdc42 binding sites,\nSH2 domains, SH3 domains and tyrosine\nkinase domains [[cite:PUB00074815]]:\n\n - the Toca subfamily (FBP17, TRIP10 or CIP4, and Toca-1 or FBP1).\n - the Fps/Fes and Fer subfamily of non-receptor tyrosine kinases.\n - the Rho GTPase (RhoGAP) activating protein subfamily.\n - the syndaptin/pacsin subfamily.\n - the GAS7/PSTPI1/FCHO subfamily.\n\nThe N-terminal part (about one third) of the F-BAR domain was previously\ncharacterized as an FCH (FER-CIP4 homology) domain. However, the region of\nsequence similarity extends to an adjacent region with a coiled-coil (CC)\nstructure. Hence, the F-BAR domain (FCH+CC, ~300 amino acids) has also been\ncalled extended FC (EFC) domain. The F-BAR domain plays a role in dimerization\nand membrane phospholipid binding. It binds specifically to certain kinds of\nlipids and acts as a a dimeric membrane-binding curvature effector [[cite:PUB00043263]][[cite:PUB00068555]][[cite:PUB00074816]].\n\nThe F-BAR domain is composed of five helices. Its structure is composed of a\nshort N-terminal helix, three long alpha helices, and a short C-terminal helix\nfollowed by an extended peptide of 17 amino acids [[cite:PUB00043263]][[cite:PUB00040395]].\n\nThe profile we developed covers the entire F-BAR domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00074815": {
"PMID": 20585502,
"ISBN": null,
"volume": "3",
"issue": "2",
"year": 2010,
"title": "F-BAR domain proteins: Families and function.",
"URL": null,
"raw_pages": "116-21",
"medline_journal": "Commun Integr Biol",
"ISO_journal": "Commun Integr Biol",
"authors": [
"Ahmed S",
"Bu W",
"Lee RT",
"Maurer-Stroh S",
"Goh WI."
],
"DOI_URL": "http://dx.doi.org/10.4161/cib.3.2.10808"
},
"PUB00068555": {
"PMID": 16326391,
"ISBN": null,
"volume": "9",
"issue": "6",
"year": 2005,
"title": "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins.",
"URL": null,
"raw_pages": "791-804",
"medline_journal": "Dev Cell",
"ISO_journal": "Dev. Cell",
"authors": [
"Itoh T",
"Erdmann KS",
"Roux A",
"Habermann B",
"Werner H",
"De Camilli P."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.devcel.2005.11.005"
},
"PUB00040395": {
"PMID": 17512409,
"ISBN": null,
"volume": "129",
"issue": "4",
"year": 2007,
"title": "Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis.",
"URL": null,
"raw_pages": "761-72",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Shimada A",
"Niwa H",
"Tsujita K",
"Suetsugu S",
"Nitta K",
"Hanawa-Suetsugu K",
"Akasaka R",
"Nishino Y",
"Toyama M",
"Chen L",
"Liu ZJ",
"Wang BC",
"Yamamoto M",
"Terada T",
"Miyazawa A",
"Tanaka A",
"Sugano S",
"Shirouzu M",
"Nagayama K",
"Takenawa T",
"Yokoyama S."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.cell.2007.03.040"
},
"PUB00043263": {
"PMID": 17540576,
"ISBN": null,
"volume": "15",
"issue": "7",
"year": 2007,
"title": "Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.",
"URL": null,
"raw_pages": "839-52",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Henne WM",
"Kent HM",
"Ford MG",
"Hegde BG",
"Daumke O",
"Butler PJ",
"Mittal R",
"Langen R",
"Evans PR",
"McMahon HT."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.str.2007.05.002"
},
"PUB00074816": {
"PMID": 16418535,
"ISBN": null,
"volume": "172",
"issue": "2",
"year": 2006,
"title": "Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis.",
"URL": null,
"raw_pages": "269-79",
"medline_journal": "J Cell Biol",
"ISO_journal": "J. Cell Biol.",
"authors": [
"Tsujita K",
"Suetsugu S",
"Sasaki N",
"Furutani M",
"Oikawa T",
"Takenawa T."
],
"DOI_URL": "http://dx.doi.org/10.1083/jcb.200508091"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 49064,
"pathways": 0,
"proteins": 49045,
"proteomes": 2813,
"sets": 0,
"structural_models": {
"alphafold": 43355,
"bfvd": 2
},
"structures": 35,
"taxa": 7920
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "7aal",
"name": "Crystal structure of the F-BAR domain of PSTIPIP1, G258A mutant"
}
}
}
