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{
"metadata": {
"accession": "PF12166",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "pfam",
"member_databases": null,
"integrated": "IPR031334",
"hierarchy": null,
"name": {
"name": "Piezo non-specific cation channel, cap domain",
"short": "Piezo_cap"
},
"description": [
{
"text": "<p>This is an extracellular domain at the C-terminus of Piezo, or FAM38 mechanosensitive non-specific cation channel proteins [[cite:PUB00075636],[cite:PUB00063634]]. Piezo is a family of proteins that form mechanosensitive non-specific cation channels whose conductance is higher for Li+, intermediate for Na+ and lowest for Li+. Divalent ions except for Mn2+ permeate the channel but more slowly than monovalent ions and can reduce K+ currents [[cite:PUB00075636],[cite:PUB00063634],[cite:PUB00155396],[cite:PUB00155399]]. These channels have a homotrimeric three-blade propeller-shaped structure that use a cap-motion and plug-and-latch mechanism to gate their ion-conducting pathways [[cite:PUB00063634],[cite:PUB00155396],[cite:PUB00155399]]. Each protomer consists of 38 TM helices that form unusual non-planar blades, and an extracellular cap-like structure, the latter represented in this entry [[cite:PUB00063634],[cite:PUB00155396],[cite:PUB00155399],[cite:PUB00155398]]. This domain is embedded in the centre of the trimer and may control the transmembrane constriction site suggested to act as a transmembrane gate [[cite:PUB00155398]]. This domain adopts a distinctive beta-sandwich fold [[cite:PUB00063634],[cite:PUB00155396],[cite:PUB00155399],[cite:PUB00155397],[cite:PUB00155398]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00155396": {
"PMID": 25242456,
"ISBN": null,
"volume": "22",
"issue": "10",
"year": 2014,
"title": "The structure of a conserved piezo channel domain reveals a topologically distinct β sandwich fold.",
"URL": null,
"raw_pages": "1520-7",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Kamajaya A",
"Kaiser JT",
"Lee J",
"Reid M",
"Rees DC."
],
"DOI_URL": "https://doi.org/10.1016/j.str.2014.08.009"
},
"PUB00155398": {
"PMID": 31435011,
"ISBN": null,
"volume": "573",
"issue": "7773",
"year": 2019,
"title": "Structure and mechanogating of the mammalian tactile channel PIEZO2.",
"URL": null,
"raw_pages": "225-229",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Wang L",
"Zhou H",
"Zhang M",
"Liu W",
"Deng T",
"Zhao Q",
"Li Y",
"Lei J",
"Li X",
"Xiao B."
],
"DOI_URL": "https://doi.org/10.1038/s41586-019-1505-8"
},
"PUB00075636": {
"PMID": 20016066,
"ISBN": null,
"volume": "123",
"issue": "Pt 1",
"year": 2010,
"title": "Integrin activation by Fam38A uses a novel mechanism of R-Ras targeting to the endoplasmic reticulum.",
"URL": null,
"raw_pages": "51-61",
"medline_journal": "J Cell Sci",
"ISO_journal": "J. Cell. Sci.",
"authors": [
"McHugh BJ",
"Buttery R",
"Lad Y",
"Banks S",
"Haslett C",
"Sethi T."
],
"DOI_URL": "http://dx.doi.org/10.1242/jcs.056424"
},
"PUB00155397": {
"PMID": 25955826,
"ISBN": null,
"volume": "10",
"issue": "5",
"year": 2015,
"title": "Ionic Selectivity and Permeation Properties of Human PIEZO1 Channels.",
"URL": null,
"raw_pages": "e0125503",
"medline_journal": "PLoS One",
"ISO_journal": "PLoS One",
"authors": [
"Gnanasambandam R",
"Bae C",
"Gottlieb PA",
"Sachs F."
],
"DOI_URL": "https://doi.org/10.1371/journal.pone.0125503"
},
"PUB00155399": {
"PMID": 35388220,
"ISBN": null,
"volume": "604",
"issue": "7905",
"year": 2022,
"title": "Structure deformation and curvature sensing of PIEZO1 in lipid membranes.",
"URL": null,
"raw_pages": "377-383",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Yang X",
"Lin C",
"Chen X",
"Li S",
"Li X",
"Xiao B."
],
"DOI_URL": "https://doi.org/10.1038/s41586-022-04574-8"
},
"PUB00063634": {
"PMID": 22343900,
"ISBN": null,
"volume": "483",
"issue": "7388",
"year": 2012,
"title": "Piezo proteins are pore-forming subunits of mechanically activated channels.",
"URL": null,
"raw_pages": "176-81",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Coste B",
"Xiao B",
"Santos JS",
"Syeda R",
"Grandl J",
"Spencer KS",
"Kim SE",
"Schmidt M",
"Mathur J",
"Dubin AE",
"Montal M",
"Patapoutian A."
],
"DOI_URL": "http://dx.doi.org/10.1038/nature10812"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 153,
"interactions": 0,
"matches": 7079,
"pathways": 0,
"proteins": 6621,
"proteomes": 1656,
"sets": 0,
"structural_models": {
"alphafold": 1217,
"bfvd": 0
},
"structures": 20,
"taxa": 5542
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 66,
"alignment:full": 4663
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "4rax",
"name": "A regulatory domain of an ion channel"
}
}
}
