{"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"}}}