"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PF12166"	"{'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}"	"{}"	"[{'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}]"	""	""	""	"IPR031334"	False	False	False	"{'PUB00155396': {'PMID': 25242456, 'ISBN': None, 'volume': '22', 'issue': '10', 'year': 2014, 'title': 'The structure of a conserved piezo channel domain reveals a topologically distinct β sandwich fold.', 'URL': None, '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': None, 'volume': '573', 'issue': '7773', 'year': 2019, 'title': 'Structure and mechanogating of the mammalian tactile channel PIEZO2.', 'URL': None, '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': None, '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': None, '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': None, 'volume': '10', 'issue': '5', 'year': 2015, 'title': 'Ionic Selectivity and Permeation Properties of Human PIEZO1 Channels.', 'URL': None, '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': None, 'volume': '604', 'issue': '7905', 'year': 2022, 'title': 'Structure deformation and curvature sensing of PIEZO1 in lipid membranes.', 'URL': None, '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': None, 'volume': '483', 'issue': '7388', 'year': 2012, 'title': 'Piezo proteins are pore-forming subunits of mechanically activated channels.', 'URL': None, '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'}}"	""	"{'name': 'Piezo non-specific cation channel, cap domain', 'short': 'Piezo_cap'}"	""	"{'accession': '4rax', 'name': 'A regulatory domain of an ion channel'}"	""	"pfam"	"domain"	""