PIEZO1
entrez
9780
canonical
uniprot
Q92508
canonical
ensembl
ENSG00000103335
resolver
ensp
ENSP00000301015
resolver
enst
ENST00000301015
resolver
genesymbol
PIEZO1
resolver
genesymbol_syn
FAM38A
resolver
genesymbol_syn
KIAA0233
resolver
hgnc
HGNC:28993
resolver
uniprot
A6NHT9
resolver
uniprot
A7E2B7
resolver
uniprot
Q0KKZ9
resolver
uniprot_entry
PIEZ1_HUMAN
resolver
uniprot_sec
A6NHT9
resolver
uniprot_sec
A7E2B7
resolver
uniprot_sec
Q0KKZ9
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by auxillary subunits MDFIC and MDFI (PubMed:37590348). Down-regulated by phosphatidylserines exposed on the cell surface. Divalent ions decrease the single-channel permeability of K(+) (PubMed:25955826). {ECO:0000269|PubMed:25955826, ECO:0000269|PubMed:29799007, ECO:0000269|PubMed:37590348}.
uniprot
proteins
amino_acid_sequence
MEPHVLGAVLYWLLLPCALLAACLLRFSGLSLVYLLFLLLLPWFPGPTRCGLQGHTGRLLRALLGLSLLFLVAHLALQICLHIVPRLDQLLGPSCSRWETLSRHIGVTRLDLKDIPNAIRLVAPDLGILVVSSVCLGICGRLARNTRQSPHPRELDDDERDVDASPTAGLQEAATLAPTRRSRLAARFRVTAHWLLVAAGRVLAVTLLALAGIAHPSALSSVYLLLFLALCTWWACHFPISTRGFSRLCVAVGCFGAGHLICLYCYQMPLAQALLPPAGIWARVLGLKDFVGPTNCSSPHALVLNTGLDWPVYASPGVLLLLCYATASLRKLRAYRPSGQRKEAAKGYEARELELAELDQWPQERESDQHVVPTAPDTEADNCIVHELTGQSSVLRRPVRPKRAEPREASPLHSLGHLIMDQSYVCALIAMMVWSITYHSWLTFVLLLWACLIWTVRSRHQLAMLCSPCILLYGMTLCCLRYVWAMDLRPELPTTLGPVSLRQLGLEHTRYPCLDLGAMLLYTLTFWLLLRQFVKEKLLKWAESPAALTEVTVADTEPTRTQTLLQSLGELVKGVYAKYWIYVCAGMFIVVSFAGRLVVYKIVYMFLFLLCLTLFQVYYSLWRKLLKAFWWLVVAYTMLVLIAVYTFQFQDFPAYWRNLTGFTDEQLGDLGLEQFSVSELFSSILVPGFFLLACILQLHYFHRPFMQLTDMEHVSLPGTRLPRWAHRQDAVSGTPLLREEQQEHQQQQQEEEEEEEDSRDEGLGVATPHQATQVPEGAAKWGLVAERLLELAAGFSDVLSRVQVFLRRLLELHVFKLVALYTVWVALKEVSVMNLLLVVLWAFALPYPRFRPMASCLSTVWTCVIIVCKMLYQLKVVNPQEYSSNCTEPFPNSTNLLPTEISQSLLYRGPVDPANWFGVRKGFPNLGYIQNHLQVLLLLVFEAIVYRRQEHYRRQHQLAPLPAQAVFASGTRQQLDQDLLGCLKYFINFFFYKFGLEICFLMAVNVIGQRMNFLVTLHGCWLVAILTRRHRQAIARLWPNYCLFLALFLLYQYLLCLGMPPALCIDYPWRWSRAVPMNSALIKWLYLPDFFRAPNSTNLISDFLLLLCASQQWQVFSAERTEEWQRMAGVNTDRLEPLRGEPNPVPNFIHCRSYLDMLKVAVFRYLFWLVLVVVFVTGATRISIFGLGYLLACFYLLLFGTALLQRDTRARLVLWDCLILYNVTVIISKNMLSLLACVFVEQMQTGFCWVIQLFSLVCTVKGYYDPKEMMDRDQDCLLPVEEAGIIWDSVCFFFLLLQRRVFLSHYYLHVRADLQATALLASRGFALYNAANLKSIDFHRRIEEKSLAQLKRQMERIRAKQEKHRQGRVDRSRPQDTLGPKDPGLEPGPDSPGGSSPPRRQWWRPWLDHATVIHSGDYFLFESDSEEEEEAVPEDPRPSAQSAFQLAYQAWVTNAQAVLRRRQQEQEQARQEQAGQLPTGGGPSQEVEPAEGPEEAAAGRSHVVQRVLSTAQFLWMLGQALVDELTRWLQEFTRHHGTMSDVLRAERYLLTQELLQGGEVHRGVLDQLYTSQAEATLPGPTEAPNAPSTVSSGLGAEEPLSSMTDDMGSPLSTGYHTRSGSEEAVTDPGEREAGASLYQGLMRTASELLLDRRLRIPELEEAELFAEGQGRALRLLRAVYQCVAAHSELLCYFIIILNHMVTASAGSLVLPVLVFLWAMLSIPRPSKRFWMTAIVFTEIAVVVKYLFQFGFFPWNSHVVLRRYENKPYFPPRILGLEKTDGYIKYDLVQLMALFFHRSQLLCYGLWDHEEDSPSKEHDKSGEEEQGAEEGPGVPAATTEDHIQVEARVGPTDGTPEPQVELRPRDTRRISLRFRRRKKEGPARKGAAAIEAEDREEEEGEEEKEAPTGREKRPSRSGGRVRAAGRRLQGFCLSLAQGTYRPLRRFFHDILHTKYRAATDVYALMFLADVVDFIIIIFGFWAFGKHSAATDITSSLSDDQVPEAFLVMLLIQFSTMVVDRALYLRKTVLGKLAFQVALVLAIHLWMFFILPAVTERMFNQNVVAQLWYFVKCIYFALSAYQIRCGYPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSSWMCVEDIYANIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLVRSVVGVVNQPIDVTVTLKLGGYEPLFTMSAQQPSIIPFTAQAYEELSRQFDPQPLAMQFISQYSPEDIVTAQIEGSSGALWRISPPSRAQMKRELYNGTADITLRFTWNFQRDLAKGGTVEYANEKHMLALAPNSTARRQLASLLEGTSDQSVVIPNLFPKYIRAPNGPEANPVKQLQPNEEADYLGVRIQLRREQGAGATGFLEWWVIELQECRTDCNLLPMVIFSDKVSPPSLGFLAGYGIMGLYVSIVLVIGKFVRGFFSEISHSIMFEELPCVDRILKLCQDIFLVRETRELELEEELYAKLIFLYRSPETMIKWTREKE
uniprot
proteins
disease_involvement
DISEASE: Dehydrated hereditary stomatocytosis 1 with or without pseudohyperkalemia and/or perinatal edema (DHS1) [MIM:194380]: An autosomal dominant hemolytic anemia characterized by primary erythrocyte dehydration. DHS erythrocytes exhibit decreased total cation and potassium content that are not accompanied by a proportional net gain of sodium and water. DHS patients typically exhibit mild to moderate compensated hemolytic anemia, with an increased erythrocyte mean corpuscular hemoglobin concentration and a decreased osmotic fragility, both of which reflect cellular dehydration. Patients may also show perinatal edema and pseudohyperkalemia due to loss of potassium from red cells stored at room temperature. A minor proportion of red cells appear as stomatocytes on blood films. Complications such as splenomegaly and cholelithiasis, resulting from increased red cell trapping in the spleen and elevated bilirubin levels, respectively, may occur. The course of DHS is frequently associated with iron overload, which may lead to hepatosiderosis. {ECO:0000269|PubMed:22529292, ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:23487776, ECO:0000269|PubMed:23581886, ECO:0000269|PubMed:23695678, ECO:0000269|PubMed:23973043}. Note=The disease is caused by variants affecting the gene represented in this entry. All disease-causing mutations characterized so far produce a gain-of-function phenotype, mutated channels exhibiting increased cation transport in erythroid cells, that could be due to slower channel inactivation rate compared to the wild-type protein.; DISEASE: Lymphatic malformation 6 (LMPHM6) [MIM:616843]: A form of primary lymphedema, a disease characterized by swelling of body parts due to developmental anomalies and functional defects of the lymphatic system. Patients with lymphedema may suffer from recurrent local infections. LMPHM6 is an autosomal recessive, severe form manifesting as generalized lymphatic dysplasia. It is characterized by uniform, widespread swelling of all segments of the body, with systemic involvement such as intestinal and/or pulmonary lymphangiectasia, pleural effusions, chylothoraces and/or pericardial effusions, and with a high incidence of non- immune hydrops fetalis. {ECO:0000269|PubMed:26333996}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Pore-forming subunit of the mechanosensitive non-specific cation Piezo channel required for rapidly adapting mechanically activated (MA) currents and has a key role in sensing touch and tactile pain (PubMed:23479567, PubMed:23695678, PubMed:25955826, PubMed:37590348). Piezo channels are homotrimeric three-blade propeller-shaped structures that utilize a cap-motion and plug-and-latch mechanism to gate their ion-conducting pathways (PubMed:37590348). Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium (By similarity). Conductance to monovalent alkali ions is highest for K(+), intermediate for Na(+) and lowest for Li(+) (PubMed:25955826). Divalent ions except for Mn(2+) permeate the channel but more slowly than the monovalent ions and they also reduce K(+) currents (PubMed:25955826). Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling (PubMed:20016066). In inner ear hair cells, PIEZO1/2 subunits may constitute part of the mechanotransducer (MET) non-selective cation channel complex where they may act as pore-forming ion-conducting component in the complex (By similarity). In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing (By similarity). Acts as a shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation (PubMed:25119035). Plays a key role in blood vessel formation and vascular structure in both development and adult physiology (By similarity). Acts as a sensor of phosphatidylserine (PS) flipping at the plasma membrane and governs morphogenesis of muscle cells (By similarity). In myoblasts, flippase-mediated PS enrichment at the inner leaflet of plasma membrane triggers channel activation and Ca2+ influx followed by Rho GTPases signal transduction, leading to assembly of cortical actomyosin fibers and myotube formation (PubMed:29799007). {ECO:0000250|UniProtKB:E2JF22, ECO:0000250|UniProtKB:Q91X60, ECO:0000269|PubMed:25955826, ECO:0000269|PubMed:29799007}.
uniprot
proteins
mass_dalton
286790
uniprot
proteins
mutagenesis
MUTAGEN 2456; /note="R->K: Does not inactivate the protein. gives rise to mechanically activated currents that inactivate more slowly than wild-type currents, suggesting it could shift the channel kinetics from phasic to tonic."; /evidence="ECO:0000269|PubMed:23487776
uniprot
proteins
protein_family
PIEZO (TC 1.A.75) family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16854388
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20016066
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
22529292
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23479567
uniprot
proteins
pubmed
23487776
uniprot
proteins
pubmed
23581886
uniprot
proteins
pubmed
23695678
uniprot
proteins
pubmed
23973043
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25119035
uniprot
proteins
pubmed
25955826
uniprot
proteins
pubmed
26333996
uniprot
proteins
pubmed
29799007
uniprot
proteins
pubmed
36122374
uniprot
proteins
pubmed
37590348
uniprot
proteins
pubmed
38184690
uniprot
proteins
pubmed
9039502
uniprot
proteins
sequence_length
2521
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20016066}; Multi-pass membrane protein {ECO:0000250|UniProtKB:E2JF22}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q0KL00}. Cell membrane {ECO:0000269|PubMed:22529292, ECO:0000269|PubMed:23479567}; Multi-pass membrane protein {ECO:0000250|UniProtKB:E2JF22}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:25119035}. Note=In erythrocytes, located in the plasma membrane (PubMed:22529292, PubMed:23479567). Accumulates at the leading apical lamellipodia of endothelial cells in response to shear stress (PubMed:25119035). Colocalizes with F-actin and MYH9 at the actomyosin cortex in myoblasts. {ECO:0000250|UniProtKB:E2JF22, ECO:0000269|PubMed:22529292, ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:25119035}.
uniprot
proteins
transmembrane_region
TRANSMEM 13..25; /note="Helical; Name=1"; TRANSMEM 29..44; /note="Helical; Name=2"; TRANSMEM 59..81; /note="Helical; Name=3"; TRANSMEM 122..138; /note="Helical; Name=4"; TRANSMEM 195..214; /note="Helical; Name=5"; TRANSMEM 217..236; /note="Helical; Name=6"; TRANSMEM 248..268; /note="Helical; Name=7"; TRANSMEM 310..330; /note="Helical; Name=8"; TRANSMEM 418..438; /note="Helical; Name=9"; TRANSMEM 441..456; /note="Helical; Name=10"; TRANSMEM 462..484; /note="Helical; Name=11"; TRANSMEM 513..530; /note="Helical; Name=12"; TRANSMEM 575..595; /note="Helical; Name=13"; TRANSMEM 597..617; /note="Helical; Name=14"; TRANSMEM 628..649; /note="Helical; Name=15"; TRANSMEM 680..696; /note="Helical; Name=16"; TRANSMEM 817..828; /note="Helical; Name=17"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 832..845; /note="Helical; Name=18"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 860..874; /note="Helical; Name=19"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 927..954; /note="Helical; Name=20"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 995..1010; /note="Helical; Name=21"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1013..1028; /note="Helical; Name=22"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1042..1057; /note="Helical; Name=23"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1097..1118; /note="Helical; Name=24"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1154..1180; /note="Helical; Name=25"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1186..1204; /note="Helical; Name=26"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1218..1236; /note="Helical; Name=27"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1286..1302; /note="Helical; Name=28"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1657..1700; /note="Helical; Name=29"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1705..1720; /note="Helical; Name=30"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1729..1747; /note="Helical; Name=31"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1780..1801; /note="Helical; Name=32"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1961..1980; /note="Helical; Name=33"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2001..2017; /note="Helical; Name=34"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2032..2052; /note="Helical; Name=35"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2061..2076; /note="Helical; Name=36"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2177..2197; /note="Helical; Name=37"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2432..2452; /note="Helical; Name=38"; /evidence="ECO:0000250|UniProtKB:E2JF22
uniprot
proteins