Piezo1
entrez
361430
canonical
uniprot
Q0KL00
canonical
ensembl
ENSRNOG00000056786
resolver
ensp
ENSRNOP00000069995
resolver
ensp
ENSRNOP00000077382
resolver
enst
ENSRNOT00000091139
resolver
enst
ENSRNOT00000105150
resolver
genesymbol
Piezo1
resolver
genesymbol_syn
Fam38a
resolver
uniprot
A0A0G2JWS3
resolver
uniprot
A0A8I5Y135
resolver
uniprot_entry
A0A0G2JWS3_RAT
resolver
uniprot_entry
A0A8I5Y135_RAT
resolver
uniprot_entry
PIEZ1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by auxillary subunits MDFIC and MDFI (By similarity). Down-regulated by phosphatidylserines exposed on the cell surface (By similarity). Divalent ions decrease the single-channel permeability of K(+). {ECO:0000250|UniProtKB:E2JF22, ECO:0000250|UniProtKB:Q92508}.
uniprot
proteins
amino_acid_sequence
MEPHVLGAGLYWLLLPCTLLAASLLRFNALSLVYLLFLLLLPWLPGPSRHSIPGHTGRLLRALLCLSLLFLVAHVAFQICLHTMPRLNQLLGQNCNLWANVSQHIGVTRLDLKDIFNTTRLVAPDLGVLVASSLCLGLCGRLTRKARQSQRTQELEEDDIDAAPAAGLQGAPTLATKRRLWLAPRFRITAHWLLVTSGRMLVIVLLALAGIAHPSAFSSVYLMVFLAICTWWSCHFPLSSLGFNTLCVMVSCFGAGHLVCLYCYQTPFVQSVLLPGSLWARLFGLKNFVDIPNCSSPNVLVLNTKHAWPIYVSPGILLLLYYTATSLLKLRKGRFSELRKEIPREDEEHELELDQLEPEPQARGTTQGATPTTTGPDIDNCTVHVLTSQSPVRQRPVRPRLAELKEMSPLHGLGHLILDQSYVCALIAMMVWSIMYHSWLTFVLLLWACLIWTVRSRHQLAMLCSPCILLYGLTLCCLRYVWAMELPELPTTLGPVSLHQLGLEHTRYPCLDLGAMLLYLLTFWLLLRQFVKEKLLKKRKAPSTLLEVTVSDTEPTQTQTLLRSLGELVTGIYVKYWIYVCAGMFIVVSFAGRLVVYKIVYMFLFLLCLTLFQVYYTLWRKLLRVFWWLVVAYTMLVLIAVYTFQFQDFPTYWRNLTGFTDEQLGDLGLEQFSVSELFSSILIPGFFLLACILQLHYFHRPFMQLTDLEHVPPPGTRRLRWAHRQDTVSEAPLLQHQEEEEVFRDDGQSMDGPHQTTQVPEGTASKWGLVADRLLDLASSFSAVLTRIQVFVRCLLELHVFKLVALYTVWVALKEVSVMNLLLVVLWAFALPYPRFRPMASCLSTVWTCIIIVCKMLYQLKIVNPHEYSSNCTEPFPNNTNLQPLEISQSLLYRGPVDPANWFGVRKGYPNLGYIQNHLQILLLLVFEAVVYRRQEHYRRQHQQAPLPAQALCADGTRQRLDQDLLSCLKYFINFFFYKFGLEICFLMAVNVIGQRMNFMVILHGCWLVAILTRRRREAIARLWPNYCLFLTLFLLYQYLLCLGMPPALCIDYPWRWSQAIPMNSALIKWLYLPDFFRAPNSTNLISDFLLLLCASQQWQVFSAEQTEEWQRMAGVNTDHLEPLRGEPNPIPNFIHCRSYLDMLKVAVFRYLFWLVLVVVFVTGATRISIFGLGYLLACFYLLLFGTTLLQKDTRAQLVLWDCLILYNVTVIISKNMLSLLSCVFVEQMQSNFCWVIQLFSLVCTVKGYYDPKEMKTRDRDCLLPVEEAGIIWDSICFFFLLLQRRVFLSHYFLHVSADLKATALQASRGFALYNAANIKNINFHRQTEERSLAQLKRQMKRIRAKQEKYRQSQASRGQLQSTDPQEPGPDSPGGSSPPRTQWWRPWQDHATVIHSGDYFLFESDSEEEEEALPEDPRPAAQSAFQMAYQAWVTNAQTVLRQRREQARRDRAEQLASGGDLSPEVELVDVPENEMAGHSHVMQRVLSTMQFLWVLGQATVDGLTRWLRTFTKDHRTMSDVLCAERYLLTQELLRGGEVHRGVLDQLYVSEDEIALSGPVENRDGPSTASSGLGAEEPLSSMTDDTGSPLSTGYNTRSGSEEIITDTGGLQAGTSLHGSQELLANARTRMRTASELLLDRRLRIPELEEAEQFEAQQGRTLRLLRAMYQCVAAHSELLCYFIIILNHMVTASAASLVLPVLVFLWAMLTIPRPSKRFWMTAIVFTEVMVVTKYLFQFGFFPWNSYIVLRRYENKPYFPPRILGLEKTDSYIKYDLVQLMALFFHRSQLLCYGLWDHEEDGVPKDHCRSSEKDQEAEEESEAKLESQPETGTGHPEEPVLTGTPKDHIQGKGSVRSKDEIQDPPEDLKPQHRRHISIRFRRRKETQGPKGAAVVEAEHEEGEEGREAAGRKRLRRPREGLKIREKMKAAGRRLQSFCLSLAQSFYQPLRRFFHDILHTKYRAATDVYALMFLADIVDIVVIIFGFWAFGKHSAATDIASSLSDDQVPQAFLFMLLVQFGTMVIDRALYLRKTVLGNLAFQVVLVVAIHLWMFFILPAVTERMFRQNAVAQLWYFVKCIYFALSAYQIRCGYPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSNWMCVEDIYANIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLIRSVVGVVNQPIDVTVTLKLGGYEPLFTMSAQQPSIVPFTPEDYEELSQQFDPYPLAMQFISQYSPEDIVTAQIEGSSGALWRISPPSRAQMKHELYNGTADITLRFTWNFQRDLAKGGSVEYTNEKHTLELAPNSTARRQLAQLLEGRPDQSVVIPHLFPKYIRAPNGPEANPVKQLQPDEEEDYLGVRIQLRREQVGTGTSGEQAGTKASDFLEWWVIELQDCQAECNLLPMVIFSDKVSPPSLGFLAGYGIVGLYVSIVLVVGKFVRGFFSDISHSIMFEELPCVDRILKLCQDIFLVRETRELELEEELYAKLIFLYRSPETMIKWTREKE
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 (By similarity). 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 (By similarity). 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(+) (By similarity). Divalent ions except for Mn(2+) permeate the channel but more slowly than the monovalent ions and they also reduce K(+) currents (By similarity). 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 (By similarity). 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 (By similarity). 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 Ca(2+) influx followed by Rho GTPases signal transduction, leading to assembly of cortical actomyosin fibers and myotube formation (By similarity). {ECO:0000250|UniProtKB:E2JF22, ECO:0000250|UniProtKB:Q92508}.
uniprot
proteins
mass_dalton
290315
uniprot
proteins
protein_family
PIEZO (TC 1.A.75) family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16854388
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
2535
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16854388}; Multi-pass membrane protein {ECO:0000269|PubMed:16854388}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:16854388}. Cell membrane {ECO:0000269|PubMed:16854388}; Multi-pass membrane protein {ECO:0000269|PubMed:16854388}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q92508}. Note=In erythrocytes, located in the plasma membrane. Accumulates at the leading apical lamellipodia of endothelial cells in response to shear stress (By similarity). Colocalizes with F-actin and MYH9 at the actomyosin cortex in myoblasts. {ECO:0000250|UniProtKB:E2JF22, ECO:0000250|UniProtKB:Q92508}.
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 193..212; /note="Helical; Name=5"; TRANSMEM 215..234; /note="Helical; Name=6"; TRANSMEM 246..266; /note="Helical; Name=7"; TRANSMEM 308..328; /note="Helical; Name=8"; TRANSMEM 416..436; /note="Helical; Name=9"; TRANSMEM 439..454; /note="Helical; Name=10"; TRANSMEM 460..482; /note="Helical; Name=11"; TRANSMEM 510..527; /note="Helical; Name=12"; TRANSMEM 572..592; /note="Helical; Name=13"; TRANSMEM 594..614; /note="Helical; Name=14"; TRANSMEM 625..646; /note="Helical; Name=15"; TRANSMEM 677..693; /note="Helical; Name=16"; TRANSMEM 803..814; /note="Helical; Name=17"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 818..831; /note="Helical; Name=18"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 846..860; /note="Helical; Name=19"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 913..940; /note="Helical; Name=20"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 981..996; /note="Helical; Name=21"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 999..1014; /note="Helical; Name=22"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1028..1043; /note="Helical; Name=23"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1083..1104; /note="Helical; Name=24"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1140..1166; /note="Helical; Name=25"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1172..1190; /note="Helical; Name=26"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1204..1222; /note="Helical; Name=27"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1272..1288; /note="Helical; Name=28"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1644..1687; /note="Helical; Name=29"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1692..1707; /note="Helical; Name=30"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1716..1734; /note="Helical; Name=31"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1767..1788; /note="Helical; Name=32"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 1965..1984; /note="Helical; Name=33"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2005..2021; /note="Helical; Name=34"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2036..2056; /note="Helical; Name=35"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2065..2080; /note="Helical; Name=36"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2181..2201; /note="Helical; Name=37"; /evidence="ECO:0000250|UniProtKB:E2JF22"; TRANSMEM 2446..2466; /note="Helical; Name=38"; /evidence="ECO:0000250|UniProtKB:E2JF22
uniprot
proteins