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Piezo-type mechanosensitive ion channel component 1 (Protein FAM38A)

 PIEZ1_MOUSE             Reviewed;        2547 AA.
E2JF22;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 1.
25-OCT-2017, entry version 44.
RecName: Full=Piezo-type mechanosensitive ion channel component 1;
AltName: Full=Protein FAM38A;
Name=Piezo1; Synonyms=Fam38a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=20813920; DOI=10.1126/science.1193270;
Coste B., Mathur J., Schmidt M., Earley T.J., Ranade S., Petrus M.J.,
Dubin A.E., Patapoutian A.;
"Piezo1 and Piezo2 are essential components of distinct mechanically
activated cation channels.";
Science 330:55-60(2010).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1385 AND SER-1646, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627; SER-1631 AND
SER-1646, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22343900; DOI=10.1038/nature10812;
Coste B., Xiao B., Santos J.S., Syeda R., Grandl J., Spencer K.S.,
Kim S.E., Schmidt M., Mathur J., Dubin A.E., Montal M.,
Patapoutian A.;
"Piezo proteins are pore-forming subunits of mechanically activated
channels.";
Nature 483:176-181(2012).
[5]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=23479567; DOI=10.1182/blood-2013-02-482489;
Andolfo I., Alper S.L., De Franceschi L., Auriemma C., Russo R.,
De Falco L., Vallefuoco F., Esposito M.R., Vandorpe D.H.,
Shmukler B.E., Narayan R., Montanaro D., D'Armiento M., Vetro A.,
Limongelli I., Zuffardi O., Glader B.E., Schrier S.L., Brugnara C.,
Stewart G.W., Delaunay J., Iolascon A.;
"Multiple clinical forms of dehydrated hereditary stomatocytosis arise
from mutations in PIEZO1.";
Blood 121:3925-3935(2013).
[6]
INTERACTION WITH PKD2, AND FUNCTION.
PubMed=24157948; DOI=10.1038/embor.2013.170;
Peyronnet R., Martins J.R., Duprat F., Demolombe S., Arhatte M.,
Jodar M., Tauc M., Duranton C., Paulais M., Teulon J., Honore E.,
Patel A.;
"Piezo1-dependent stretch-activated channels are inhibited by
Polycystin-2 in renal tubular epithelial cells.";
EMBO Rep. 14:1143-1148(2013).
[7]
INTERACTION WITH STOML3.
PubMed=24662763; DOI=10.1038/ncomms4520;
Poole K., Herget R., Lapatsina L., Ngo H.D., Lewin G.R.;
"Tuning Piezo ion channels to detect molecular-scale movements
relevant for fine touch.";
Nat. Commun. 5:3520-3520(2014).
[8]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=24958852; DOI=10.1073/pnas.1409233111;
Ranade S.S., Qiu Z., Woo S.H., Hur S.S., Murthy S.E., Cahalan S.M.,
Xu J., Mathur J., Bandell M., Coste B., Li Y.S., Chien S.,
Patapoutian A.;
"Piezo1, a mechanically activated ion channel, is required for
vascular development in mice.";
Proc. Natl. Acad. Sci. U.S.A. 111:10347-10352(2014).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=25119035; DOI=10.1038/nature13701;
Li J., Hou B., Tumova S., Muraki K., Bruns A., Ludlow M.J., Sedo A.,
Hyman A.J., McKeown L., Young R.S., Yuldasheva N.Y., Majeed Y.,
Wilson L.A., Rode B., Bailey M.A., Kim H.R., Fu Z., Carter D.A.,
Bilton J., Imrie H., Ajuh P., Dear T.N., Cubbon R.M., Kearney M.T.,
Prasad R.K., Evans P.C., Ainscough J.F., Beech D.J.;
"Piezo1 integration of vascular architecture with physiological
force.";
Nature 515:279-282(2014).
[10]
STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS), X-RAY
CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 2214-2457, SUBUNIT, SUBCELLULAR
LOCATION, AND TOPOLOGY.
PubMed=26390154; DOI=10.1038/nature15247;
Ge J., Li W., Zhao Q., Li N., Chen M., Zhi P., Li R., Gao N., Xiao B.,
Yang M.;
"Architecture of the mammalian mechanosensitive Piezo1 channel.";
Nature 527:64-69(2015).
-!- FUNCTION: Pore-forming subunit of a mechanosensitive non-specific
cation channel. Generates currents characterized by a linear
current-voltage relationship that are sensitive to ruthenium red
and gadolinium. 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. In the kidney, may contribute to
the detection of intraluminal pressure changes and to urine flow
sensing. Acts as shear-stress sensor that promotes endothelial
cell organization and alignment in the direction of blood flow
through calpain activation. Plays a key role in blood vessel
formation and vascular structure in both development and adult
physiology. {ECO:0000269|PubMed:20813920,
ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:24157948,
ECO:0000269|PubMed:24958852, ECO:0000269|PubMed:25119035}.
-!- SUBUNIT: Homotrimer (PubMed:26390154). Interacts with PKD2
(PubMed:24157948). Interacts with STOML3 (PubMed:24662763).
{ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:24157948,
ECO:0000269|PubMed:24662763, ECO:0000269|PubMed:26390154}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-9837938, EBI-9837938;
O35245:Pkd2; NbExp=3; IntAct=EBI-9837938, EBI-9823400;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q92508}; Multi-pass membrane protein.
Endoplasmic reticulum-Golgi intermediate compartment membrane
{ECO:0000250|UniProtKB:Q0KL00}. Cell membrane
{ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:26390154}; Multi-
pass membrane protein {ECO:0000269|PubMed:26390154}. Cell
projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q92508}.
Note=In erythrocytes, located in the plasma membrane
(PubMed:23479567). Accumulates at the leading apical lamellipodia
of endothelial cells in response to shear stress (By similarity).
{ECO:0000250|UniProtKB:Q92508, ECO:0000269|PubMed:23479567}.
-!- TISSUE SPECIFICITY: Expressed in bladder, colon, kidney and skin.
Also expressed in bone marrow, liver, lung, spleen and
erythrocytes (at protein level). {ECO:0000269|PubMed:20813920,
ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:24958852}.
-!- DEVELOPMENTAL STAGE: Expressed at least from 9.5 dpc. Expression
levels increase up to 15.5 dpc and remain high at least until
birth. {ECO:0000269|PubMed:23479567}.
-!- DISRUPTION PHENOTYPE: Embryo lethality at midgestation with
defects in vascular remodeling. {ECO:0000269|PubMed:24958852,
ECO:0000269|PubMed:25119035}.
-!- MISCELLANEOUS: Piezo comes from the Greek 'piesi' meaning
pressure. {ECO:0000305|PubMed:20813920}.
-!- SIMILARITY: Belongs to the PIEZO (TC 1.A.75) family.
{ECO:0000305}.
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EMBL; HQ215520; ADN28064.1; -; mRNA.
UniGene; Mm.37324; -.
PDB; 3JAC; EM; 4.80 A; A/B/C=1-2547.
PDB; 4RAX; X-ray; 1.45 A; A=2214-2457.
PDBsum; 3JAC; -.
PDBsum; 4RAX; -.
ProteinModelPortal; E2JF22; -.
SMR; E2JF22; -.
DIP; DIP-59655N; -.
IntAct; E2JF22; 1.
STRING; 10090.ENSMUSP00000089777; -.
iPTMnet; E2JF22; -.
PhosphoSitePlus; E2JF22; -.
EPD; E2JF22; -.
MaxQB; E2JF22; -.
PaxDb; E2JF22; -.
PeptideAtlas; E2JF22; -.
PRIDE; E2JF22; -.
MGI; MGI:3603204; Piezo1.
eggNOG; KOG1893; Eukaryota.
eggNOG; ENOG410YVF6; LUCA.
InParanoid; E2JF22; -.
PRO; PR:E2JF22; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005261; F:cation channel activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008381; F:mechanically-gated ion channel activity; IDA:MGI.
GO; GO:0006812; P:cation transport; IMP:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IBA:GO_Central.
GO; GO:0050982; P:detection of mechanical stimulus; IMP:MGI.
GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0033625; P:positive regulation of integrin activation; ISS:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
InterPro; IPR027272; Piezo.
InterPro; IPR031805; Piezo_dom.
InterPro; IPR031334; Piezo_RRas-bd_dom.
PANTHER; PTHR13167; PTHR13167; 2.
Pfam; PF15917; PIEZO; 1.
Pfam; PF12166; Piezo_RRas_bdg; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Coiled coil;
Complete proteome; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 2547 Piezo-type mechanosensitive ion channel
component 1.
/FTId=PRO_0000403959.
TRANSMEM 5 25 Helical. {ECO:0000255}.
TRANSMEM 27 47 Helical. {ECO:0000255}.
TRANSMEM 62 82 Helical. {ECO:0000255}.
TRANSMEM 120 140 Helical. {ECO:0000255}.
TRANSMEM 217 237 Helical. {ECO:0000255}.
TRANSMEM 250 270 Helical. {ECO:0000255}.
TRANSMEM 317 337 Helical. {ECO:0000255}.
TRANSMEM 435 455 Helical. {ECO:0000255}.
TRANSMEM 467 487 Helical. {ECO:0000255}.
TRANSMEM 520 540 Helical. {ECO:0000255}.
TRANSMEM 577 597 Helical. {ECO:0000255}.
TRANSMEM 608 628 Helical. {ECO:0000255}.
TRANSMEM 635 655 Helical. {ECO:0000255}.
TRANSMEM 687 707 Helical. {ECO:0000255}.
TRANSMEM 818 838 Helical. {ECO:0000255}.
TRANSMEM 847 867 Helical. {ECO:0000255}.
TRANSMEM 921 941 Helical. {ECO:0000255}.
TRANSMEM 982 1002 Helical. {ECO:0000255}.
TRANSMEM 1006 1023 Helical. {ECO:0000255}.
TRANSMEM 1038 1058 Helical. {ECO:0000255}.
TRANSMEM 1155 1175 Helical. {ECO:0000255}.
TRANSMEM 1179 1199 Helical. {ECO:0000255}.
TRANSMEM 1207 1227 Helical. {ECO:0000255}.
TRANSMEM 1232 1252 Helical. {ECO:0000255}.
TRANSMEM 1272 1292 Helical. {ECO:0000255}.
TRANSMEM 1678 1698 Helical. {ECO:0000255}.
TRANSMEM 1700 1720 Helical. {ECO:0000255}.
TRANSMEM 1734 1754 Helical. {ECO:0000255}.
TRANSMEM 1978 1998 Helical. {ECO:0000255}.
TRANSMEM 2019 2039 Helical. {ECO:0000255}.
TRANSMEM 2048 2068 Helical. {ECO:0000255}.
TRANSMEM 2077 2097 Helical. {ECO:0000255}.
TRANSMEM 2145 2165 Helical. {ECO:0000255}.
TRANSMEM 2193 2213 Helical. {ECO:0000255}.
TOPO_DOM 2214 2457 Extracellular.
{ECO:0000269|PubMed:26390154}.
TRANSMEM 2458 2478 Helical. {ECO:0000255}.
COILED 1334 1365 {ECO:0000255}.
COMPBIAS 6 142 Leu-rich.
COMPBIAS 157 170 Asp-rich.
MOD_RES 758 758 Phosphoserine.
{ECO:0000250|UniProtKB:Q0KL00}.
MOD_RES 1385 1385 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 1390 1390 Phosphoserine.
{ECO:0000250|UniProtKB:Q92508}.
MOD_RES 1627 1627 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1631 1631 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1646 1646 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 2437 2441 {ECO:0000269|PubMed:26390154}.
STRAND 2224 2232 {ECO:0000244|PDB:4RAX}.
STRAND 2238 2243 {ECO:0000244|PDB:4RAX}.
STRAND 2247 2250 {ECO:0000244|PDB:4RAX}.
HELIX 2253 2263 {ECO:0000244|PDB:4RAX}.
HELIX 2267 2273 {ECO:0000244|PDB:4RAX}.
HELIX 2278 2280 {ECO:0000244|PDB:4RAX}.
STRAND 2281 2289 {ECO:0000244|PDB:4RAX}.
HELIX 2298 2310 {ECO:0000244|PDB:4RAX}.
STRAND 2315 2324 {ECO:0000244|PDB:4RAX}.
HELIX 2327 2329 {ECO:0000244|PDB:4RAX}.
STRAND 2334 2344 {ECO:0000244|PDB:4RAX}.
HELIX 2349 2357 {ECO:0000244|PDB:4RAX}.
STRAND 2366 2372 {ECO:0000244|PDB:4RAX}.
STRAND 2375 2378 {ECO:0000244|PDB:4RAX}.
STRAND 2380 2383 {ECO:0000244|PDB:4RAX}.
TURN 2388 2390 {ECO:0000244|PDB:4RAX}.
HELIX 2394 2397 {ECO:0000244|PDB:4RAX}.
STRAND 2398 2409 {ECO:0000244|PDB:4RAX}.
STRAND 2426 2434 {ECO:0000244|PDB:4RAX}.
STRAND 2443 2450 {ECO:0000244|PDB:4RAX}.
SEQUENCE 2547 AA; 292002 MW; 0C24CF18BDF502E3 CRC64;
MEPHVLGAGL YWLLLPCTLL AASLLRFNAL SLVYLLFLLL LPWLPGPSRH SIPGHTGRLL
RALLCLSLLF LVAHLAFQIC LHTVPHLDQF LGQNGSLWVK VSQHIGVTRL DLKDIFNTTR
LVAPDLGVLL ASSLCLGLCG RLTRKAGQSR RTQELQDDDD DDDDDDEDID AAPAVGLKGA
PALATKRRLW LASRFRVTAH WLLMTSGRTL VIVLLALAGI AHPSAFSSIY LVVFLAICTW
WSCHFPLSPL GFNTLCVMVS CFGAGHLICL YCYQTPFIQD MLPPGNIWAR LFGLKNFVDL
PNYSSPNALV LNTKHAWPIY VSPGILLLLY YTATSLLKLH KSCPSELRKE TPREDEEHEL
ELDHLEPEPQ ARDATQGEMP MTTEPDLDNC TVHVLTSQSP VRQRPVRPRL AELKEMSPLH
GLGHLIMDQS YVCALIAMMV WSIMYHSWLT FVLLLWACLI WTVRSRHQLA MLCSPCILLY
GLTLCCLRYV WAMELPELPT TLGPVSLHQL GLEHTRYPCL DLGAMLLYLL TFWLLLRQFV
KEKLLKKQKV PAALLEVTVA DTEPTQTQTL LRSLGELVTG IYVKYWIYVC AGMFIVVSFA
GRLVVYKIVY MFLFLLCLTL FQVYYTLWRK LLRVFWWLVV AYTMLVLIAV YTFQFQDFPT
YWRNLTGFTD EQLGDLGLEQ FSVSELFSSI LIPGFFLLAC ILQLHYFHRP FMQLTDLEHV
PPPGTRHPRW AHRQDAVSEA PLLEHQEEEE VFREDGQSMD GPHQATQVPE GTASKWGLVA
DRLLDLAASF SAVLTRIQVF VRRLLELHVF KLVALYTVWV ALKEVSVMNL LLVVLWAFAL
PYPRFRPMAS CLSTVWTCII IVCKMLYQLK IVNPHEYSSN CTEPFPNNTN LQPLEINQSL
LYRGPVDPAN WFGVRKGYPN LGYIQNHLQI LLLLVFEAVV YRRQEHYRRQ HQQAPLPAQA
VCADGTRQRL DQDLLSCLKY FINFFFYKFG LEICFLMAVN VIGQRMNFMV ILHGCWLVAI
LTRRRREAIA RLWPNYCLFL TLFLLYQYLL CLGMPPALCI DYPWRWSKAI PMNSALIKWL
YLPDFFRAPN STNLISDFLL LLCASQQWQV FSAERTEEWQ RMAGINTDHL EPLRGEPNPI
PNFIHCRSYL DMLKVAVFRY LFWLVLVVVF VAGATRISIF GLGYLLACFY LLLFGTTLLQ
KDTRAQLVLW DCLILYNVTV IISKNMLSLL SCVFVEQMQS NFCWVIQLFS LVCTVKGYYD
PKEMMTRDRD CLLPVEEAGI IWDSICFFFL LLQRRIFLSH YFLHVSADLK ATALQASRGF
ALYNAANLKS INFHRQIEEK SLAQLKRQMK RIRAKQEKYR QSQASRGQLQ SKDPQDPSQE
PGPDSPGGSS PPRRQWWRPW LDHATVIHSG DYFLFESDSE EEEEALPEDP RPAAQSAFQM
AYQAWVTNAQ TVLRQRRERA RQERAEQLAS GGDLNPDVEP VDVPEDEMAG RSHMMQRVLS
TMQFLWVLGQ ATVDGLTRWL RAFTKHHRTM SDVLCAERYL LTQELLRVGE VRRGVLDQLY
VGEDEATLSG PVETRDGPST ASSGLGAEEP LSSMTDDTSS PLSTGYNTRS GSEEIVTDAG
DLQAGTSLHG SQELLANART RMRTASELLL DRRLHIPELE EAERFEAQQG RTLRLLRAGY
QCVAAHSELL CYFIIILNHM VTASAASLVL PVLVFLWAML TIPRPSKRFW MTAIVFTEVM
VVTKYLFQFG FFPWNSYVVL RRYENKPYFP PRILGLEKTD SYIKYDLVQL MALFFHRSQL
LCYGLWDHEE DRYPKDHCRS SVKDREAKEE PEAKLESQSE TGTGHPKEPV LAGTPRDHIQ
GKGSIRSKDV IQDPPEDLKP RHTRHISIRF RRRKETPGPK GTAVMETEHE EGEGKETTER
KRPRHTQEKS KFRERMKAAG RRLQSFCVSL AQSFYQPLQR FFHDILHTKY RAATDVYALM
FLADIVDIII IIFGFWAFGK HSAATDIASS LSDDQVPQAF LFMLLVQFGT MVIDRALYLR
KTVLGKLAFQ VVLVVAIHIW MFFILPAVTE RMFSQNAVAQ LWYFVKCIYF ALSAYQIRCG
YPTRILGNFL TKKYNHLNLF LFQGFRLVPF LVELRAVMDW VWTDTTLSLS NWMCVEDIYA
NIFIIKCSRE TEKKYPQPKG QKKKKIVKYG MGGLIILFLI AIIWFPLLFM SLIRSVVGVV
NQPIDVTVTL KLGGYEPLFT MSAQQPSIVP FTPQAYEELS QQFDPYPLAM QFISQYSPED
IVTAQIEGSS GALWRISPPS RAQMKQELYN GTADITLRFT WNFQRDLAKG GTVEYTNEKH
TLELAPNSTA RRQLAQLLEG RPDQSVVIPH LFPKYIRAPN GPEANPVKQL QPDEEEDYLG
VRIQLRREQV GTGASGEQAG TKASDFLEWW VIELQDCKAD CNLLPMVIFS DKVSPPSLGF
LAGYGIVGLY VSIVLVVGKF VRGFFSEISH SIMFEELPCV DRILKLCQDI FLVRETRELE
LEEELYAKLI FLYRSPETMI KWTRERE


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