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Piezo-type mechanosensitive ion channel component 1 (Membrane protein induced by beta-amyloid treatment) (Mib) (Protein FAM38A)

 PIEZ1_HUMAN             Reviewed;        2521 AA.
Q92508; A6NHT9; A7E2B7; Q0KKZ9;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
30-AUG-2017, entry version 143.
RecName: Full=Piezo-type mechanosensitive ion channel component 1;
AltName: Full=Membrane protein induced by beta-amyloid treatment;
Short=Mib;
AltName: Full=Protein FAM38A;
Name=PIEZO1; Synonyms=FAM38A, KIAA0233;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 432-2521, AND TISSUE SPECIFICITY.
PubMed=16854388; DOI=10.1016/j.brainres.2006.06.050;
Satoh K., Hata M., Takahara S., Tsuzaki H., Yokota H., Akatsu H.,
Yamamoto T., Kosaka K., Yamada T.;
"A novel membrane protein, encoded by the gene covering KIAA0233, is
transcriptionally induced in senile plaque-associated astrocytes.";
Brain Res. 1108:19-27(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-2521.
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-2521.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 955-972; 1324-1334; 1548-1562 AND 1656-1671,
VARIANTS DHS1 ARG-2225 AND HIS-2456, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22529292; DOI=10.1182/blood-2012-04-422253;
Zarychanski R., Schulz V.P., Houston B.L., Maksimova Y., Houston D.S.,
Smith B., Rinehart J., Gallagher P.G.;
"Mutations in the mechanotransduction protein PIEZO1 are associated
with hereditary xerocytosis.";
Blood 120:1908-1915(2012).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1391; SER-1646 AND
THR-1854, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2294.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1646, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20016066; DOI=10.1242/jcs.056424;
McHugh B.J., Buttery R., Lad Y., Banks S., Haslett C., Sethi T.;
"Integrin activation by Fam38A uses a novel mechanism of R-Ras
targeting to the endoplasmic reticulum.";
J. Cell Sci. 123:51-61(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1391 AND SER-1646, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-734; SER-758; SER-1391;
SER-1396; SER-1636; SER-1646 AND THR-1854, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1646, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
SUBCELLULAR LOCATION.
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).
[15]
VARIANTS DHS1 SER-718; SER-782; GLN-808; LEU-1117; ASP-2003; VAL-2020;
MET-2127; 2166-LYS--LYS-2169 DEL; HIS-2456 AND GLN-2488,
CHARACTERIZATION OF VARIANTS DHS1 HIS-2456 AND GLN-2488, FUNCTION,
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).
[16]
VARIANTS DHS1 PRO-1358; THR-2020; MET-2127 AND LEU-GLU-2496 INS,
CHARACTERIZATION OF VARIANTS DHS1 PRO-1358; THR-2020; MET-2127;
LEU-GLU-2496 INS; ARG-2225 AND HIS-2456, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=23695678; DOI=10.1038/ncomms2899;
Albuisson J., Murthy S.E., Bandell M., Coste B., Louis-Dit-Picard H.,
Mathur J., Feneant-Thibault M., Tertian G., de Jaureguiberry J.P.,
Syfuss P.Y., Cahalan S., Garcon L., Toutain F., Simon Rohrlich P.,
Delaunay J., Picard V., Jeunemaitre X., Patapoutian A.;
"Dehydrated hereditary stomatocytosis linked to gain-of-function
mutations in mechanically activated PIEZO1 ion channels.";
Nat. Commun. 4:1884-1884(2013).
[17]
VARIANTS DHS1 ARG-2225 AND HIS-2456, CHARACTERIZATION OF VARIANTS DHS1
ARG-2225 AND HIS-2456, AND MUTAGENESIS OF ARG-2456.
PubMed=23487776; DOI=10.1073/pnas.1219777110;
Bae C., Gnanasambandam R., Nicolai C., Sachs F., Gottlieb P.A.;
"Xerocytosis is caused by mutations that alter the kinetics of the
mechanosensitive channel PIEZO1.";
Proc. Natl. Acad. Sci. U.S.A. 110:E1162-1168(2013).
[18]
VARIANT DHS1 HIS-2456.
PubMed=23973043; DOI=10.1016/j.bcmd.2013.07.015;
Shmukler B.E., Vandorpe D.H., Rivera A., Auerbach M., Brugnara C.,
Alper S.L.;
"Dehydrated stomatocytic anemia due to the heterozygous mutation
R2456H in the mechanosensitive cation channel PIEZO1: a case report.";
Blood Cells Mol. Dis. 52:53-54(2014).
[19]
VARIANT DHS1 HIS-2456.
PubMed=23581886; DOI=10.1111/cge.12147;
Beneteau C., Thierry G., Blesson S., Le Vaillant C., Picard V.,
Bene M.C., Eveillard M., Le Caignec C.;
"Recurrent mutation in the PIEZO1 gene in two families of hereditary
xerocytosis with fetal hydrops.";
Clin. Genet. 85:293-295(2014).
[20]
INVOLVEMENT IN LMPH3, AND VARIANTS LMPH3 MET-939; LEU-2430; CYS-2456
AND LEU-2458.
PubMed=26333996; DOI=10.1038/ncomms9085;
Fotiou E., Martin-Almedina S., Simpson M.A., Lin S., Gordon K.,
Brice G., Atton G., Jeffery I., Rees D.C., Mignot C., Vogt J.,
Homfray T., Snyder M.P., Rockson S.G., Jeffery S., Mortimer P.S.,
Mansour S., Ostergaard P.;
"Novel mutations in PIEZO1 cause an autosomal recessive generalized
lymphatic dysplasia with non-immune hydrops fetalis.";
Nat. Commun. 6:8085-8085(2015).
-!- FUNCTION: Pore-forming subunit of a mechanosensitive non-specific
cation channel (PubMed:23479567, PubMed:23695678). 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 (PubMed:20016066). 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 (PubMed:25119035). Plays a key role in
blood vessel formation and vascular structure in both development
and adult physiology (By similarity).
{ECO:0000250|UniProtKB:E2JF22, ECO:0000269|PubMed:20016066,
ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:23695678,
ECO:0000269|PubMed:25119035}.
-!- SUBUNIT: Homotrimer. Interacts with PKD2. Interacts with STOML3.
{ECO:0000250|UniProtKB:E2JF22}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:20016066}; Multi-pass membrane protein.
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:0000305}. 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). {ECO:0000269|PubMed:22529292,
ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:25119035}.
-!- TISSUE SPECIFICITY: Expressed in numerous tissues. In normal
brain, expressed exclusively in neurons, not in astrocytes. In
Alzheimer disease brains, expressed in about half of the activated
astrocytes located around classical senile plaques. In Parkinson
disease substantia nigra, not detected in melanin-containing
neurons nor in activated astrocytes. Expressed in erythrocytes (at
protein level). {ECO:0000269|PubMed:16854388,
ECO:0000269|PubMed:22529292, ECO:0000269|PubMed:23479567}.
-!- DEVELOPMENTAL STAGE: At 17 weeks of gestation, strongly expressed
in hepatic erythroblasts. At that stage, also expressed in fetal
splenic plasma cells and in lymphatic vessel of fetal peritoneum.
In vitro, up-regulated during the erythroid differentiation of
CD34+ cells from healthy donors (at protein level).
{ECO:0000269|PubMed:23479567}.
-!- 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
mutations 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: Lymphedema, hereditary, 3 (LMPH3) [MIM:616843]: A severe
form of lymphedema, a chronic disabling condition which results in
swelling of the extremities due to altered lymphatic flow.
Patients with lymphedema suffer from recurrent local infections,
and physical impairment. LMPH3 manifests as generalized lymphatic
dysplasia, characterized by uniform, widespread lymphedema
affecting 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
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Piezo comes from the Greek 'piesi' meaning
pressure.
-!- SIMILARITY: Belongs to the PIEZO (TC 1.A.75) family.
{ECO:0000305}.
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EMBL; AC138028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB161230; BAF03565.1; -; mRNA.
EMBL; D87071; BAA13240.1; -; mRNA.
EMBL; BC150271; AAI50272.1; -; mRNA.
CCDS; CCDS54058.1; -.
RefSeq; NP_001136336.2; NM_001142864.3.
UniGene; Hs.377001; -.
UniGene; Hs.592074; -.
ProteinModelPortal; Q92508; -.
BioGrid; 115124; 15.
IntAct; Q92508; 10.
MINT; MINT-4991257; -.
STRING; 9606.ENSP00000301015; -.
TCDB; 1.A.75.1.1; the mechanical nociceptor, piezo (piezo) family.
iPTMnet; Q92508; -.
PhosphoSitePlus; Q92508; -.
BioMuta; PIEZO1; -.
DMDM; 317373533; -.
EPD; Q92508; -.
MaxQB; Q92508; -.
PaxDb; Q92508; -.
PeptideAtlas; Q92508; -.
PRIDE; Q92508; -.
Ensembl; ENST00000301015; ENSP00000301015; ENSG00000103335.
GeneID; 9780; -.
KEGG; hsa:9780; -.
UCSC; uc010vpb.3; human.
CTD; 9780; -.
DisGeNET; 9780; -.
GeneCards; MIR4722; -.
GeneCards; PIEZO1; -.
H-InvDB; HIX0022749; -.
H-InvDB; HIX0173225; -.
HGNC; HGNC:28993; PIEZO1.
HPA; HPA047185; -.
MalaCards; PIEZO1; -.
MIM; 194380; phenotype.
MIM; 611184; gene.
MIM; 616843; phenotype.
neXtProt; NX_Q92508; -.
OpenTargets; ENSG00000103335; -.
Orphanet; 3202; Dehydrated hereditary stomatocytosis.
eggNOG; KOG1893; Eukaryota.
eggNOG; ENOG410YVF6; LUCA.
GeneTree; ENSGT00390000013029; -.
HOVERGEN; HBG107901; -.
InParanoid; Q92508; -.
OMA; LLKAFWW; -.
OrthoDB; EOG091G0SD8; -.
PhylomeDB; Q92508; -.
TreeFam; TF314295; -.
ChiTaRS; PIEZO1; human.
GenomeRNAi; 9780; -.
PRO; PR:Q92508; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103335; -.
CleanEx; HS_FAM38A; -.
ExpressionAtlas; Q92508; baseline and differential.
Genevisible; Q92508; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA: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; ISS:UniProtKB.
GO; GO:0005261; F:cation channel activity; ISS:UniProtKB.
GO; GO:0008381; F:mechanically-gated ion channel activity; IBA:GO_Central.
GO; GO:0006812; P:cation transport; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IBA:GO_Central.
GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IMP:UniProtKB.
GO; GO:0033625; P:positive regulation of integrin activation; IMP:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
InterPro; IPR027272; Piezo.
InterPro; IPR031805; Piezo_dom.
InterPro; IPR031334; Piezo_RRas-bd_dom.
PANTHER; PTHR13167; PTHR13167; 1.
Pfam; PF15917; PIEZO; 1.
Pfam; PF12166; Piezo_RRas_bdg; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Hereditary hemolytic anemia;
Ion channel; Ion transport; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 2521 Piezo-type mechanosensitive ion channel
component 1.
/FTId=PRO_0000186817.
TRANSMEM 5 25 Helical. {ECO:0000255}.
TRANSMEM 27 47 Helical. {ECO:0000255}.
TRANSMEM 64 84 Helical. {ECO:0000255}.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TRANSMEM 194 214 Helical. {ECO:0000255}.
TRANSMEM 218 238 Helical. {ECO:0000255}.
TRANSMEM 248 268 Helical. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TRANSMEM 428 448 Helical. {ECO:0000255}.
TRANSMEM 460 480 Helical. {ECO:0000255}.
TRANSMEM 514 534 Helical. {ECO:0000255}.
TRANSMEM 579 599 Helical. {ECO:0000255}.
TRANSMEM 602 622 Helical. {ECO:0000255}.
TRANSMEM 629 649 Helical. {ECO:0000255}.
TRANSMEM 681 701 Helical. {ECO:0000255}.
TRANSMEM 823 843 Helical. {ECO:0000255}.
TRANSMEM 852 872 Helical. {ECO:0000255}.
TRANSMEM 926 946 Helical. {ECO:0000255}.
TRANSMEM 987 1007 Helical. {ECO:0000255}.
TRANSMEM 1043 1063 Helical. {ECO:0000255}.
TRANSMEM 1160 1180 Helical. {ECO:0000255}.
TRANSMEM 1184 1204 Helical. {ECO:0000255}.
TRANSMEM 1218 1240 Helical. {ECO:0000255}.
TRANSMEM 1247 1264 Helical. {ECO:0000255}.
TRANSMEM 1277 1297 Helical. {ECO:0000255}.
TRANSMEM 1678 1698 Helical. {ECO:0000255}.
TRANSMEM 1700 1720 Helical. {ECO:0000255}.
TRANSMEM 1734 1754 Helical. {ECO:0000255}.
TRANSMEM 1962 1982 Helical. {ECO:0000255}.
TRANSMEM 2003 2023 Helical. {ECO:0000255}.
TRANSMEM 2032 2052 Helical. {ECO:0000255}.
TRANSMEM 2061 2081 Helical. {ECO:0000255}.
TRANSMEM 2100 2122 Helical. {ECO:0000255}.
TRANSMEM 2129 2149 Helical. {ECO:0000255}.
TRANSMEM 2177 2197 Helical. {ECO:0000255}.
TOPO_DOM 2198 2431 Extracellular.
{ECO:0000250|UniProtKB:E2JF22}.
TRANSMEM 2432 2452 Helical. {ECO:0000255}.
COILED 1339 1368 {ECO:0000255}.
COMPBIAS 6 91 Leu-rich.
MOD_RES 734 734 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 758 758 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1391 1391 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1396 1396 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1636 1636 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1646 1646 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1854 1854 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2294 2294 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 2411 2415 {ECO:0000250|UniProtKB:E2JF22}.
VARIANT 718 718 G -> S (in DHS1; dbSNP:rs755885744).
{ECO:0000269|PubMed:23479567}.
/FTId=VAR_069822.
VARIANT 782 782 G -> S (in DHS1; dbSNP:rs200970763).
{ECO:0000269|PubMed:23479567}.
/FTId=VAR_069823.
VARIANT 808 808 R -> Q (in DHS1; dbSNP:rs202103485).
{ECO:0000269|PubMed:23479567}.
/FTId=VAR_069824.
VARIANT 939 939 L -> M (in LMPH3; unknown pathological
significance; found in compound
heterozygous state; dbSNP:rs201226914).
{ECO:0000269|PubMed:26333996}.
/FTId=VAR_076407.
VARIANT 1117 1117 S -> L (in DHS1; dbSNP:rs587777765).
{ECO:0000269|PubMed:23479567}.
/FTId=VAR_069825.
VARIANT 1358 1358 R -> P (in DHS1; gives rise to
mechanically activated currents that
inactivate more slowly than wild-type
currents; dbSNP:rs587776990).
{ECO:0000269|PubMed:23695678}.
/FTId=VAR_069826.
VARIANT 2003 2003 A -> D (in DHS1).
{ECO:0000269|PubMed:23479567}.
/FTId=VAR_069827.
VARIANT 2020 2020 A -> T (in DHS1; gives rise to
mechanically activated currents that
inactivate more slowly than wild-type
currents; dbSNP:rs587776989).
{ECO:0000269|PubMed:23695678}.
/FTId=VAR_069828.
VARIANT 2020 2020 A -> V (in DHS1; dbSNP:rs587777764).
{ECO:0000269|PubMed:23479567}.
/FTId=VAR_069829.
VARIANT 2127 2127 T -> M (in DHS1; gives rise to
mechanically activated currents that
inactivate more slowly than wild-type
currents; dbSNP:rs587776991).
{ECO:0000269|PubMed:23479567,
ECO:0000269|PubMed:23695678}.
/FTId=VAR_069830.
VARIANT 2166 2169 Missing (in DHS1).
{ECO:0000269|PubMed:23479567}.
/FTId=VAR_069831.
VARIANT 2225 2225 M -> R (in DHS1; gives rise to
mechanically activated currents that
inactivate more slowly than wild-type
currents; dbSNP:rs587776987).
{ECO:0000269|PubMed:22529292,
ECO:0000269|PubMed:23487776,
ECO:0000269|PubMed:23695678}.
/FTId=VAR_069832.
VARIANT 2430 2430 P -> L (in LMPH3; unknown pathological
significance; found in compound
heterozygous state; dbSNP:rs869025601).
{ECO:0000269|PubMed:26333996}.
/FTId=VAR_076408.
VARIANT 2456 2456 R -> C (in LMPH3; unknown pathological
significance; found in compound
heterozygous state).
{ECO:0000269|PubMed:26333996}.
/FTId=VAR_076409.
VARIANT 2456 2456 R -> H (in DHS1; gives rise to
mechanically activated currents that
inactivate more slowly than wild-type
currents; dbSNP:rs587776988).
{ECO:0000269|PubMed:22529292,
ECO:0000269|PubMed:23479567,
ECO:0000269|PubMed:23487776,
ECO:0000269|PubMed:23581886,
ECO:0000269|PubMed:23695678,
ECO:0000269|PubMed:23973043}.
/FTId=VAR_069833.
VARIANT 2458 2458 F -> L (in LMPH3; unknown pathological
significance; found in compound
heterozygous state; dbSNP:rs577860843).
{ECO:0000269|PubMed:26333996}.
/FTId=VAR_076410.
VARIANT 2488 2488 R -> Q (in DHS1; increased cation
transport in erythroid cells;
dbSNP:rs749288233).
{ECO:0000269|PubMed:23479567}.
/FTId=VAR_069834.
VARIANT 2496 2496 E -> ELE (in DHS1; gives rise to
mechanically activated currents that
inactivate more slowly than wild-type
currents). {ECO:0000269|PubMed:23695678}.
/FTId=VAR_069835.
MUTAGEN 2456 2456 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. {ECO:0000269|PubMed:23487776}.
CONFLICT 750 750 Missing (in Ref. 3; BAA13240 and 4;
AAI50272). {ECO:0000305}.
SEQUENCE 2521 AA; 286790 MW; 127A3DA3E7CBD2DD CRC64;
MEPHVLGAVL YWLLLPCALL AACLLRFSGL SLVYLLFLLL LPWFPGPTRC GLQGHTGRLL
RALLGLSLLF LVAHLALQIC LHIVPRLDQL LGPSCSRWET LSRHIGVTRL DLKDIPNAIR
LVAPDLGILV VSSVCLGICG RLARNTRQSP HPRELDDDER DVDASPTAGL QEAATLAPTR
RSRLAARFRV TAHWLLVAAG RVLAVTLLAL AGIAHPSALS SVYLLLFLAL CTWWACHFPI
STRGFSRLCV AVGCFGAGHL ICLYCYQMPL AQALLPPAGI WARVLGLKDF VGPTNCSSPH
ALVLNTGLDW PVYASPGVLL LLCYATASLR KLRAYRPSGQ RKEAAKGYEA RELELAELDQ
WPQERESDQH VVPTAPDTEA DNCIVHELTG QSSVLRRPVR PKRAEPREAS PLHSLGHLIM
DQSYVCALIA MMVWSITYHS WLTFVLLLWA CLIWTVRSRH QLAMLCSPCI LLYGMTLCCL
RYVWAMDLRP ELPTTLGPVS LRQLGLEHTR YPCLDLGAML LYTLTFWLLL RQFVKEKLLK
WAESPAALTE VTVADTEPTR TQTLLQSLGE LVKGVYAKYW IYVCAGMFIV VSFAGRLVVY
KIVYMFLFLL CLTLFQVYYS LWRKLLKAFW WLVVAYTMLV LIAVYTFQFQ DFPAYWRNLT
GFTDEQLGDL GLEQFSVSEL FSSILVPGFF LLACILQLHY FHRPFMQLTD MEHVSLPGTR
LPRWAHRQDA VSGTPLLREE QQEHQQQQQE EEEEEEDSRD EGLGVATPHQ ATQVPEGAAK
WGLVAERLLE LAAGFSDVLS RVQVFLRRLL ELHVFKLVAL YTVWVALKEV SVMNLLLVVL
WAFALPYPRF RPMASCLSTV WTCVIIVCKM LYQLKVVNPQ EYSSNCTEPF PNSTNLLPTE
ISQSLLYRGP VDPANWFGVR KGFPNLGYIQ NHLQVLLLLV FEAIVYRRQE HYRRQHQLAP
LPAQAVFASG TRQQLDQDLL GCLKYFINFF FYKFGLEICF LMAVNVIGQR MNFLVTLHGC
WLVAILTRRH RQAIARLWPN YCLFLALFLL YQYLLCLGMP PALCIDYPWR WSRAVPMNSA
LIKWLYLPDF FRAPNSTNLI SDFLLLLCAS QQWQVFSAER TEEWQRMAGV NTDRLEPLRG
EPNPVPNFIH CRSYLDMLKV AVFRYLFWLV LVVVFVTGAT RISIFGLGYL LACFYLLLFG
TALLQRDTRA RLVLWDCLIL YNVTVIISKN MLSLLACVFV EQMQTGFCWV IQLFSLVCTV
KGYYDPKEMM DRDQDCLLPV EEAGIIWDSV CFFFLLLQRR VFLSHYYLHV RADLQATALL
ASRGFALYNA ANLKSIDFHR RIEEKSLAQL KRQMERIRAK QEKHRQGRVD RSRPQDTLGP
KDPGLEPGPD SPGGSSPPRR QWWRPWLDHA TVIHSGDYFL FESDSEEEEE AVPEDPRPSA
QSAFQLAYQA WVTNAQAVLR RRQQEQEQAR QEQAGQLPTG GGPSQEVEPA EGPEEAAAGR
SHVVQRVLST AQFLWMLGQA LVDELTRWLQ EFTRHHGTMS DVLRAERYLL TQELLQGGEV
HRGVLDQLYT SQAEATLPGP TEAPNAPSTV SSGLGAEEPL SSMTDDMGSP LSTGYHTRSG
SEEAVTDPGE REAGASLYQG LMRTASELLL DRRLRIPELE EAELFAEGQG RALRLLRAVY
QCVAAHSELL CYFIIILNHM VTASAGSLVL PVLVFLWAML SIPRPSKRFW MTAIVFTEIA
VVVKYLFQFG FFPWNSHVVL RRYENKPYFP PRILGLEKTD GYIKYDLVQL MALFFHRSQL
LCYGLWDHEE DSPSKEHDKS GEEEQGAEEG PGVPAATTED HIQVEARVGP TDGTPEPQVE
LRPRDTRRIS LRFRRRKKEG PARKGAAAIE AEDREEEEGE EEKEAPTGRE KRPSRSGGRV
RAAGRRLQGF CLSLAQGTYR PLRRFFHDIL HTKYRAATDV YALMFLADVV DFIIIIFGFW
AFGKHSAATD ITSSLSDDQV PEAFLVMLLI QFSTMVVDRA LYLRKTVLGK LAFQVALVLA
IHLWMFFILP AVTERMFNQN VVAQLWYFVK CIYFALSAYQ IRCGYPTRIL GNFLTKKYNH
LNLFLFQGFR LVPFLVELRA VMDWVWTDTT LSLSSWMCVE DIYANIFIIK CSRETEKKYP
QPKGQKKKKI VKYGMGGLII LFLIAIIWFP LLFMSLVRSV VGVVNQPIDV TVTLKLGGYE
PLFTMSAQQP SIIPFTAQAY EELSRQFDPQ PLAMQFISQY SPEDIVTAQI EGSSGALWRI
SPPSRAQMKR ELYNGTADIT LRFTWNFQRD LAKGGTVEYA NEKHMLALAP NSTARRQLAS
LLEGTSDQSV VIPNLFPKYI RAPNGPEANP VKQLQPNEEA DYLGVRIQLR REQGAGATGF
LEWWVIELQE CRTDCNLLPM VIFSDKVSPP SLGFLAGYGI MGLYVSIVLV IGKFVRGFFS
EISHSIMFEE LPCVDRILKL CQDIFLVRET RELELEEELY AKLIFLYRSP ETMIKWTREK
E


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