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Piezo-type mechanosensitive ion channel component 2 (Protein FAM38B)

 PIEZ2_HUMAN             Reviewed;        2752 AA.
Q9H5I5; B7Z812; M4GPJ9; Q6ZS91; Q8N787; Q8NAR6; Q9H5R4;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
22-NOV-2017, entry version 117.
RecName: Full=Piezo-type mechanosensitive ion channel component 2;
AltName: Full=Protein FAM38B;
Name=PIEZO2; Synonyms=C18orf30, C18orf58, FAM38B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ILE-1354 AND
ILE-2463.
TISSUE=Spinal ganglion;
Eijkelkamp N., Cox J., Torres J.M., Sang H.G., Wood J.N.;
"A role for Fam38b in mechanical hypersensitivity.";
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 713-1275 (ISOFORM 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 934-1595 (ISOFORM 1), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 2141-2752 (ISOFORM 2), AND VARIANT
ILE-1354.
TISSUE=Brain, Chondrocyte, Hepatoma, Lung, Teratocarcinoma, and
Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[4]
INVOLVEMENT IN DAIPT.
PubMed=27607563; DOI=10.1111/cge.12850;
Mahmud A.A., Nahid N.A., Nassif C., Sayeed M.S., Ahmed M.U.,
Parveen M., Khalil M.I., Islam M.M., Nahar Z., Rypens F., Hamdan F.F.,
Rouleau G.A., Hasnat A., Michaud J.L.;
"Loss of the proprioception and touch sensation channel PIEZO2 in
siblings with a progressive form of contractures.";
Clin. Genet. 91:470-475(2017).
[5]
INVOLVEMENT IN DAIPT, AND VARIANT DAIPT PRO-1685.
PubMed=27653382; DOI=10.1056/NEJMoa1602812;
Chesler A.T., Szczot M., Bharucha-Goebel D., Ceko M., Donkervoort S.,
Laubacher C., Hayes L.H., Alter K., Zampieri C., Stanley C.,
Innes A.M., Mah J.K., Grosmann C.M., Bradley N., Nguyen D.,
Foley A.R., Le Pichon C.E., Boennemann C.G.;
"The Role of PIEZO2 in Human Mechanosensation.";
N. Engl. J. Med. 375:1355-1364(2016).
[6]
VARIANTS DA5 PHE-802 AND GLU-2727 DEL, AND CHARACTERIZATION OF
VARIANTS DA5 PHE-802 AND GLU-2727 DEL.
PubMed=23487782; DOI=10.1073/pnas.1221400110;
Coste B., Houge G., Murray M.F., Stitziel N., Bandell M.,
Giovanni M.A., Philippakis A., Hoischen A., Riemer G., Steen U.,
Steen V.M., Mathur J., Cox J., Lebo M., Rehm H., Weiss S.T.,
Wood J.N., Maas R.L., Sunyaev S.R., Patapoutian A.;
"Gain-of-function mutations in the mechanically activated ion channel
PIEZO2 cause a subtype of distal arthrogryposis.";
Proc. Natl. Acad. Sci. U.S.A. 110:4667-4672(2013).
[7]
INVOLVEMENT IN DA3; DA5 AND MWKS, VARIANT MWKS CYS-2686, VARIANT DA3
HIS-2686, AND VARIANTS DA5 VAL-712; LEU-2718; PRO-2718 AND PRO-2739.
PubMed=24726473; DOI=10.1016/j.ajhg.2014.03.015;
University of Washington Center for Mendelian Genomics;
McMillin M.J., Beck A.E., Chong J.X., Shively K.M., Buckingham K.J.,
Gildersleeve H.I., Aracena M.I., Aylsworth A.S., Bitoun P.,
Carey J.C., Clericuzio C.L., Crow Y.J., Curry C.J., Devriendt K.,
Everman D.B., Fryer A., Gibson K., Giovannucci Uzielli M.L.,
Graham J.M. Jr., Hall J.G., Hecht J.T., Heidenreich R.A., Hurst J.A.,
Irani S., Krapels I.P., Leroy J.G., Mowat D., Plant G.T.,
Robertson S.P., Schorry E.K., Scott R.H., Seaver L.H., Sherr E.,
Splitt M., Stewart H., Stumpel C., Temel S.G., Weaver D.D.,
Whiteford M., Williams M.S., Tabor H.K., Smith J.D., Shendure J.,
Nickerson D.A., Bamshad M.J.;
"Mutations in PIEZO2 cause Gordon syndrome, Marden-Walker syndrome,
and distal arthrogryposis type 5.";
Am. J. Hum. Genet. 94:734-744(2014).
-!- FUNCTION: Component of a mechanosensitive channel required for
rapidly adapting mechanically activated (MA) currents. Required
for Merkel-cell mechanotransduction. Plays a major role in light-
touch mechanosensation. {ECO:0000250|UniProtKB:Q8CD54}.
-!- SUBUNIT: Homooligomer, most likely homotetramer. Interacts with
STOML3. {ECO:0000250|UniProtKB:Q8CD54}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9H5I5-1; Sequence=Displayed;
Name=2;
IsoId=Q9H5I5-2; Sequence=VSP_040472;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9H5I5-3; Sequence=VSP_040471;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9H5I5-4; Sequence=VSP_040630;
Note=No experimental confirmation available.;
-!- DISEASE: Arthrogryposis, distal, 5 (DA5) [MIM:108145]: A form of
distal arthrogryposis, a disease characterized by congenital joint
contractures that mainly involve two or more distal parts of the
limbs, in the absence of a primary neurological or muscle disease.
DA5 features include ocular abnormalities, typically ptosis,
ophthalmoplegia and/or strabismus, in addition to contractures of
the skeletal muscles. Some patients have pulmonary hypertension as
a result of restrictive lung disease.
{ECO:0000269|PubMed:23487782, ECO:0000269|PubMed:24726473}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Arthrogryposis, distal, 3 (DA3) [MIM:114300]: A form of
distal arthrogryposis, a disease characterized by congenital joint
contractures that mainly involve two or more distal parts of the
limbs, in the absence of a primary neurological or muscle disease.
DA3 features include short stature and cleft palate.
{ECO:0000269|PubMed:24726473}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Marden-Walker syndrome (MWKS) [MIM:248700]: A syndrome
characterized by a mask-like face with blepharophimosis,
micrognathia, cleft or high-arched palate, low-set ears,
congenital joint contractures, kyphoscoliosis, pectus excavatum or
carinatum, and arachnodactyly. Additional features include
decreased muscular mass, failure to thrive, renal anomalies,
hypoplastic corpus callosum, cerebellar vermis hypoplasia,
enlarged cisterna magna, and psychomotor retardation.
{ECO:0000269|PubMed:24726473}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Arthrogryposis, distal, with impaired proprioception and
touch (DAIPT) [MIM:617146]: A form of distal arthrogryposis, a
disease characterized by congenital joint contractures that mainly
involve two or more distal parts of the limbs, in the absence of a
primary neurological or muscle disease. DAIPT is an autosomal
recessive disease characterized by selective loss of
discriminative touch perception, ataxia, difficulty walking,
dysmetria, and progressive skeletal contractures.
{ECO:0000269|PubMed:27607563, ECO:0000269|PubMed:27653382}.
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}.
-!- SEQUENCE CAUTION:
Sequence=BAB15556.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15556.1; Type=Erroneous termination; Positions=2718; Note=Translated as Arg.; Evidence={ECO:0000305};
Sequence=BAB15641.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC03832.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
Sequence=BAC05412.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC05412.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence at the 3'end. Probable cloning artifact.; Evidence={ECO:0000305};
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EMBL; JN790819; AFC88283.1; -; mRNA.
EMBL; AK026797; BAB15556.1; ALT_SEQ; mRNA.
EMBL; AK027056; BAB15641.1; ALT_INIT; mRNA.
EMBL; AK092226; BAC03832.1; ALT_SEQ; mRNA.
EMBL; AK098782; BAC05412.1; ALT_SEQ; mRNA.
EMBL; AK127627; BAC87063.1; -; mRNA.
EMBL; AK302764; BAH13798.1; -; mRNA.
EMBL; AP001180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS11850.2; -. [Q9H5I5-1]
RefSeq; NP_071351.2; NM_022068.3. [Q9H5I5-1]
RefSeq; XP_011524026.1; XM_011525724.2. [Q9H5I5-4]
UniGene; Hs.436902; -.
ProteinModelPortal; Q9H5I5; -.
STRING; 9606.ENSP00000463094; -.
TCDB; 1.A.75.1.2; the mechanical nociceptor, piezo (piezo) family.
iPTMnet; Q9H5I5; -.
PhosphoSitePlus; Q9H5I5; -.
BioMuta; PIEZO2; -.
DMDM; 317373264; -.
MaxQB; Q9H5I5; -.
PaxDb; Q9H5I5; -.
PeptideAtlas; Q9H5I5; -.
PRIDE; Q9H5I5; -.
DNASU; 63895; -.
Ensembl; ENST00000302079; ENSP00000303316; ENSG00000154864. [Q9H5I5-2]
Ensembl; ENST00000503781; ENSP00000421377; ENSG00000154864. [Q9H5I5-1]
Ensembl; ENST00000538948; ENSP00000443129; ENSG00000154864. [Q9H5I5-3]
Ensembl; ENST00000580640; ENSP00000463094; ENSG00000154864. [Q9H5I5-4]
GeneID; 63895; -.
KEGG; hsa:63895; -.
UCSC; uc002koq.4; human. [Q9H5I5-1]
CTD; 63895; -.
DisGeNET; 63895; -.
EuPathDB; HostDB:ENSG00000154864.11; -.
GeneCards; PIEZO2; -.
HGNC; HGNC:26270; PIEZO2.
HPA; HPA015986; -.
HPA; HPA031974; -.
HPA; HPA031975; -.
HPA; HPA040616; -.
MalaCards; PIEZO2; -.
MIM; 108145; phenotype.
MIM; 114300; phenotype.
MIM; 248700; phenotype.
MIM; 613629; gene.
MIM; 617146; phenotype.
neXtProt; NX_Q9H5I5; -.
OpenTargets; ENSG00000154864; -.
Orphanet; 1154; Arthrogryposis with oculomotor limitation and electroretinal anomalies.
Orphanet; 376; Gordon syndrome.
Orphanet; 2461; Marden-Walker syndrome.
PharmGKB; PA134930761; -.
eggNOG; KOG1893; Eukaryota.
eggNOG; ENOG410YVF6; LUCA.
GeneTree; ENSGT00390000013029; -.
HOVERGEN; HBG060934; -.
InParanoid; Q9H5I5; -.
KO; K22128; -.
OMA; EMDDKFE; -.
OrthoDB; EOG091G0SD8; -.
PhylomeDB; Q9H5I5; -.
TreeFam; TF314295; -.
ChiTaRS; PIEZO2; human.
GenomeRNAi; 63895; -.
PRO; PR:Q9H5I5; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000154864; -.
CleanEx; HS_FAM38B; -.
ExpressionAtlas; Q9H5I5; baseline and differential.
Genevisible; Q9H5I5; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
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:0050974; P:detection of mechanical stimulus involved in sensory perception; ISS:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR027272; Piezo.
InterPro; IPR031805; Piezo_dom.
InterPro; IPR031334; Piezo_RRas-bd_dom.
PANTHER; PTHR13167; PTHR13167; 3.
Pfam; PF15917; PIEZO; 1.
Pfam; PF12166; Piezo_RRas_bdg; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome;
Disease mutation; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Polymorphism; Reference proteome;
Sensory transduction; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 2752 Piezo-type mechanosensitive ion channel
component 2.
/FTId=PRO_0000186818.
TRANSMEM 5 25 Helical. {ECO:0000255}.
TRANSMEM 27 47 Helical. {ECO:0000255}.
TRANSMEM 62 82 Helical. {ECO:0000255}.
TRANSMEM 119 139 Helical. {ECO:0000255}.
TRANSMEM 214 234 Helical. {ECO:0000255}.
TRANSMEM 237 257 Helical. {ECO:0000255}.
TRANSMEM 266 286 Helical. {ECO:0000255}.
TRANSMEM 336 356 Helical. {ECO:0000255}.
TRANSMEM 505 525 Helical. {ECO:0000255}.
TRANSMEM 541 561 Helical. {ECO:0000255}.
TRANSMEM 581 598 Helical. {ECO:0000255}.
TRANSMEM 678 698 Helical. {ECO:0000255}.
TRANSMEM 704 724 Helical. {ECO:0000255}.
TRANSMEM 732 752 Helical. {ECO:0000255}.
TRANSMEM 782 802 Helical. {ECO:0000255}.
TRANSMEM 932 952 Helical. {ECO:0000255}.
TRANSMEM 958 978 Helical. {ECO:0000255}.
TRANSMEM 985 1005 Helical. {ECO:0000255}.
TRANSMEM 1053 1073 Helical. {ECO:0000255}.
TRANSMEM 1134 1154 Helical. {ECO:0000255}.
TRANSMEM 1170 1190 Helical. {ECO:0000255}.
TRANSMEM 1217 1237 Helical. {ECO:0000255}.
TRANSMEM 1291 1311 Helical. {ECO:0000255}.
TRANSMEM 1315 1335 Helical. {ECO:0000255}.
TRANSMEM 1349 1371 Helical. {ECO:0000255}.
TRANSMEM 1404 1424 Helical. {ECO:0000255}.
TRANSMEM 1900 1920 Helical. {ECO:0000255}.
TRANSMEM 1935 1955 Helical. {ECO:0000255}.
TRANSMEM 1967 1987 Helical. {ECO:0000255}.
TRANSMEM 2191 2211 Helical. {ECO:0000255}.
TRANSMEM 2232 2252 Helical. {ECO:0000255}.
TRANSMEM 2260 2280 Helical. {ECO:0000255}.
TRANSMEM 2290 2310 Helical. {ECO:0000255}.
TRANSMEM 2327 2344 Helical. {ECO:0000255}.
TRANSMEM 2358 2378 Helical. {ECO:0000255}.
TRANSMEM 2406 2426 Helical. {ECO:0000255}.
TRANSMEM 2662 2682 Helical. {ECO:0000255}.
COILED 1458 1529 {ECO:0000255}.
COMPBIAS 453 480 Glu-rich.
COMPBIAS 609 668 Glu-rich.
COMPBIAS 852 901 Glu-rich.
COMPBIAS 2099 2135 Ser-rich.
MOD_RES 838 838 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CD54}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1013 1013 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1085 1085 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 2043 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040471.
VAR_SEQ 831 831 R -> SHAKVNGRVYLIINSIKKKLPIHQNE (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040630.
VAR_SEQ 2387 2449 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040472.
VARIANT 712 712 M -> V (in DA5; dbSNP:rs587777453).
{ECO:0000269|PubMed:24726473}.
/FTId=VAR_071817.
VARIANT 802 802 I -> F (in DA5; recovers faster from
inactivation; dbSNP:rs587777076).
{ECO:0000269|PubMed:23487782}.
/FTId=VAR_070938.
VARIANT 1354 1354 V -> I (in dbSNP:rs7234309).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.1}.
/FTId=VAR_071039.
VARIANT 1685 1685 R -> P (in DAIPT).
{ECO:0000269|PubMed:27653382}.
/FTId=VAR_077843.
VARIANT 2463 2463 V -> I (in dbSNP:rs3748428).
{ECO:0000269|Ref.1}.
/FTId=VAR_033925.
VARIANT 2686 2686 R -> C (in MWKS; dbSNP:rs587777451).
{ECO:0000269|PubMed:24726473}.
/FTId=VAR_071302.
VARIANT 2686 2686 R -> H (in DA3; dbSNP:rs587777450).
{ECO:0000269|PubMed:24726473}.
/FTId=VAR_071303.
VARIANT 2718 2718 R -> L (in DA5; dbSNP:rs587777452).
{ECO:0000269|PubMed:24726473}.
/FTId=VAR_071304.
VARIANT 2718 2718 R -> P (in DA5; dbSNP:rs587777452).
{ECO:0000269|PubMed:24726473}.
/FTId=VAR_071305.
VARIANT 2727 2727 Missing (in DA5; causes slowing of
inactivation of PIEZO2-dependent
mechanically activated currents as well
as significantly faster recovery from
inactivation compared to wild-type).
{ECO:0000269|PubMed:23487782}.
/FTId=VAR_071818.
VARIANT 2739 2739 S -> P (in DA5; dbSNP:rs587777454).
{ECO:0000269|PubMed:24726473}.
/FTId=VAR_071306.
CONFLICT 455 455 S -> F (in Ref. 2; BAC03832).
{ECO:0000305}.
CONFLICT 758 758 N -> D (in Ref. 2; BAC05412).
{ECO:0000305}.
CONFLICT 980 980 R -> C (in Ref. 2; BAC87063).
{ECO:0000305}.
CONFLICT 999 999 L -> S (in Ref. 2; BAC05412).
{ECO:0000305}.
CONFLICT 1175 1175 C -> G (in Ref. 2; BAC87063).
{ECO:0000305}.
SEQUENCE 2752 AA; 318064 MW; AD11A1FCEB6D0079 CRC64;
MASEVVCGLI FRLLLPICLA VACAFRYNGL SFVYLIYLLL IPLFSEPTKT TMQGHTGRLL
KSLCFISLSF LLLHIIFHIT LVSLEAQHRI APGYNCSTWE KTFRQIGFES LKGADAGNGI
RVFVPDIGMF IASLTIWLLC RNIVQKPVTD EAAQSNPEFE NEELAEGEKI DSEEALIYEE
DFNGGDGVEG ELEESTKLKM FRRLASVASK LKEFIGNMIT TAGKVVVTIL LGSSGMMLPS
LTSSVYFFVF LGLCTWWSWC RTFDPLLFSC LCVLLAIFTA GHLIGLYLYQ FQFFQEAVPP
NDYYARLFGI KSVIQTDCSS TWKIIVNPDL SWYHHANPIL LLVMYYTLAT LIRIWLQEPL
VQDEGTKEED KALACSPIQI TAGRRRSLWY ATHYPTDERK LLSMTQDDYK PSDGLLVTVN
GNPVDYHTIH PSLPMENGPG KADLYSTPQY RWEPSDESSE KREEEEEEKE EFEEERSREE
KRSIKVHAMV SVFQFIMKQS YICALIAMMA WSITYHSWLT FVLLIWSCTL WMIRNRRKYA
MISSPFMVVY GNLLLILQYI WSFELPEIKK VPGFLEKKEP GELASKILFT ITFWLLLRQH
LTEQKALQEK EALLSEVKIG SQENEEKDEE LQDIQVEGEP KEEEEEEAKE EKQERKKVEQ
EEAEEEDEQD IMKVLGNLVV AMFIKYWIYV CGGMFFFVSF EGKIVMYKII YMVLFLFCVA
LYQVHYEWWR KILKYFWMSV VIYTMLVLIF IYTYQFENFP GLWQNMTGLK KEKLEDLGLK
QFTVAELFTR IFIPTSFLLV CILHLHYFHD RFLELTDLKS IPSKEDNTIY RLAHPEGSLP
DLTMMHLTAS LEKPEVRKLA EPGEEKLEGY SEKAQKGDLG KDSEESEEDG EEEEESEEEE
ETSDLRNKWH LVIDRLTVLF LKFLEYFHKL QVFMWWILEL HIIKIVSSYI IWVSVKEVSL
FNYVFLISWA FALPYAKLRR LASSVCTVWT CVIIVCKMLY QLQTIKPENF SVNCSLPNEN
QTNIPFNELN KSLLYSAPID PTEWVGLRKS SPLLVYLRNN LLMLAILAFE VTIYRHQEYY
RGRNNLTAPV SRTIFHDITR LHLDDGLINC AKYFINYFFY KFGLETCFLM SVNVIGQRMD
FYAMIHACWL IAVLYRRRRK AIAEIWPKYC CFLACIITFQ YFICIGIPPA PCRDYPWRFK
GASFNDNIIK WLYFPDFIVR PNPVFLVYDF MLLLCASLQR QIFEDENKAA VRIMAGDNVE
ICMNLDAASF SQHNPVPDFI HCRSYLDMSK VIIFSYLFWF VLTIIFITGT TRISIFCMGY
LVACFYFLLF GGDLLLKPIK SILRYWDWLI AYNVFVITMK NILSIGACGY IGTLVHNSCW
LIQAFSLACT VKGYQMPAAN SPCTLPSGEA GIIWDSICFA FLLLQRRVFM SYYFLHVVAD
IKASQILASR GAELFQATIV KAVKARIEEE KKSMDQLKRQ MDRIKARQQK YKKGKERMLS
LTQEPGEGQD MQKLSEEDDE READKQKAKG KKKQWWRPWV DHASMVRSGD YYLFETDSEE
EEEEELKKED EEPPRRSAFQ FVYQAWITDP KTALRQRHKE KKRSAREERK RRRKGSKEGP
VEWEDREDEP IKKKSDGPDN IIKRIFNILK FTWVLFLATV DSFTTWLNSI SREHIDISTV
LRIERCMLTR EIKKGNVPTR ESIHMYYQNH IMNLSRESGL DTIDEHPGAA SGAQTAHRMD
SLDSHDSISS EPTQCTMLYS RQGTTETIEE VEAEQEEEAG STAPEPREAK EYEATGYDVG
AMGAEEASLT PEEELTQFST LDGDVEAPPS YSKAVSFEHL SFGSQDDSAG KNRMAVSPDD
SRTDKLGSSI LPPLTHELTA SELLLKKMFH DDELEESEKF YVGQPRFLLL FYAMYNTLVA
RSEMVCYFVI ILNHMVSASM ITLLLPILIF LWAMLSVPRP SRRFWMMAIV YTEVAIVVKY
FFQFGFFPWN KNVEVNKDKP YHPPNIIGVE KKEGYVLYDL IQLLALFFHR SILKCHGLWD
EDDMTESGMA REESDDELSL GHGRRDSSDS LKSINLAASV ESVHVTFPEQ QTAVRRKRSG
SSSEPSQRSS FSSNRSQRGS TSTRNSSQKG SSVLSIKQKG KRELYMEKLQ EHLIKAKAFT
IKKTLEIYVP IKQFFYNLIH PEYSAVTDVY VLMFLADTVD FIIIVFGFWA FGKHSAAADI
TSSLSEDQVP GPFLVMVLIQ FGTMVVDRAL YLRKTVLGKV IFQVILVFGI HFWMFFILPG
VTERKFSQNL VAQLWYFVKC VYFGLSAYQI RCGYPTRVLG NFLTKSYNYV NLFLFQGFRL
VPFLTELRAV MDWVWTDTTL SLSSWICVED IYAHIFILKC WRESEKRYPQ PRGQKKKKVV
KYGMGGMIIV LLICIVWFPL LFMSLIKSVA GVINQPLDVS VTITLGGYQP IFTMSAQQSQ
LKVMDQQSFN KFIQAFSRDT GAMQFLENYE KEDITVAELE GNSNSLWTIS PPSKQKMIHE
LLDPNSSFSV VFSWSIQRNL SLGAKSEIAT DKLSFPLKNI TRKNIAKMIA GNSTESSKTP
VTIEKIYPYY VKAPSDSNSK PIKQLLSENN FMDITIILSR DNTTKYNSEW WVLNLTGNRI
YNPNSQALEL VVFNDKVSPP SLGFLAGYGI MGLYASVVLV IGKFVREFFS GISHSIMFEE
LPNVDRILKL CTDIFLVRET GELELEEDLY AKLIFLYRSP ETMIKWTREK TN


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