PIEZ2_HUMAN
ID PIEZ2_HUMAN Reviewed; 2752 AA.
AC Q9H5I5; B7Z812; M4GPJ9; Q6ZS91; Q8N787; Q8NAR6; Q9H5R4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Piezo-type mechanosensitive ion channel component 2;
DE AltName: Full=Protein FAM38B;
GN Name=PIEZO2; Synonyms=C18orf30, C18orf58, FAM38B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ILE-1354 AND ILE-2463.
RC TISSUE=Spinal ganglion;
RA Eijkelkamp N., Cox J., Torres J.M., Sang H.G., Wood J.N.;
RT "A role for Fam38b in mechanical hypersensitivity.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 713-1275 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 934-1595 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
RP OF 2141-2752 (ISOFORM 2), AND VARIANT ILE-1354.
RC TISSUE=Brain, Chondrocyte, Hepatoma, Lung, Teratocarcinoma, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP INVOLVEMENT IN DAIPT.
RX PubMed=27607563; DOI=10.1111/cge.12850;
RA Mahmud A.A., Nahid N.A., Nassif C., Sayeed M.S., Ahmed M.U., Parveen M.,
RA Khalil M.I., Islam M.M., Nahar Z., Rypens F., Hamdan F.F., Rouleau G.A.,
RA Hasnat A., Michaud J.L.;
RT "Loss of the proprioception and touch sensation channel PIEZO2 in siblings
RT with a progressive form of contractures.";
RL Clin. Genet. 91:470-475(2017).
RN [5]
RP INVOLVEMENT IN DAIPT, AND VARIANT DAIPT PRO-1685.
RX PubMed=27653382; DOI=10.1056/nejmoa1602812;
RA Chesler A.T., Szczot M., Bharucha-Goebel D., Ceko M., Donkervoort S.,
RA Laubacher C., Hayes L.H., Alter K., Zampieri C., Stanley C., Innes A.M.,
RA Mah J.K., Grosmann C.M., Bradley N., Nguyen D., Foley A.R., Le Pichon C.E.,
RA Boennemann C.G.;
RT "The Role of PIEZO2 in Human Mechanosensation.";
RL N. Engl. J. Med. 375:1355-1364(2016).
RN [6]
RP VARIANTS DA5 PHE-802 AND GLU-2727 DEL, AND CHARACTERIZATION OF VARIANTS DA5
RP PHE-802 AND GLU-2727 DEL.
RX PubMed=23487782; DOI=10.1073/pnas.1221400110;
RA Coste B., Houge G., Murray M.F., Stitziel N., Bandell M., Giovanni M.A.,
RA Philippakis A., Hoischen A., Riemer G., Steen U., Steen V.M., Mathur J.,
RA Cox J., Lebo M., Rehm H., Weiss S.T., Wood J.N., Maas R.L., Sunyaev S.R.,
RA Patapoutian A.;
RT "Gain-of-function mutations in the mechanically activated ion channel
RT PIEZO2 cause a subtype of distal arthrogryposis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:4667-4672(2013).
RN [7]
RP INVOLVEMENT IN DA3; DA5 AND MWKS, VARIANT MWKS CYS-2686, VARIANT DA3
RP HIS-2686, AND VARIANTS DA5 VAL-712; LEU-2718; PRO-2718 AND PRO-2739.
RX PubMed=24726473; DOI=10.1016/j.ajhg.2014.03.015;
RG University of Washington Center for Mendelian Genomics;
RA McMillin M.J., Beck A.E., Chong J.X., Shively K.M., Buckingham K.J.,
RA Gildersleeve H.I., Aracena M.I., Aylsworth A.S., Bitoun P., Carey J.C.,
RA Clericuzio C.L., Crow Y.J., Curry C.J., Devriendt K., Everman D.B.,
RA Fryer A., Gibson K., Giovannucci Uzielli M.L., Graham J.M. Jr., Hall J.G.,
RA Hecht J.T., Heidenreich R.A., Hurst J.A., Irani S., Krapels I.P.,
RA Leroy J.G., Mowat D., Plant G.T., Robertson S.P., Schorry E.K., Scott R.H.,
RA Seaver L.H., Sherr E., Splitt M., Stewart H., Stumpel C., Temel S.G.,
RA Weaver D.D., Whiteford M., Williams M.S., Tabor H.K., Smith J.D.,
RA Shendure J., Nickerson D.A., Bamshad M.J.;
RT "Mutations in PIEZO2 cause Gordon syndrome, Marden-Walker syndrome, and
RT distal arthrogryposis type 5.";
RL Am. J. Hum. Genet. 94:734-744(2014).
CC -!- FUNCTION: Component of a mechanosensitive channel required for rapidly
CC adapting mechanically activated (MA) currents. Required for Merkel-cell
CC mechanotransduction. Plays a major role in light-touch
CC mechanosensation. {ECO:0000250|UniProtKB:Q8CD54}.
CC -!- SUBUNIT: Homooligomer, most likely homotetramer. Interacts with STOML3.
CC {ECO:0000250|UniProtKB:Q8CD54}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H5I5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H5I5-2; Sequence=VSP_040472;
CC Name=3;
CC IsoId=Q9H5I5-3; Sequence=VSP_040471;
CC Name=4;
CC IsoId=Q9H5I5-4; Sequence=VSP_040630;
CC -!- DISEASE: Arthrogryposis, distal, 5 (DA5) [MIM:108145]: A form of distal
CC arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. DA5
CC features include ocular abnormalities, typically ptosis,
CC ophthalmoplegia and/or strabismus, in addition to contractures of the
CC skeletal muscles. Some patients have pulmonary hypertension as a result
CC of restrictive lung disease. {ECO:0000269|PubMed:23487782,
CC ECO:0000269|PubMed:24726473}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Arthrogryposis, distal, 3 (DA3) [MIM:114300]: A form of distal
CC arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. DA3
CC features include short stature and cleft palate.
CC {ECO:0000269|PubMed:24726473}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Marden-Walker syndrome (MWKS) [MIM:248700]: A syndrome
CC characterized by a mask-like face with blepharophimosis, micrognathia,
CC cleft or high-arched palate, low-set ears, congenital joint
CC contractures, kyphoscoliosis, pectus excavatum or carinatum, and
CC arachnodactyly. Additional features include decreased muscular mass,
CC failure to thrive, renal anomalies, hypoplastic corpus callosum,
CC cerebellar vermis hypoplasia, enlarged cisterna magna, and psychomotor
CC retardation. {ECO:0000269|PubMed:24726473}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Arthrogryposis, distal, with impaired proprioception and touch
CC (DAIPT) [MIM:617146]: A form of distal arthrogryposis, a disease
CC characterized by congenital joint contractures that mainly involve two
CC or more distal parts of the limbs, in the absence of a primary
CC neurological or muscle disease. DAIPT is an autosomal recessive disease
CC characterized by selective loss of discriminative touch perception,
CC ataxia, difficulty walking, dysmetria, and progressive skeletal
CC contractures. {ECO:0000269|PubMed:27607563,
CC ECO:0000269|PubMed:27653382}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Piezo comes from the Greek 'piesi' meaning pressure.
CC -!- SIMILARITY: Belongs to the PIEZO (TC 1.A.75) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15556.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15556.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC03832.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=BAC05412.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC05412.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence at the 3'end. Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; JN790819; AFC88283.1; -; mRNA.
DR EMBL; AK026797; BAB15556.1; ALT_SEQ; mRNA.
DR EMBL; AK027056; BAB15641.1; ALT_INIT; mRNA.
DR EMBL; AK092226; BAC03832.1; ALT_SEQ; mRNA.
DR EMBL; AK098782; BAC05412.1; ALT_SEQ; mRNA.
DR EMBL; AK127627; BAC87063.1; -; mRNA.
DR EMBL; AK302764; BAH13798.1; -; mRNA.
DR EMBL; AP001180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11850.2; -. [Q9H5I5-1]
DR RefSeq; NP_071351.2; NM_022068.3. [Q9H5I5-1]
DR RefSeq; XP_011524026.1; XM_011525724.2. [Q9H5I5-4]
DR SMR; Q9H5I5; -.
DR BioGRID; 121975; 3.
DR IntAct; Q9H5I5; 1.
DR STRING; 9606.ENSP00000421377; -.
DR TCDB; 1.A.75.1.2; the mechanical nociceptor, piezo (piezo) family.
DR GlyGen; Q9H5I5; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H5I5; -.
DR PhosphoSitePlus; Q9H5I5; -.
DR BioMuta; PIEZO2; -.
DR DMDM; 317373264; -.
DR EPD; Q9H5I5; -.
DR jPOST; Q9H5I5; -.
DR MassIVE; Q9H5I5; -.
DR MaxQB; Q9H5I5; -.
DR PaxDb; Q9H5I5; -.
DR PeptideAtlas; Q9H5I5; -.
DR PRIDE; Q9H5I5; -.
DR ProteomicsDB; 80910; -. [Q9H5I5-1]
DR ProteomicsDB; 80911; -. [Q9H5I5-2]
DR ProteomicsDB; 80912; -. [Q9H5I5-3]
DR ProteomicsDB; 80913; -. [Q9H5I5-4]
DR Antibodypedia; 2900; 210 antibodies from 21 providers.
DR DNASU; 63895; -.
DR Ensembl; ENST00000302079.10; ENSP00000303316.6; ENSG00000154864.14. [Q9H5I5-2]
DR Ensembl; ENST00000503781.7; ENSP00000421377.3; ENSG00000154864.14. [Q9H5I5-1]
DR Ensembl; ENST00000580640.5; ENSP00000463094.1; ENSG00000154864.14. [Q9H5I5-4]
DR GeneID; 63895; -.
DR KEGG; hsa:63895; -.
DR UCSC; uc002koq.4; human. [Q9H5I5-1]
DR CTD; 63895; -.
DR DisGeNET; 63895; -.
DR GeneCards; PIEZO2; -.
DR HGNC; HGNC:26270; PIEZO2.
DR HPA; ENSG00000154864; Tissue enriched (brain).
DR MalaCards; PIEZO2; -.
DR MIM; 108145; phenotype.
DR MIM; 114300; phenotype.
DR MIM; 248700; phenotype.
DR MIM; 613629; gene.
DR MIM; 617146; phenotype.
DR neXtProt; NX_Q9H5I5; -.
DR OpenTargets; ENSG00000154864; -.
DR Orphanet; 1154; Arthrogryposis-oculomotor limitation-electroretinal anomalies syndrome.
DR Orphanet; 376; Gordon syndrome.
DR Orphanet; 2461; Marden-Walker syndrome.
DR PharmGKB; PA134930761; -.
DR VEuPathDB; HostDB:ENSG00000154864; -.
DR eggNOG; KOG1893; Eukaryota.
DR GeneTree; ENSGT00940000154456; -.
DR HOGENOM; CLU_031849_0_0_1; -.
DR InParanoid; Q9H5I5; -.
DR OrthoDB; 13738at2759; -.
DR PhylomeDB; Q9H5I5; -.
DR TreeFam; TF314295; -.
DR PathwayCommons; Q9H5I5; -.
DR SignaLink; Q9H5I5; -.
DR SIGNOR; Q9H5I5; -.
DR BioGRID-ORCS; 63895; 6 hits in 246 CRISPR screens.
DR ChiTaRS; PIEZO2; human.
DR GenomeRNAi; 63895; -.
DR Pharos; Q9H5I5; Tbio.
DR PRO; PR:Q9H5I5; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9H5I5; protein.
DR Bgee; ENSG00000154864; Expressed in sural nerve and 167 other tissues.
DR ExpressionAtlas; Q9H5I5; baseline and differential.
DR Genevisible; Q9H5I5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IBA:GO_Central.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB.
DR InterPro; IPR027272; Piezo.
DR InterPro; IPR031805; Piezo_dom.
DR InterPro; IPR031334; Piezo_RRas-bd_dom.
DR PANTHER; PTHR13167; PTHR13167; 1.
DR Pfam; PF15917; PIEZO; 1.
DR Pfam; PF12166; Piezo_RRas_bdg; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disease variant; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2752
FT /note="Piezo-type mechanosensitive ion channel component 2"
FT /id="PRO_0000186818"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 782..802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 958..978
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1053..1073
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1134..1154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1170..1190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1217..1237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1291..1311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1315..1335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1349..1371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1404..1424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1900..1920
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1935..1955
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1967..1987
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2191..2211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2232..2252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2260..2280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2290..2310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2327..2344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2358..2378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2406..2426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2662..2682
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 446..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1844..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2047..2069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1458..1529
FT /evidence="ECO:0000255"
FT COMPBIAS 459..473
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..647
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..901
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1610
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CD54"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1013
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1085
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..2043
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040471"
FT VAR_SEQ 831
FT /note="R -> SHAKVNGRVYLIINSIKKKLPIHQNE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040630"
FT VAR_SEQ 2387..2449
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040472"
FT VARIANT 712
FT /note="M -> V (in DA5; dbSNP:rs587777453)"
FT /evidence="ECO:0000269|PubMed:24726473"
FT /id="VAR_071817"
FT VARIANT 802
FT /note="I -> F (in DA5; recovers faster from inactivation;
FT dbSNP:rs587777076)"
FT /evidence="ECO:0000269|PubMed:23487782"
FT /id="VAR_070938"
FT VARIANT 1354
FT /note="V -> I (in dbSNP:rs7234309)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT /id="VAR_071039"
FT VARIANT 1685
FT /note="R -> P (in DAIPT; dbSNP:rs886039823)"
FT /evidence="ECO:0000269|PubMed:27653382"
FT /id="VAR_077843"
FT VARIANT 2463
FT /note="V -> I (in dbSNP:rs3748428)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_033925"
FT VARIANT 2686
FT /note="R -> C (in MWKS; dbSNP:rs587777451)"
FT /evidence="ECO:0000269|PubMed:24726473"
FT /id="VAR_071302"
FT VARIANT 2686
FT /note="R -> H (in DA3; dbSNP:rs587777450)"
FT /evidence="ECO:0000269|PubMed:24726473"
FT /id="VAR_071303"
FT VARIANT 2718
FT /note="R -> L (in DA5; dbSNP:rs587777452)"
FT /evidence="ECO:0000269|PubMed:24726473"
FT /id="VAR_071304"
FT VARIANT 2718
FT /note="R -> P (in DA5; dbSNP:rs587777452)"
FT /evidence="ECO:0000269|PubMed:24726473"
FT /id="VAR_071305"
FT VARIANT 2727
FT /note="Missing (in DA5; causes slowing of inactivation of
FT PIEZO2-dependent mechanically activated currents as well as
FT significantly faster recovery from inactivation compared to
FT wild-type)"
FT /evidence="ECO:0000269|PubMed:23487782"
FT /id="VAR_071818"
FT VARIANT 2739
FT /note="S -> P (in DA5; dbSNP:rs587777454)"
FT /evidence="ECO:0000269|PubMed:24726473"
FT /id="VAR_071306"
FT CONFLICT 455
FT /note="S -> F (in Ref. 2; BAC03832)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="N -> D (in Ref. 2; BAC05412)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="R -> C (in Ref. 2; BAC87063)"
FT /evidence="ECO:0000305"
FT CONFLICT 999
FT /note="L -> S (in Ref. 2; BAC05412)"
FT /evidence="ECO:0000305"
FT CONFLICT 1175
FT /note="C -> G (in Ref. 2; BAC87063)"
FT /evidence="ECO:0000305"
SQ 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
