ID PIEZ2_MOUSE Reviewed; 2822 AA.
AC Q8CD54; E2JF23; Q8BSM4; Q9D341;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 27-NOV-2024, entry version 138.
DE RecName: Full=Piezo-type mechanosensitive ion channel component 2;
DE AltName: Full=Protein FAM38B {ECO:0000303|PubMed:20813920};
GN Name=Piezo2 {ECO:0000312|MGI:MGI:1918781};
GN Synonyms=Fam38b {ECO:0000303|PubMed:20813920};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=20813920; DOI=10.1126/science.1193270;
RA Coste B., Mathur J., Schmidt M., Earley T.J., Ranade S., Petrus M.J.,
RA Dubin A.E., Patapoutian A.;
RT "Piezo1 and Piezo2 are essential components of distinct mechanically
RT activated cation channels.";
RL Science 330:55-60(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-2822 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2049-2822 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2142-2822 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Colon, Forelimb, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND HOMOOLIGOMERIZATION.
RX PubMed=22343900; DOI=10.1038/nature10812;
RA Coste B., Xiao B., Santos J.S., Syeda R., Grandl J., Spencer K.S.,
RA Kim S.E., Schmidt M., Mathur J., Dubin A.E., Montal M., Patapoutian A.;
RT "Piezo proteins are pore-forming subunits of mechanically activated
RT channels.";
RL Nature 483:176-181(2012).
RN [5]
RP INTERACTION WITH STOML3, AND TISSUE SPECIFICITY.
RX PubMed=24662763; DOI=10.1038/ncomms4520;
RA Poole K., Herget R., Lapatsina L., Ngo H.D., Lewin G.R.;
RT "Tuning Piezo ion channels to detect molecular-scale movements relevant for
RT fine touch.";
RL Nat. Commun. 5:3520-3520(2014).
RN [6]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=24717433; DOI=10.1038/nature13251;
RA Woo S.H., Ranade S., Weyer A.D., Dubin A.E., Baba Y., Qiu Z., Petrus M.,
RA Miyamoto T., Reddy K., Lumpkin E.A., Stucky C.L., Patapoutian A.;
RT "Piezo2 is required for Merkel-cell mechanotransduction.";
RL Nature 509:622-626(2014).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25471886; DOI=10.1038/nature13980;
RA Ranade S.S., Woo S.H., Dubin A.E., Moshourab R.A., Wetzel C., Petrus M.,
RA Mathur J., Begay V., Coste B., Mainquist J., Wilson A.J., Francisco A.G.,
RA Reddy K., Qiu Z., Wood J.N., Lewin G.R., Patapoutian A.;
RT "Piezo2 is the major transducer of mechanical forces for touch sensation in
RT mice.";
RL Nature 516:121-125(2014).
RN [8]
RP FUNCTION, INTERACTION WITH TMC7, AND TISSUE SPECIFICITY.
RX PubMed=38568807; DOI=10.1016/j.celrep.2024.114014;
RA Zhang X., Shao J., Wang C., Liu C., Hao H., Li X., An Y., He J., Zhao W.,
RA Zhao Y., Kong Y., Jia Z., Wan S., Yuan Y., Zhang H., Zhang H., Du X.;
RT "TMC7 functions as a suppressor of Piezo2 in primary sensory neurons
RT blunting peripheral mechanotransduction.";
RL Cell Rep. 43:114014-114014(2024).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH TMC1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 2767-MET--GLU-2770.
RX PubMed=38228630; DOI=10.1038/s41467-023-44230-x;
RA Lee J.H., Perez-Flores M.C., Park S., Kim H.J., Chen Y., Kang M.,
RA Kersigo J., Choi J., Thai P.N., Woltz R.L., Perez-Flores D.C., Perkins G.,
RA Sihn C.R., Trinh P., Zhang X.D., Sirish P., Dong Y., Feng W.W.,
RA Pessah I.N., Dixon R.E., Sokolowski B., Fritzsch B., Chiamvimonvat N.,
RA Yamoah E.N.;
RT "The Piezo channel is a mechano-sensitive complex component in the
RT mammalian inner ear hair cell.";
RL Nat. Commun. 15:526-526(2024).
RN [10] {ECO:0007744|PDB:6KG7}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), DISULFIDE BONDS,
RP SUBUNIT, FUNCTION, TRANSPORTER ACTIVITY, TOPOLOGY, AND MUTAGENESIS OF
RP GLU-2757.
RX PubMed=31435011; DOI=10.1038/s41586-019-1505-8;
RA Wang L., Zhou H., Zhang M., Liu W., Deng T., Zhao Q., Li Y., Lei J., Li X.,
RA Xiao B.;
RT "Structure and mechanogating of the mammalian tactile channel PIEZO2.";
RL Nature 573:225-229(2019).
CC -!- FUNCTION: Pore-forming subunit of the mechanosensitive non-specific
CC cation Piezo channel required for rapidly adapting mechanically
CC activated (MA) currents and has a key role in sensing touch and tactile
CC pain (PubMed:20813920, PubMed:24717433, PubMed:31435011). Piezo
CC channels are homotrimeric three-blade propeller-shaped structure that
CC utilize a cap-motion and plug-and-latch mechanism to gate their ion-
CC conducting pathways (PubMed:31435011). In inner ear hair cells,
CC PIEZO1/2 subunits may constitute part of the mechanotransducer (MET)
CC non-selective cation channel complex where they may act as pore-forming
CC ion-conducting component in the complex (PubMed:38228630). Required for
CC Merkel-cell mechanotransduction (PubMed:24717433). Plays a major role
CC in light-touch mechanosensation (PubMed:25471886).
CC {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:24717433,
CC ECO:0000269|PubMed:25471886, ECO:0000269|PubMed:31435011,
CC ECO:0000269|PubMed:38228630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:31435011};
CC -!- SUBUNIT: Forms the Piezo channel composed of a homotrimer
CC (PubMed:31435011). Heterotrimeric interaction may occur between PIEZO1
CC and PIEZO2 (PubMed:38228630). Interacts with STOML3. Interacts with
CC TMC7; the interaction inhibits PIEZO2-conducted mechanically activated
CC currents (PubMed:38568807). Interacts with TMC1; the interaction may be
CC part of the MET complex (PubMed:38228630).
CC {ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:24662763,
CC ECO:0000269|PubMed:31435011, ECO:0000269|PubMed:38228630,
CC ECO:0000269|PubMed:38568807}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:38228630,
CC ECO:0000305|PubMed:25471886}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:31435011, ECO:0007744|PDB:6KG7}. Note=Located at
CC the tips and sides of stereocilia and cuticular plate membranes.
CC {ECO:0000269|PubMed:38228630}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CD54-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CD54-2; Sequence=VSP_040473, VSP_040474;
CC Name=3;
CC IsoId=Q8CD54-3; Sequence=VSP_040631, VSP_040632;
CC -!- TISSUE SPECIFICITY: Expressed in bladder, colon, and lung, but less
CC abundant in kidney or skin (PubMed:20813920). Strong expression is
CC observed in dorsal root ganglia (DRG) sensory neurons (PubMed:20813920,
CC PubMed:38568807). Expressed in a wide range of cutaneous low-threshold
CC mechanoreceptors (LTMRs), including Merkel cells and Meissner's
CC corpuscles (PubMed:24717433, PubMed:25471886). Expressed in sensory
CC neurons (PubMed:24662763). Expressed in cochlear inner and outer hair
CC cells and vestibular organ hair cells (PubMed:38228630).
CC {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:24662763,
CC ECO:0000269|PubMed:24717433, ECO:0000269|PubMed:25471886,
CC ECO:0000269|PubMed:38228630, ECO:0000269|PubMed:38568807}.
CC -!- DISRUPTION PHENOTYPE: Perinatal lethality. Conditional knockout in
CC sensory neurons and Merkel cells causes severe defects in light-touch
CC sensation, although detection of pain (nociception) is unaffected.
CC Conditional knockout in inner ear hair cells show no auditory and
CC vestibular defects (PubMed:38228630). {ECO:0000269|PubMed:25471886,
CC ECO:0000269|PubMed:38228630}.
CC -!- MISCELLANEOUS: Piezo comes from the Greek 'piesi' meaning pressure.
CC {ECO:0000305|PubMed:20813920}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PIEZO (TC 1.A.75) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31242.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27312.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; HQ215521; ADN28065.1; -; mRNA.
DR EMBL; AK018503; BAB31242.1; ALT_INIT; mRNA.
DR EMBL; AK031235; BAC27312.1; ALT_INIT; mRNA.
DR EMBL; AK031422; BAC27396.1; ALT_INIT; mRNA.
DR RefSeq; NP_001034574.4; NM_001039485.4.
DR PDB; 6KG7; EM; 3.80 A; A/B/C=1-2822.
DR PDBsum; 6KG7; -.
DR EMDB; EMD-9975; -.
DR SMR; Q8CD54; -.
DR IntAct; Q8CD54; 1.
DR STRING; 10090.ENSMUSP00000040019; -.
DR GlyCosmos; Q8CD54; 4 sites, No reported glycans.
DR GlyGen; Q8CD54; 4 sites.
DR iPTMnet; Q8CD54; -.
DR PhosphoSitePlus; Q8CD54; -.
DR PaxDb; 10090-ENSMUSP00000040019; -.
DR ProteomicsDB; 289495; -. [Q8CD54-1]
DR ProteomicsDB; 289496; -. [Q8CD54-2]
DR ProteomicsDB; 289497; -. [Q8CD54-3]
DR Antibodypedia; 2900; 212 antibodies from 20 providers.
DR Ensembl; ENSMUST00000182166.9; ENSMUSP00000138754.3; ENSMUSG00000041482.18. [Q8CD54-3]
DR GeneID; 667742; -.
DR KEGG; mmu:667742; -.
DR UCSC; uc008fdw.1; mouse. [Q8CD54-3]
DR AGR; MGI:1918781; -.
DR CTD; 63895; -.
DR MGI; MGI:1918781; Piezo2.
DR VEuPathDB; HostDB:ENSMUSG00000041482; -.
DR eggNOG; KOG1893; Eukaryota.
DR GeneTree; ENSGT00940000154456; -.
DR HOGENOM; CLU_021835_2_0_1; -.
DR InParanoid; Q8CD54; -.
DR OrthoDB; 5491808at2759; -.
DR PhylomeDB; Q8CD54; -.
DR BioGRID-ORCS; 667742; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Piezo2; mouse.
DR PRO; PR:Q8CD54; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8CD54; protein.
DR Bgee; ENSMUSG00000041482; Expressed in lumbar dorsal root ganglion and 130 other cell types or tissues.
DR ExpressionAtlas; Q8CD54; baseline and differential.
DR GO; GO:0032437; C:cuticular plate; IDA:UniProtKB.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:MGI.
DR GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
DR GO; GO:0140135; F:mechanosensitive monoatomic cation channel activity; IDA:MGI.
DR GO; GO:0008381; F:mechanosensitive monoatomic ion channel activity; IDA:UniProtKB.
DR GO; GO:0005261; F:monoatomic cation channel activity; IDA:MGI.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:UniProtKB.
DR GO; GO:0006812; P:monoatomic cation transport; IDA:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0009612; P:response to mechanical stimulus; IDA:UniProtKB.
DR InterPro; IPR027272; Piezo.
DR InterPro; IPR031805; Piezo_dom.
DR InterPro; IPR031334; Piezo_RRas-bd_dom.
DR PANTHER; PTHR47049:SF5; PIEZO-TYPE MECHANOSENSITIVE ION CHANNEL COMPONENT; 1.
DR PANTHER; PTHR47049; PIEZO-TYPE MECHANOSENSITIVE ION CHANNEL HOMOLOG; 1.
DR Pfam; PF15917; PIEZO; 1.
DR Pfam; PF12166; Piezo_RRas_bdg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..2822
FT /note="Piezo-type mechanosensitive ion channel component 2"
FT /id="PRO_0000186819"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31435011"
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 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..806
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 975..995
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1151..1171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1187..1207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1234..1254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1308..1328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1332..1352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1371..1391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1422..1442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1443..1978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31435011"
FT TRANSMEM 1979..2001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2008..2028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2037..2057
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2261..2281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2302..2322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2330..2350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2360..2380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2397..2414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2428..2448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2476..2496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2497..2731
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:31435011"
FT TRANSMEM 2732..2752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2753..2822
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31435011"
FT REGION 450..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2120..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2164..2205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 455..482
FT /evidence="ECO:0000255"
FT COILED 1475..1515
FT /evidence="ECO:0000255"
FT COMPBIAS 454..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..652
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..918
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2166..2205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1031..1209
FT /evidence="ECO:0000269|PubMed:31435011,
FT ECO:0007744|PDB:6KG7"
FT VAR_SEQ 629..644
FT /note="DEELQDVQVEGEPTEK -> MLFPMKDNTKCQRNFL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040631"
FT VAR_SEQ 645..2822
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040632"
FT VAR_SEQ 2457..2504
FT /note="RYPQPRGQKKKKAVKYGMGGMIIVLLICIVWFPLLFMSLIKSVAGVIN ->
FT VKSRWKCLCHACRPRAQVCYKINMDTAWLVARWMEAGDTTCREPEIQH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040473"
FT VAR_SEQ 2505..2822
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040474"
FT MUTAGEN 2757
FT /note="E->A: Reduces to around 50% the permeability of
FT Ca(2+)."
FT /evidence="ECO:0000269|PubMed:31435011"
FT MUTAGEN 2767..2770
FT /note="MFEE->AAAA: Hearing and vestibular impairment in
FT conditional knockin mice in inner ear hair cells."
FT /evidence="ECO:0000269|PubMed:38228630"
FT CONFLICT 2810
FT /note="P -> Q (in Ref. 2; BAC27396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2822 AA; 325628 MW; D786FBB41F48BA79 CRC64;
MASEVVCGLI FRLLLPICLA VACAFRYNGL SFVYLIYLLL IPLFSEPTKA TMQGHTGRLL
QSLCITSLSF LLLHIIFHIT LASLEAQHRI TPAYNCSTWE KTFRQIGFES LKGADAGNGI
RVFVPDIGMF IASLTIWLVC RTIVKKPDTE EIAQLNSECE NEELAGGEKM DSEEALIYEE
DLDGEEGMEG ELEESTKLKI LRRFASVASK LKEFIGNMIT TAGKVVVTIL LGSSGMMLPS
LTSAVYFFVF LGLCTWWSWC RTFDPLLFGC LCVLLAIFTA GHLIGLYLYQ FQFFQEAVPP
NDYYARLFGI KSVIQTDCAS TWKIIVNPDL SWYHHANPIL LLVMYYTLAT LIRIWLQEPL
VQEEMAKEDE GALDCSSNQN TAERRRSLWY ATQYPTDERK LLSMTQDDYK PSDGLLVTVN
GNPVDYHTIH PSLPIENGPA KTDLYTTPQY RWEPSEESSE KKEEEEDKRE DSEGEGSQEE
KRSVRMHAMV AVFQFIMKQS YICALIAMMA WSITYHSWLT FVLLIWSCTL WMIRNRRKYA
MISSPFMVVY ANLLLVLQYI WSFELPEIKK VPGFLEKKEP GELASKILFT ITFWLLLRQH
LTEQKALREK EALLSEVKIG SQELEEKEDE ELQDVQVEGE PTEKEEEEEE EIKEERHEVK
KEEEEEVEED DDQDIMKVLG NLVVALFIKY WIYVCGGMFF FVSFEGKIVM YKIIYMVLFL
FCVALYQVHY EWWRKILKYF WMSVVIYTML VLIFIYTYQF ENFPGLWQNM TGLKKEKLED
LGLKQFTVAE LFTRIFIPTS FLLVCILHLH YFHDRFLELT DLKSIPSKED NTIYSHAKVN
GRVYLIINRL AHPEGSLPDL AIMNMTASLD KPEVQKLAES GEERPEECVK KTEKGEAGKD
SDESEEEEDE EEESEEEESS DLRNKWHLVI DRLTVLFLKF LEYFHKLQVF MWWILELHII
KIVSSYIIWV TVKEVSLFNY VFLISWAFAL PYAKLRRAAS SVCTVWTCVI IVCKMLYQLQ
TIKPENFSVN CSLPNENQTN IPLHELNKSL LYSAPVDPTE WVGLRKSSPL LVYLRNNLLM
LAILAFEVTV YRHQEYYRGR NNLTAPVSKT IFHDITRLHL DDGLINCAKY FVNYFFYKFG
LETCFLMSVN VIGQRMDFYA MIHACWLIGV LYRRRRKAIA EVWPKYCCFL ACIITFQYFV
CIGIPPAPCR DYPWRFKGAY FNDNIIKWLY FPDFIVRPNP VFLVYDFMLL LCASLQRQIF
EDENKAAVRI MAGDNVEICM NLDAASFSQH NPVPDFIHCR SYLDMSKVII FSYLFWFVLT
IIFITGTTRI SIFCMGYLVA CFYFLLFGGD LLLKPIKSIL RYWDWLIAYN VFVITMKNIL
SIGACGYIGA LVRNSCWLIQ AFSLACTVKG YQMPEDDSRC KLPSGEAGII WDSICFAFLL
LQRRVFMSYY FLHVVADIKA SQILASRGAE LFQATIVKAV KARIEEEKKS MDQLKRQMDR
IKARQQKYKK GKERMLSLTQ ESGEGQDIQK VSEEDDEREA DKQKAKGKKK QWWRPWVDHA
SMVRSGDYYL FETDSEEEEE EELKKEDEEP PRKSAFQFVY QAWITDPKTA LRQRRKEKKK
LAREEQKERR KGSGDGPVEW EDREDEPVKK KSDGPDNIIK RIFNILKFTW VLFLATVDSF
TTWLNSISRE HIDISTVLRI ERCMLTREIK KGNVPTRESI HMYYQNHIMN LSRESGLDTI
DEHSGAGSRA QAAHRMDSLD SRDSISSCYT EATLLISRQS TLDDLDGQDP VPKTSERARP
RLRKMFSLDM SSSSADSGSV ASSEPTQCTM LYSRQGTTET IEEVEAEAEE EVVEGLEPEL
HDAEEKEYAA EYEAGVEEIS LTPDEELPQF STDDCEAPPS YSKAVSFEHL SFASQDDSGA
KNHMVVSPDD SRTDKLESSI LPPLTHELTA SDLLMSKMFH DDELEESEKF YVDQPRFLLL
FYAMYNTLVA RSEMVCYFVI ILNHMTSASI ITLLLPILIF LWAMLSVPRP SRRFWMMAIV
YTEVAIVVKY FFQFGFFPWN KDLEIYKERP YFPPNIIGVE KKEGYVLYDL IQLLALFFHR
SILKCHGLWD EDDIVDSNTD KEGSDDELSL DQGRRGSSDS LKSINLAASV ESVHVTFPEQ
PAAIRRKRSC SSSQISPRSS FSSNRSKRGS TSTRNSSQKG SSVLSLKQKS KRELYMEKLQ
EHLIKAKAFT IKKTLQIYVP IRQFFYDLIH PDYSAVTDVY VLMFLADTVD FIIIVFGFWA
FGKHSAAADI TSSLSEDQVP GPFLVMVLIQ FGTMVVDRAL YLRKTVLGKV IFQVILVFGI
HFWMFFILPG VTERKFSQNL VAQLWYFVKC VYFGLSAYQI RCGYPTRVLG NFLTKSYNYV
NLFLFQGFRL VPFLTELRAV MDWVWTDTTL SLSSWICVED IYAHIFILKC WRESEKRYPQ
PRGQKKKKAV KYGMGGMIIV LLICIVWFPL LFMSLIKSVA GVINQPLDVS VTITLGGYQP
IFTMSAQQSQ LKVMDNSKYN EFLKSFGPNS GAMQFLENYE REDVTVAELE GNSNSLWTIS
PPSKQKMIQE LTDPNSCFSV VFSWSIQRNM TLGAKAEIAT DKLSFPLAVA TRNSIAKMIA
GNDTESSNTP VTIEKIYPYY VKAPSDSNSK PIKQLLSENN FMNITIILFR DNVTKSNSEW
WVLNLTGSRI FNQGSQALEL VVFNDKVSPP SLGFLAGYGI MGLYASVVLV IGKFVREFFS
GISHSIMFEE LPNVDRILKL CTDIFLVRET GELELEEDLY AKLIFLYRSP ETMIKWTREK
TN
//
