P2RX2_HUMAN
ID P2RX2_HUMAN Reviewed; 471 AA.
AC Q9UBL9; A6NGB4; A6NH93; A6NHC2; A6NHU3; A6NIG9; Q6V9R6; Q9NR37; Q9NR38;
AC Q9UHD5; Q9UHD6; Q9UHD7; Q9Y637; Q9Y638;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=P2X purinoceptor 2;
DE Short=P2X2;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RX2; Synonyms=P2X2;
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 [GENOMIC DNA / MRNA] (ISOFORMS A; B; C AND D).
RC TISSUE=Pituitary;
RX PubMed=10570044; DOI=10.1124/mol.56.6.1171;
RA Lynch K.J., Touma E., Niforatos W., Kage K.L., Burgard E.C., van Biesen T.,
RA Kowaluk E.A., Jarvis M.F.;
RT "Molecular and functional characterization of human P2X(2) receptors.";
RL Mol. Pharmacol. 56:1171-1181(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC TISSUE=Placenta;
RA McMahon R.A., Egan T.M., Hurley P.T., Nelson A., Rogers M., Martin F.;
RT "Cloning of the human P2X2 receptor cDNA and multiple splice variants.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; H AND I).
RC TISSUE=Prostate;
RA Chang T.K., Kosaka A.H., Oglesby I.B., Gever J.R., Lachnit W.G.,
RA Ford A.P.D.W., Chang D.J.;
RT "Cloning and molecular characterization of human P2X2 and its splice
RT variants.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM K).
RA Lin L., Zheng G., Yu R., Li H., Shen C., Zhou G., Zhong G., Li M., Xiao W.,
RA Ke R., Yang S.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP VARIANT DFNA41 LEU-60, CHARACTERIZATION OF VARIANT DFNA41 LEU-60, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=23345450; DOI=10.1073/pnas.1222285110;
RA Yan D., Zhu Y., Walsh T., Xie D., Yuan H., Sirmaci A., Fujikawa T.,
RA Wong A.C., Loh T.L., Du L., Grati M., Vlajkovic S.M., Blanton S.,
RA Ryan A.F., Chen Z.Y., Thorne P.R., Kachar B., Tekin M., Zhao H.B.,
RA Housley G.D., King M.C., Liu X.Z.;
RT "Mutation of the ATP-gated P2X(2) receptor leads to progressive hearing
RT loss and increased susceptibility to noise.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2228-2233(2013).
RN [7]
RP VARIANT DFNA41 ARG-353.
RX PubMed=24211385; DOI=10.1016/j.gene.2013.10.052;
RA Faletra F., Girotto G., D'Adamo A.P., Vozzi D., Morgan A., Gasparini P.;
RT "A novel P2RX2 mutation in an Italian family affected by autosomal dominant
RT nonsyndromic hearing loss.";
RL Gene 534:236-239(2014).
CC -!- FUNCTION: Ion channel gated by extracellular ATP involved in a variety
CC of cellular responses, such as excitatory postsynaptic responses in
CC sensory neurons, neuromuscular junctions (NMJ) formation, hearing,
CC perception of taste and peristalsis. In the inner ear, regulates sound
CC transduction and auditory neurotransmission, outer hair cell
CC electromotility, inner ear gap junctions, and K(+) recycling. Mediates
CC synaptic transmission between neurons and from neurons to smooth
CC muscle. {ECO:0000269|PubMed:23345450}.
CC -!- SUBUNIT: Homotrimer and heterotrimer; functional P2XRs are organized as
CC homomeric and heteromeric trimers.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23345450};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23345450}.
CC Note=Localizes to the apical membranes of hair cells in the organ of
CC Corti.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=A;
CC IsoId=Q9UBL9-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9UBL9-2; Sequence=VSP_004499;
CC Name=C;
CC IsoId=Q9UBL9-3; Sequence=VSP_004497;
CC Name=D;
CC IsoId=Q9UBL9-4; Sequence=VSP_004498;
CC Name=H;
CC IsoId=Q9UBL9-5; Sequence=VSP_004495;
CC Name=I;
CC IsoId=Q9UBL9-6; Sequence=VSP_004496;
CC Name=K;
CC IsoId=Q9UBL9-7; Sequence=VSP_004497, VSP_014135, VSP_004499;
CC -!- DISEASE: Deafness, autosomal dominant, 41 (DFNA41) [MIM:608224]: A form
CC of non-syndromic deafness characterized by onset of progressive
CC sensorineural hearing loss usually in the second decade. The hearing
CC loss is severe and ultimately affects all frequencies. Exposure to
CC noise exacerbates the hearing loss, particularly at high frequencies.
CC {ECO:0000269|PubMed:23345450, ECO:0000269|PubMed:24211385}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=P2X receptor entry;
CC URL="https://en.wikipedia.org/wiki/P2X_receptor";
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DR EMBL; AF190822; AAF19170.1; -; mRNA.
DR EMBL; AF190823; AAF19171.1; -; mRNA.
DR EMBL; AF190824; AAF19172.1; -; mRNA.
DR EMBL; AF190825; AAF19173.1; -; mRNA.
DR EMBL; AF190826; AAF19174.1; -; Genomic_DNA.
DR EMBL; AF109387; AAD42947.1; -; mRNA.
DR EMBL; AF109388; AAD42948.1; -; mRNA.
DR EMBL; AF260426; AAF74201.1; -; mRNA.
DR EMBL; AF260427; AAF74202.1; -; mRNA.
DR EMBL; AF260428; AAF74203.1; -; mRNA.
DR EMBL; AF260429; AAF74204.1; -; mRNA.
DR EMBL; AY346374; AAQ54329.1; -; mRNA.
DR EMBL; AC131212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS31930.1; -. [Q9UBL9-4]
DR CCDS; CCDS31931.1; -. [Q9UBL9-1]
DR CCDS; CCDS31932.1; -. [Q9UBL9-2]
DR CCDS; CCDS31933.1; -. [Q9UBL9-3]
DR CCDS; CCDS31934.1; -. [Q9UBL9-6]
DR CCDS; CCDS31935.1; -. [Q9UBL9-5]
DR CCDS; CCDS61286.1; -. [Q9UBL9-7]
DR RefSeq; NP_001269093.1; NM_001282164.1. [Q9UBL9-7]
DR RefSeq; NP_001269094.1; NM_001282165.1.
DR RefSeq; NP_036358.2; NM_012226.4. [Q9UBL9-6]
DR RefSeq; NP_057402.1; NM_016318.3. [Q9UBL9-3]
DR RefSeq; NP_733782.1; NM_170682.3. [Q9UBL9-1]
DR RefSeq; NP_733783.1; NM_170683.3. [Q9UBL9-4]
DR RefSeq; NP_777361.1; NM_174872.2. [Q9UBL9-5]
DR RefSeq; NP_777362.1; NM_174873.2. [Q9UBL9-2]
DR AlphaFoldDB; Q9UBL9; -.
DR SMR; Q9UBL9; -.
DR BioGRID; 116607; 78.
DR IntAct; Q9UBL9; 21.
DR STRING; 9606.ENSP00000343339; -.
DR BindingDB; Q9UBL9; -.
DR ChEMBL; CHEMBL2531; -.
DR DrugBank; DB01069; Promethazine.
DR GuidetoPHARMACOLOGY; 479; -.
DR GlyGen; Q9UBL9; 3 sites.
DR iPTMnet; Q9UBL9; -.
DR PhosphoSitePlus; Q9UBL9; -.
DR BioMuta; P2RX2; -.
DR DMDM; 12643353; -.
DR MassIVE; Q9UBL9; -.
DR MaxQB; Q9UBL9; -.
DR PeptideAtlas; Q9UBL9; -.
DR PRIDE; Q9UBL9; -.
DR ProteomicsDB; 83999; -. [Q9UBL9-1]
DR ProteomicsDB; 84000; -. [Q9UBL9-2]
DR ProteomicsDB; 84001; -. [Q9UBL9-3]
DR ProteomicsDB; 84002; -. [Q9UBL9-4]
DR ProteomicsDB; 84003; -. [Q9UBL9-5]
DR ProteomicsDB; 84004; -. [Q9UBL9-6]
DR ProteomicsDB; 84005; -. [Q9UBL9-7]
DR Antibodypedia; 2714; 336 antibodies from 32 providers.
DR DNASU; 22953; -.
DR Ensembl; ENST00000343948.8; ENSP00000343339.4; ENSG00000187848.15. [Q9UBL9-4]
DR Ensembl; ENST00000348800.9; ENSP00000345095.5; ENSG00000187848.15. [Q9UBL9-2]
DR Ensembl; ENST00000350048.9; ENSP00000343904.5; ENSG00000187848.15. [Q9UBL9-3]
DR Ensembl; ENST00000351222.8; ENSP00000344502.4; ENSG00000187848.15. [Q9UBL9-5]
DR Ensembl; ENST00000352418.8; ENSP00000341419.4; ENSG00000187848.15. [Q9UBL9-6]
DR Ensembl; ENST00000449132.6; ENSP00000405531.2; ENSG00000187848.15. [Q9UBL9-7]
DR Ensembl; ENST00000643471.2; ENSP00000494644.1; ENSG00000187848.15. [Q9UBL9-1]
DR GeneID; 22953; -.
DR KEGG; hsa:22953; -.
DR MANE-Select; ENST00000643471.2; ENSP00000494644.1; NM_170682.4; NP_733782.1.
DR UCSC; uc001uki.3; human. [Q9UBL9-1]
DR CTD; 22953; -.
DR DisGeNET; 22953; -.
DR GeneCards; P2RX2; -.
DR HGNC; HGNC:15459; P2RX2.
DR HPA; ENSG00000187848; Tissue enhanced (brain, epididymis, prostate).
DR MalaCards; P2RX2; -.
DR MIM; 600844; gene.
DR MIM; 608224; phenotype.
DR neXtProt; NX_Q9UBL9; -.
DR OpenTargets; ENSG00000187848; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA32862; -.
DR VEuPathDB; HostDB:ENSG00000187848; -.
DR eggNOG; ENOG502QVP9; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_4_0_1; -.
DR InParanoid; Q9UBL9; -.
DR OMA; SHCKPTY; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; Q9UBL9; -.
DR TreeFam; TF328633; -.
DR PathwayCommons; Q9UBL9; -.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-418346; Platelet homeostasis.
DR SignaLink; Q9UBL9; -.
DR BioGRID-ORCS; 22953; 20 hits in 1068 CRISPR screens.
DR GeneWiki; P2RX2; -.
DR GenomeRNAi; 22953; -.
DR Pharos; Q9UBL9; Tchem.
DR PRO; PR:Q9UBL9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UBL9; protein.
DR Bgee; ENSG00000187848; Expressed in mucosa of stomach and 99 other tissues.
DR ExpressionAtlas; Q9UBL9; baseline and differential.
DR Genevisible; Q9UBL9; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0043235; C:receptor complex; IDA:ARUK-UCL.
DR GO; GO:0005524; F:ATP binding; NAS:BHF-UCL.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0015276; F:ligand-gated ion channel activity; TAS:ProtInc.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; NAS:BHF-UCL.
DR GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl.
DR GO; GO:0003029; P:detection of hypoxic conditions in blood by carotid body chemoreceptor signaling; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR GO; GO:0030432; P:peristalsis; IEA:Ensembl.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; NAS:BHF-UCL.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; NAS:BHF-UCL.
DR GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; ISS:ARUK-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003045; P2X2_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01309; P2X2RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Deafness; Disease variant;
KW Disulfide bond; Glycoprotein; Hearing; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Non-syndromic deafness; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..471
FT /note="P2X purinoceptor 2"
FT /id="PRO_0000161549"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 320..333
FT /note="Pore-forming motif"
FT /evidence="ECO:0000255"
FT REGION 400..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..439
FT /evidence="ECO:0000250"
FT DISULFID 125..176
FT /evidence="ECO:0000250"
FT DISULFID 136..159
FT /evidence="ECO:0000250"
FT DISULFID 142..170
FT /evidence="ECO:0000250"
FT DISULFID 226..236
FT /evidence="ECO:0000250"
FT DISULFID 270..279
FT /evidence="ECO:0000250"
FT VAR_SEQ 36..127
FT /note="Missing (in isoform H)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_004495"
FT VAR_SEQ 38..152
FT /note="NRRLGVLYRAVQLLILLYFVWYVFIVQKSYQESETGPESSIITKVKGITTSE
FT HKVWDVEEYVKPPEGGSVFSIITRVEATHSQTQGTCPESIRVHNATCLSDADCVAGELD
FT MLGN -> IHRAEKLPGERDGPRELHHHQGQGDHHVRAQSVGRGGVREAPR (in
FT isoform I)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_004496"
FT VAR_SEQ 104..127
FT /note="Missing (in isoform C and isoform K)"
FT /evidence="ECO:0000303|PubMed:10570044, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.4"
FT /id="VSP_004497"
FT VAR_SEQ 154..258
FT /note="LRTGRCVPYYQGPSKTCEVFGWCPVEDGASVSQFLGTMAPNFTILIKNSIHY
FT PKFHFSKGNIADRTDGYLKRCTFHEASDLYCPIFKLGFIVEKAGESFTELAHK -> AL
FT QDLRGVRLVPGGRWGLCQPISGYDGPKFHHPHQEQHPLPQIPLLQGQHRRPHRRVPEAL
FT HVPRGLRPLLPHLQAGLYRGEGWGELHRARTQGR (in isoform K)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_014135"
FT VAR_SEQ 354
FT /note="V -> VVRNPLWGPSGCGGSTRPLHTGLCWPQ (in isoform D)"
FT /evidence="ECO:0000303|PubMed:10570044"
FT /id="VSP_004498"
FT VAR_SEQ 381..447
FT /note="Missing (in isoform B and isoform K)"
FT /evidence="ECO:0000303|PubMed:10570044, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.4"
FT /id="VSP_004499"
FT VARIANT 60
FT /note="V -> L (in DFNA41; found in heterozygous status in
FT patients; abolished ATP-stimulated permeability;
FT dbSNP:rs587777692)"
FT /evidence="ECO:0000269|PubMed:23345450"
FT /id="VAR_070687"
FT VARIANT 353
FT /note="G -> R (in DFNA41; dbSNP:rs202138002)"
FT /evidence="ECO:0000269|PubMed:24211385"
FT /id="VAR_070688"
FT CONFLICT 1..14
FT /note="MAAAQPKYPAGATA -> MV (in Ref. 3; AAD42947/AAD42948)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="V -> A (in Ref. 4; AAQ54329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 51754 MW; 84CD61DA136EF420 CRC64;
MAAAQPKYPA GATARRLARG CWSALWDYET PKVIVVRNRR LGVLYRAVQL LILLYFVWYV
FIVQKSYQES ETGPESSIIT KVKGITTSEH KVWDVEEYVK PPEGGSVFSI ITRVEATHSQ
TQGTCPESIR VHNATCLSDA DCVAGELDML GNGLRTGRCV PYYQGPSKTC EVFGWCPVED
GASVSQFLGT MAPNFTILIK NSIHYPKFHF SKGNIADRTD GYLKRCTFHE ASDLYCPIFK
LGFIVEKAGE SFTELAHKGG VIGVIINWDC DLDLPASECN PKYSFRRLDP KHVPASSGYN
FRFAKYYKIN GTTTRTLIKA YGIRIDVIVH GQAGKFSLIP TIINLATALT SVGVGSFLCD
WILLTFMNKN KVYSHKKFDK VCTPSHPSGS WPVTLARVLG QAPPEPGHRS EDQHPSPPSG
QEGQQGAECG PAFPPLRPCP ISAPSEQMVD TPASEPAQAS TPTDPKGLAQ L
