ID PCD15_HUMAN Reviewed; 1955 AA. AC Q96QU1; A6NL19; C6ZEF5; C6ZEF6; C6ZEF7; Q5VY38; Q5VY39; Q6TRH8; AC Q8NDB9; Q96QT8; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 11-DEC-2013, entry version 116. DE RecName: Full=Protocadherin-15; DE Flags: Precursor; GN Name=PCDH15; Synonyms=USH1F; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, RP INVOLVEMENT IN USHER SYNDROME TYPE 1F, AND VARIANT GLN-929. RC TISSUE=Fetal brain; RX PubMed=11487575; DOI=10.1093/hmg/10.16.1709; RA Alagramam K.N., Yuan H., Kuehn M.H., Murcia C.L., Wayne S., RA Srisailpathy C.R.S., Lowry R.B., Knaus R., Van Laer L., Bernier F.P., RA Schwartz S., Lee C., Morton C.C., Mullins R.F., Ramesh A., RA Van Camp G., Hagemen G.S., Woychik R.P., Smith R.J.H.; RT "Mutations in the novel protocadherin PCDH15 cause Usher syndrome type RT 1F."; RL Hum. Mol. Genet. 10:1709-1718(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN USHER RP SYNDROME TYPE 1F. RX PubMed=11398101; DOI=10.1086/321277; RA Ahmed Z.M., Riazuddin S., Bernstein S.L., Ahmed Z., Khan S., RA Griffith A.J., Morell R.J., Friedman T.B., Riazuddin S., Wilcox E.R.; RT "Mutations of the protocadherin gene PCDH15 cause Usher syndrome type RT 1F."; RL Am. J. Hum. Genet. 69:25-34(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS DFNB23 GLY-134 RP AND ASP-262. RX PubMed=14570705; DOI=10.1093/hmg/ddg358; RA Ahmed Z.M., Riazuddin S., Ahmad J., Bernstein S.L., Guo Y., RA Sabar M.F., Sieving P., Riazuddin S., Griffith A.J., Friedman T.B., RA Belyantseva I.A., Wilcox E.R.; RT "PCDH15 is expressed in the neurosensory epithelium of the eye and ear RT and mutant alleles are responsible for both USH1F and DFNB23."; RL Hum. Mol. Genet. 12:3215-3223(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6), TISSUE SPECIFICITY, RP VARIANT DFNB23 GLY-134, AND VARIANT USH1DF GLY-178. RC TISSUE=Retina; RX PubMed=18719945; DOI=10.1007/s00439-008-0543-3; RA Ahmed Z.M., Riazuddin S., Aye S., Ali R.A., Venselaar H., Anwar S., RA Belyantseva P.P., Qasim M., Riazuddin S., Friedman T.B.; RT "Gene structure and mutant alleles of PCDH15: nonsyndromic deafness RT DFNB23 and type 1 Usher syndrome."; RL Hum. Genet. 124:215-223(2008). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS RP ALA-435 AND GLN-929. RC TISSUE=Lymph node; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [7] RP IDENTIFICATION OF ISOFORMS 1 AND 3, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND VARIANT ALA-19. RX PubMed=16369489; DOI=10.1038/sj.onc.1209301; RA Rouget-Quermalet V., Giustiniani J., Marie-Cardine A., Beaud G., RA Besnard F., Loyaux D., Ferrara P., Leroy K., Shimizu N., Gaulard P., RA Bensussan A., Schmitt C.; RT "Protocadherin 15 (PCDH15): a new secreted isoform and a potential RT marker for NK/T cell lymphomas."; RL Oncogene 25:2807-2811(2006). RN [8] RP VARIANTS USH1F LYS-1342 AND THR-1867 DEL. RX PubMed=15660226; DOI=10.1007/s00439-004-1227-2; RA Ouyang X.M., Yan D., Du L.L., Hejtmancik J.F., Jacobson S.G., RA Nance W.E., Li A.R., Angeli S., Kaiser M., Newton V., Brown S.D.M., RA Balkany T., Liu X.Z.; RT "Characterization of Usher syndrome type I gene mutations in an Usher RT syndrome patient population."; RL Hum. Genet. 116:292-299(2005). RN [9] RP INVOLVEMENT IN USH1DF. RX PubMed=15537665; DOI=10.1093/hmg/ddi010; RA Zheng Q.Y., Yan D., Ouyang X.M., Du L.L., Yu H., Chang B., RA Johnson K.R., Liu X.Z.; RT "Digenic inheritance of deafness caused by mutations in genes encoding RT cadherin 23 and protocadherin 15 in mice and humans."; RL Hum. Mol. Genet. 14:103-111(2005). CC -!- FUNCTION: Calcium-dependent cell-adhesion protein. Essential for CC maintenance of normal retinal and cochlear function. CC -!- SUBUNIT: Interacts with MYO7A. antiparallel heterodimer with CDH23 CC (By similarity). Interacts with USH1G; this interaction may CC recruit USH1G to the plasma membrane (By similarity). Interacts CC with LHFPL5/TMHS; this interaction is required for efficient CC localization to hair bundles (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein (By similarity). Note=Efficient localization to the plasma CC membrane requires the presence of LHFPL5 (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=A, CD1-1; CC IsoId=Q96QU1-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=Q96QU1-2; Sequence=VSP_028257, VSP_028258; CC Name=3; Synonyms=C; CC IsoId=Q96QU1-3; Sequence=VSP_028259, VSP_028260; CC Note=Ref.5 (CAD38850) sequence differs from that shown at CC position 957 due to erroneous termination; CC Name=4; Synonyms=CD2-1; CC IsoId=Q96QU1-4; Sequence=VSP_046616, VSP_046617, VSP_046622; CC Name=5; Synonyms=CD2-2; CC IsoId=Q96QU1-5; Sequence=VSP_046619, VSP_046620; CC Name=6; Synonyms=CD3-1; CC IsoId=Q96QU1-6; Sequence=VSP_046618, VSP_046621; CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, kidney, spleen and CC testis. Found also in the inner and outer synaptic layers, and the CC nerve fiber layer in adult and fetal retinas. Found in the CC supporting cells, outer sulcus cells and spiral ganglion of fetal CC cochlea. Expressed in cytotoxic tumor-derived T- and NK-cell lines CC as well as biopsies of nasal NK/T-cell lymphomas. Not detected in CC normal or in vitro activated peripheral blood cells, CD4 or CD8 CC lymphocytes or NK cells. Isoform 3 is expressed in brain, heart, CC cerebellum and kidney. CD1 isoforms, such as isoform 1, have a CC limited pattern of expression and is detected in testis, retina CC and cochlea. CD2 isoforms, such as isoforms 4 and 5, are expressed CC in heart, kidney, thymus, spleen, testis, retina and cochlea. CD3 CC isoforms, such as isoform 6, are widely expressed. CC -!- DOMAIN: Cadherin repeats 1 and 2 mediate calcium-dependent CC heterophilic interaction with CDH23 (By similarity). CC -!- DOMAIN: Three calcium ions are usually bound at the interface of CC each cadherin domain and rigidify the connections, imparting a CC strong curvature to the full-length ectodomain (By similarity). CC -!- DISEASE: Usher syndrome 1F (USH1F) [MIM:602083]: USH is a CC genetically heterogeneous condition characterized by the CC association of retinitis pigmentosa with sensorineural deafness. CC Age at onset and differences in auditory and vestibular function CC distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 CC (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by CC profound congenital sensorineural deafness, absent vestibular CC function and prepubertal onset of progressive retinitis pigmentosa CC leading to blindness. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- DISEASE: Usher syndrome 1D/F (USH1DF) [MIM:601067]: USH1DF CC patients are heterozygous for mutations in CDH23 and PCDH15, CC indicating a digenic inheritance pattern. Note=The disease is CC caused by mutations affecting distinct genetic loci, including the CC gene represented in this entry. CC -!- DISEASE: Deafness, autosomal recessive, 23 (DFNB23) [MIM:609533]: CC A form of non-syndromic sensorineural hearing loss. Sensorineural CC deafness results from damage to the neural receptors of the inner CC ear, the nerve pathways to the brain, or the area of the brain CC that receives sound information. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Contains 11 cadherin domains. CC -!- WEB RESOURCE: Name=GeneReviews; CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PCDH15"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY029205; AAK31581.1; -; mRNA. DR EMBL; AY029237; AAK31804.1; -; mRNA. DR EMBL; AY388963; AAR26468.1; -; mRNA. DR EMBL; EU718480; ACF76476.1; -; mRNA. DR EMBL; EU718481; ACF76477.1; -; mRNA. DR EMBL; EU718482; ACF76478.1; -; mRNA. DR EMBL; AL834134; CAD38850.2; ALT_TERM; mRNA. DR EMBL; AL353784; CAH72389.1; -; Genomic_DNA. DR EMBL; AC013737; CAH72389.1; JOINED; Genomic_DNA. DR EMBL; AC024073; CAH72389.1; JOINED; Genomic_DNA. DR EMBL; AC027671; CAH72389.1; JOINED; Genomic_DNA. DR EMBL; AL356114; CAH72389.1; JOINED; Genomic_DNA. DR EMBL; AL360214; CAH72389.1; JOINED; Genomic_DNA. DR EMBL; AL353784; CAH72390.1; -; Genomic_DNA. DR EMBL; AC013737; CAH72390.1; JOINED; Genomic_DNA. DR EMBL; AC016817; CAH72390.1; JOINED; Genomic_DNA. DR EMBL; AC024073; CAH72390.1; JOINED; Genomic_DNA. DR EMBL; AC027671; CAH72390.1; JOINED; Genomic_DNA. DR EMBL; AL356114; CAH72390.1; JOINED; Genomic_DNA. DR EMBL; AL360214; CAH72390.1; JOINED; Genomic_DNA. DR EMBL; AL365496; CAH72390.1; JOINED; Genomic_DNA. DR EMBL; AL356114; CAH71768.1; -; Genomic_DNA. DR EMBL; AC013737; CAH71768.1; JOINED; Genomic_DNA. DR EMBL; AC024073; CAH71768.1; JOINED; Genomic_DNA. DR EMBL; AC027671; CAH71768.1; JOINED; Genomic_DNA. DR EMBL; AL353784; CAH71768.1; JOINED; Genomic_DNA. DR EMBL; AL360214; CAH71768.1; JOINED; Genomic_DNA. DR EMBL; AL356114; CAH71769.1; -; Genomic_DNA. DR EMBL; AC013737; CAH71769.1; JOINED; Genomic_DNA. DR EMBL; AC016817; CAH71769.1; JOINED; Genomic_DNA. DR EMBL; AC024073; CAH71769.1; JOINED; Genomic_DNA. DR EMBL; AC027671; CAH71769.1; JOINED; Genomic_DNA. DR EMBL; AL353784; CAH71769.1; JOINED; Genomic_DNA. DR EMBL; AL360214; CAH71769.1; JOINED; Genomic_DNA. DR EMBL; AL365496; CAH71769.1; JOINED; Genomic_DNA. DR EMBL; AL360214; CAI15200.1; -; Genomic_DNA. DR EMBL; AC013737; CAI15200.1; JOINED; Genomic_DNA. DR EMBL; AC024073; CAI15200.1; JOINED; Genomic_DNA. DR EMBL; AC027671; CAI15200.1; JOINED; Genomic_DNA. DR EMBL; AL353784; CAI15200.1; JOINED; Genomic_DNA. DR EMBL; AL356114; CAI15200.1; JOINED; Genomic_DNA. DR EMBL; AL360214; CAI15201.1; -; Genomic_DNA. DR EMBL; AC013737; CAI15201.1; JOINED; Genomic_DNA. DR EMBL; AC016817; CAI15201.1; JOINED; Genomic_DNA. DR EMBL; AC024073; CAI15201.1; JOINED; Genomic_DNA. DR EMBL; AC027671; CAI15201.1; JOINED; Genomic_DNA. DR EMBL; AL353784; CAI15201.1; JOINED; Genomic_DNA. DR EMBL; AL356114; CAI15201.1; JOINED; Genomic_DNA. DR EMBL; AL365496; CAI15201.1; JOINED; Genomic_DNA. DR EMBL; AL365496; CAH73916.1; -; Genomic_DNA. DR EMBL; AC013737; CAH73916.1; JOINED; Genomic_DNA. DR EMBL; AC016817; CAH73916.1; JOINED; Genomic_DNA. DR EMBL; AC024073; CAH73916.1; JOINED; Genomic_DNA. DR EMBL; AC027671; CAH73916.1; JOINED; Genomic_DNA. DR EMBL; AL353784; CAH73916.1; JOINED; Genomic_DNA. DR EMBL; AL356114; CAH73916.1; JOINED; Genomic_DNA. DR EMBL; AL360214; CAH73916.1; JOINED; Genomic_DNA. DR IPI; IPI00290035; -. DR IPI; IPI00513908; -. DR IPI; IPI00646069; -. DR RefSeq; NP_149045.3; NM_033056.3. DR RefSeq; XP_005270113.1; XM_005270056.1. DR RefSeq; XP_005270114.1; XM_005270057.1. DR UniGene; Hs.280209; -. DR ProteinModelPortal; Q96QU1; -. DR SMR; Q96QU1; 27-255. DR IntAct; Q96QU1; 1. DR MINT; MINT-2815151; -. DR STRING; 9606.ENSP00000354950; -. DR ChEMBL; CHEMBL6112; -. DR TCDB; 1.A.82.1.1; the hair cell mechanotransduction channel (hcmc) family. DR PhosphoSite; Q96QU1; -. DR DMDM; 116242702; -. DR PaxDb; Q96QU1; -. DR PRIDE; Q96QU1; -. DR Ensembl; ENST00000320301; ENSP00000322604; ENSG00000150275. DR Ensembl; ENST00000373955; ENSP00000363066; ENSG00000150275. DR GeneID; 65217; -. DR KEGG; hsa:65217; -. DR UCSC; uc010qht.2; human. DR CTD; 65217; -. DR GeneCards; GC10M055473; -. DR HGNC; HGNC:14674; PCDH15. DR MIM; 276900; phenotype. DR MIM; 601067; phenotype. DR MIM; 602083; phenotype. DR MIM; 605514; gene. DR MIM; 609533; phenotype. DR neXtProt; NX_Q96QU1; -. DR Orphanet; 90636; Autosomal recessive nonsyndromic sensorineural deafness type DFNB. DR Orphanet; 231169; Usher syndrome type 1. DR PharmGKB; PA32999; -. DR eggNOG; NOG253862; -. DR HOVERGEN; HBG053521; -. DR KO; K16500; -. DR GeneWiki; PCDH15; -. DR GenomeRNAi; 65217; -. DR NextBio; 35483369; -. DR PRO; PR:Q96QU1; -. DR ArrayExpress; Q96QU1; -. DR Bgee; Q96QU1; -. DR CleanEx; HS_PCDH15; -. DR Genevestigator; Q96QU1; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; IDA:HGNC. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:HGNC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032420; C:stereocilium; ISS:HGNC. DR GO; GO:0045202; C:synapse; IDA:HGNC. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0050957; P:equilibrioception; IMP:HGNC. DR GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro. DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:HGNC. DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:HGNC. DR GO; GO:0007605; P:sensory perception of sound; IMP:HGNC. DR Gene3D; 2.60.40.60; -; 10. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR015919; Cadherin-like. DR InterPro; IPR020894; Cadherin_CS. DR Pfam; PF00028; Cadherin; 9. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 11. DR SUPFAM; SSF49313; SSF49313; 10. DR PROSITE; PS00232; CADHERIN_1; 3. DR PROSITE; PS50268; CADHERIN_2; 10. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; KW Complete proteome; Deafness; Disease mutation; Disulfide bond; KW Glycoprotein; Hearing; Membrane; Non-syndromic deafness; Polymorphism; KW Reference proteome; Repeat; Retinitis pigmentosa; Secreted; Signal; KW Transmembrane; Transmembrane helix; Usher syndrome. FT SIGNAL 1 26 Potential. FT CHAIN 27 1955 Protocadherin-15. FT /FTId=PRO_0000003998. FT TOPO_DOM 27 1376 Extracellular (Potential). FT TRANSMEM 1377 1397 Helical; (Potential). FT TOPO_DOM 1398 1955 Cytoplasmic (Potential). FT DOMAIN 40 147 Cadherin 1. FT DOMAIN 148 265 Cadherin 2. FT DOMAIN 278 395 Cadherin 3. FT DOMAIN 396 509 Cadherin 4. FT DOMAIN 510 616 Cadherin 5. FT DOMAIN 617 717 Cadherin 6. FT DOMAIN 719 819 Cadherin 7. FT DOMAIN 820 926 Cadherin 8. FT DOMAIN 927 1035 Cadherin 9. FT DOMAIN 1037 1144 Cadherin 10. FT DOMAIN 1145 1259 Cadherin 11. FT COMPBIAS 1435 1443 Poly-Pro. FT COMPBIAS 1746 1752 Poly-Pro. FT COMPBIAS 1815 1823 Poly-Pro. FT COMPBIAS 1826 1831 Poly-Pro. FT CARBOHYD 52 52 N-linked (GlcNAc...) (Potential). FT CARBOHYD 97 97 N-linked (GlcNAc...) (Potential). FT CARBOHYD 201 201 N-linked (GlcNAc...) (Potential). FT CARBOHYD 419 419 N-linked (GlcNAc...) (Potential). FT CARBOHYD 559 559 N-linked (GlcNAc...) (Potential). FT CARBOHYD 662 662 N-linked (GlcNAc...) (Potential). FT CARBOHYD 724 724 N-linked (GlcNAc...) (Potential). FT CARBOHYD 768 768 N-linked (GlcNAc...) (Potential). FT CARBOHYD 821 821 N-linked (GlcNAc...) (Potential). FT CARBOHYD 851 851 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1064 1064 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1084 1084 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1175 1175 N-linked (GlcNAc...) (Potential). FT DISULFID 32 120 By similarity. FT VAR_SEQ 1 1118 Missing (in isoform 2). FT /FTId=VSP_028257. FT VAR_SEQ 435 435 D -> DVPPSGVP (in isoform 4). FT /FTId=VSP_046616. FT VAR_SEQ 957 961 GLPAS -> VSRRH (in isoform 3). FT /FTId=VSP_028259. FT VAR_SEQ 962 1955 Missing (in isoform 3). FT /FTId=VSP_028260. FT VAR_SEQ 1119 1125 LRVPSKS -> MTFSHSG (in isoform 2). FT /FTId=VSP_028258. FT VAR_SEQ 1456 1776 ILFLLYHFQQSRGNNSVSEDRKHQQVVMPFSSNTIEAHKSA FT HVDGSLKSNKLKSARKFTFLSDEDDLSAHNPLYKENISQVS FT TNSDISQRTDFVDPFSPKIQAKSKSLRGPREKIQRLWSQSV FT SLPRRLMRKVPNRPEIIDLQQWQGTRQKAENENTGICTNKR FT GSSNPLLTTEEANLTEKEEIRQGETLMIEGTEQLKSLSSDS FT SFCFPRPHFSFSTLPTVSRTVELKSEPNVISSPAECSLELS FT PSRPCVLHSSLSRRETPICMLPIETERNIFENFAHPPNISP FT SACPLPPPPPISPPSPPPAPAPLAPPPDISPFSL -> MYE FT MPQYGSRRRLLPPAGQEEYGEVVGEAEEEYEEEEEEPKKIK FT KPKVEIREPSEEEEVVVTIEKPPAAEPTYTTWKRARIFPMI FT FKKVRGLADKRGIVDLEGEEWQRRLEEEDKDYLKLTLDQEE FT ATESTVESEEESSSDYTEYSEEESEFSESETTEEESESETP FT SEEEESSTPESEESESTESEGEKARKNIVLARRRPMVEEVK FT EVKGRKEEPQEEQKEPKMEEEEHSEEEESGPAPVEESTDPE FT AQDIPEEGSAESASVEGGVESEEESESGSSSSSSESQSGGP FT WGYQVPAYDRSKNANQKKSPGANSEGYNTAL (in FT isoform 4). FT /FTId=VSP_046617. FT VAR_SEQ 1456 1675 ILFLLYHFQQSRGNNSVSEDRKHQQVVMPFSSNTIEAHKSA FT HVDGSLKSNKLKSARKFTFLSDEDDLSAHNPLYKENISQVS FT TNSDISQRTDFVDPFSPKIQAKSKSLRGPREKIQRLWSQSV FT SLPRRLMRKVPNRPEIIDLQQWQGTRQKAENENTGICTNKR FT GSSNPLLTTEEANLTEKEEIRQGETLMIEGTEQLKSLSSDS FT SFCFPRPHFSFSTLP -> MYEMPQYGSRRRLLPPAGQEEY FT GEVVGEAEEEYEEEEWARKRMIKLVVDREYETSSTGEDSAP FT ECQRNRLHHPSIHSNINGNIYIAQNGSVVRTRRACLTDNLK FT VASPVRLGGPFKKLDKLAVTHEENVPLNTLSKGPFSTEKMN FT ARPTLVTFAPCPVGTDNTAVKPLRNRLKSTVEQESMIDSKN FT IKEALEFHSDHTQSDDEELWMGPWNNLHIPMTKL (in FT isoform 6). FT /FTId=VSP_046618. FT VAR_SEQ 1458 1520 FLLYHFQQSRGNNSVSEDRKHQQVVMPFSSNTIEAHKSAHV FT DGSLKSNKLKSARKFTFLSDED -> YYRNYPWSLELILAR FT NMDKIITVMSMGMKCLNMGVAVDCYHQLDRRNMVRWLVKLR FT KNMRRKR (in isoform 5). FT /FTId=VSP_046619. FT VAR_SEQ 1521 1955 Missing (in isoform 5). FT /FTId=VSP_046620. FT VAR_SEQ 1676 1955 Missing (in isoform 6). FT /FTId=VSP_046621. FT VAR_SEQ 1777 1955 Missing (in isoform 4). FT /FTId=VSP_046622. FT VARIANT 19 19 S -> A (in dbSNP:rs11004439). FT /FTId=VAR_028289. FT VARIANT 134 134 R -> G (in DFNB23). FT /FTId=VAR_024035. FT VARIANT 178 178 D -> G (in USH1DF). FT /FTId=VAR_069297. FT VARIANT 262 262 G -> D (in DFNB23). FT /FTId=VAR_024036. FT VARIANT 380 380 G -> S (in dbSNP:rs10825269). FT /FTId=VAR_028290. FT VARIANT 435 435 D -> A (in dbSNP:rs4935502). FT /FTId=VAR_028291. FT VARIANT 929 929 R -> Q (in dbSNP:rs2135720). FT /FTId=VAR_028292. FT VARIANT 1342 1342 Q -> K (in USH1F; dbSNP:rs61731387). FT /FTId=VAR_024037. FT VARIANT 1867 1867 Missing (in USH1F). FT /FTId=VAR_024038. FT CONFLICT 261 261 L -> S (in Ref. 1; AAK31581). FT CONFLICT 467 467 Q -> L (in Ref. 1; AAK31581). FT CONFLICT 1276 1276 Q -> R (in Ref. 1; AAK31581). SQ SEQUENCE 1955 AA; 216069 MW; 23BA3A237CB188E7 CRC64; MFRQFYLWTC LASGIILGSL FEICLGQYDD DCKLARGGPP ATIVAIDEES RNGTILVDNM LIKGTAGGPD PTIELSLKDN VDYWVLMDPV KQMLFLNSTG RVLDRDPPMN IHSIVVQVQC INKKVGTIIY HEVRIVVRDR NDNSPTFKHE SYYATVNELT PVGTTIFTGF SGDNGATDID DGPNGQIEYV IQYNPDDPTS NDTFEIPLML TGNIVLRKRL NYEDKTRYFV IIQANDRAQN LNERRTTTTT LTVDVLDGDD LGPMFLPCVL VPNTRDCRPL TYQAAIPELR TPEELNPIIV TPPIQAIDQD RNIQPPSDRP GILYSILVGT PEDYPRFFHM HPRTAELSLL EPVNRDFHQK FDLVIKAEQD NGHPLPAFAG LHIEILDENN QSPYFTMPSY QGYILESAPV GATISDSLNL TSPLRIVALD KDIEDTKDPE LHLFLNDYTS VFTVTQTGIT RYLTLLQPVD REEQQTYTFS ITAFDGVQES EPVIVNIQVM DANDNTPTFP EISYDVYVYT DMRPGDSVIQ LTAVDADEGS NGEITYEILV GAQGDFIINK TTGLITIAPG VEMIVGRTYA LTVQAADNAP PAERRNSICT VYIEVLPPNN QSPPRFPQLM YSLEISEAMR VGAVLLNLQA TDREGDSITY AIENGDPQRV FNLSETTGIL TLGKALDRES TDRYILIITA SDGRPDGTST ATVNIVVTDV NDNAPVFDPY LPRNLSVVEE EANAFVGQVK ATDPDAGING QVHYSLGNFN NLFRITSNGS IYTAVKLNRE VRDYYELVVV ATDGAVHPRH STLTLAIKVL DIDDNSPVFT NSTYTVLVEE NLPAGTTILQ IEAKDVDLGA NVSYRIRSPE VKHFFALHPF TGELSLLRSL DYEAFPDQEA SITFLVEAFD IYGTMPPGIA TVTVIVKDMN DYPPVFSKRI YKGMVAPDAV KGTPITTVYA EDADPPGLPA SRVRYRVDDV QFPYPASIFE VEEDSGRVIT RVNLNEEPTT IFKLVVVAFD DGEPVMSSSA TVKILVLHPG EIPRFTQEEY RPPPVSELAT KGTMVGVISA AAINQSIVYS IVSGNEEDTF GINNITGVIY VNGPLDYETR TSYVLRVQAD SLEVVLANLR VPSKSNTAKV YIEIQDENNH PPVFQKKFYI GGVSEDARMF TSVLRVKATD KDTGNYSVMA YRLIIPPIKE GKEGFVVETY TGLIKTAMLF HNMRRSYFKF QVIATDDYGK GLSGKADVLV SVVNQLDMQV IVSNVPPTLV EKKIEDLTEI LDRYVQEQIP GAKVVVESIG ARRHGDAFSL EDYTKCDLTV YAIDPQTNRA IDRNELFKFL DGKLLDINKD FQPYYGEGGR ILEIRTPEAV TSIKKRGESL GYTEGALLAL AFIIILCCIP AILVVLVSYR QFKVRQAECT KTARIQAALP AAKPAVPAPA PVAAPPPPPP PPPGAHLYEE LGDSSILFLL YHFQQSRGNN SVSEDRKHQQ VVMPFSSNTI EAHKSAHVDG SLKSNKLKSA RKFTFLSDED DLSAHNPLYK ENISQVSTNS DISQRTDFVD PFSPKIQAKS KSLRGPREKI QRLWSQSVSL PRRLMRKVPN RPEIIDLQQW QGTRQKAENE NTGICTNKRG SSNPLLTTEE ANLTEKEEIR QGETLMIEGT EQLKSLSSDS SFCFPRPHFS FSTLPTVSRT VELKSEPNVI SSPAECSLEL SPSRPCVLHS SLSRRETPIC MLPIETERNI FENFAHPPNI SPSACPLPPP PPISPPSPPP APAPLAPPPD ISPFSLFCPP PSPPSIPLPL PPPTFFPLSV STSGPPTPPL LPPFPTPLPP PPPSIPCPPP PSASFLSTEC VCITGVKCTT NLMPAEKIKS SMTQLSTTTV CKTDPQREPK GILRHVKNLA ELEKSVANMY SQIEKNYLRT NVSELQTMCP SEVTNMEITS EQNKGSLNNI VEGTEKQSHS QSTSL //