ID PCD15_MOUSE Reviewed; 1943 AA. AC Q99PJ1; D6RCH0; E9Q7D7; E9Q7R1; E9Q7R2; F6KJX4; F6KKG6; F6R5Z7; AC F6RBV2; F6U3Q6; F6UPC9; F6VPR3; F6WUN7; F6X715; F6XPA1; F6Y0A5; AC F6YP25; F6YZQ9; F7ASH0; F7CIN1; F7D5J8; F7DFU0; F8VQ61; H3BKS0; AC Q0ZM15; Q0ZM16; Q0ZM18; Q0ZM19; Q0ZM20; Q0ZM21; Q0ZM22; Q0ZM23; AC Q0ZM24; Q0ZM25; Q0ZM26; Q0ZM27; Q0ZM28; Q0ZM29; Q0ZM30; Q0ZM31; AC Q0ZM32; Q0ZM33; Q0ZM34; Q0ZM35; Q0ZM37; Q2VQG7; Q3URZ1; Q3UTS7; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2013, sequence version 3. DT 22-JUL-2015, entry version 124. DE RecName: Full=Protocadherin-15; DE Flags: Precursor; GN Name=Pcdh15; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11138007; DOI=10.1038/83837; RA Alagramam K.N., Murcia C.L., Kwon H.Y., Pawlowski K.S., Wright C.G., RA Woychik R.P.; RT "The mouse Ames waltzer hearing-loss mutant is caused by mutation of RT Pcdh15, a novel protocadherin gene."; RL Nat. Genet. 27:99-102(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 24), AND TISSUE SPECIFICITY. RC TISSUE=Retina; RX PubMed=16799054; DOI=10.1167/iovs.06-0108; RA Haywood-Watson R.J. II, Ahmed Z.M., Kjellstrom S., Bush R.A., RA Takada Y., Hampton L.L., Battey J.F., Sieving P.A., Friedman T.B.; RT "Ames Waltzer deaf mice have reduced electroretinogram amplitudes and RT complex alternative splicing of Pcdh15 transcripts."; RL Invest. Ophthalmol. Vis. Sci. 47:3074-3084(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9; 10; 11; RP 12; 13; 14; 15; 16; 17; 18; 19; 20; 21; 22 AND 23), AND DEVELOPMENTAL RP STAGE. RC STRAIN=C57BL/6J; TISSUE=Inner ear; RX PubMed=16807332; DOI=10.1523/JNEUROSCI.1163-06.2006; RA Ahmed Z.M., Goodyear R., Riazuddin S., Lagziel A., Legan P.K., RA Behra M., Burgess S.M., Lilley K.S., Wilcox E.R., Riazuddin S., RA Griffith A.J., Frolenkov G.I., Belyantseva I.A., Richardson G.P., RA Friedman T.B.; RT "The tip-link antigen, a protein associated with the transduction RT complex of sensory hair cells, is protocadherin-15."; RL J. Neurosci. 26:7022-7034(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 21), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1763-1943 (ISOFORMS 1/2/4/5/6/7/8/9). RC STRAIN=C57BL/6J; TISSUE=Cerebellum; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1368-1943 (ISOFORMS 25 AND 26), RP INTERACTION WITH USH1G, AND SUBCELLULAR LOCATION. RC STRAIN=Swiss; TISSUE=Cochlea; RX PubMed=21436032; DOI=10.1073/pnas.1017114108; RA Caberlotto E., Michel V., Foucher I., Bahloul A., Goodyear R.J., RA Pepermans E., Michalski N., Perfettini I., Alegria-Prevot O., RA Chardenoux S., Do Cruzeiro M., Hardelin J.P., Richardson G.P., RA Avan P., Weil D., Petit C.; RT "Usher type 1G protein sans is a critical component of the tip-link RT complex, a structure controlling actin polymerization in RT stereocilia."; RL Proc. Natl. Acad. Sci. U.S.A. 108:5825-5830(2011). RN [7] RP PROTEIN SEQUENCE OF 1876-1882, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [8] RP TISSUE SPECIFICITY. RX PubMed=11429292; DOI=10.1016/S0925-4773(01)00388-4; RA Murcia C.L., Woychik R.P.; RT "Expression of Pcdh15 in the inner ear, nervous system and various RT epithelia of the developing embryo."; RL Mech. Dev. 105:163-166(2001). RN [9] RP INTERACTION WITH MYO7A, AND TISSUE SPECIFICITY. RX PubMed=16481439; DOI=10.1523/JNEUROSCI.4251-05.2006; RA Senften M., Schwander M., Kazmierczak P., Lillo C., Shin J.B., RA Hasson T., Geleoc G.S., Gillespie P.G., Williams D., Holt J.R., RA Muller U.; RT "Physical and functional interaction between protocadherin 15 and RT myosin VIIa in mechanosensory hair cells."; RL J. Neurosci. 26:2060-2071(2006). RN [10] RP INTERACTION WITH CDH23, AND TISSUE SPECIFICITY. RX PubMed=17805295; DOI=10.1038/nature06091; RA Kazmierczak P., Sakaguchi H., Tokita J., Wilson-Kubalek E.M., RA Milligan R.A., Muller U., Kachar B.; RT "Cadherin 23 and protocadherin 15 interact to form tip-link filaments RT in sensory hair cells."; RL Nature 449:87-91(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [12] RP SUBCELLULAR LOCATION, AND INTERACTION WITH LHFPL5. RX PubMed=23217710; DOI=10.1016/j.cell.2012.10.041; RA Xiong W., Grillet N., Elledge H.M., Wagner T.F., Zhao B., RA Johnson K.R., Kazmierczak P., Muller U.; RT "TMHS is an integral component of the mechanotransduction machinery of RT cochlear hair cells."; RL Cell 151:1283-1295(2012). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 27-259 IN COMPLEX WITH RP CALCIUM IONS AND CDH23, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF RP ILE-48 AND ARG-139. RX PubMed=23135401; DOI=10.1038/nature11590; RA Sotomayor M., Weihofen W.A., Gaudet R., Corey D.P.; RT "Structure of a force-conveying cadherin bond essential for inner-ear RT mechanotransduction."; RL Nature 492:128-132(2012). CC -!- FUNCTION: Calcium-dependent cell-adhesion protein. Required for CC inner ear neuroepithelial cell elaboration and cochlear function. CC Probably involved in the maintenance of normal retinal function. CC -!- SUBUNIT: antiparallel heterodimer with CDH23. Interacts with CC MYO7A. Interacts with USH1G; this interaction may recruit USH1G to CC the plasma membrane. Interacts with LHFPL5/TMHS; this interaction CC is required for efficient localization to hair bundles. CC {ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:17805295, CC ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:23135401, CC ECO:0000269|PubMed:23217710}. CC -!- INTERACTION: CC Q9ES64:Ush1c; NbExp=3; IntAct=EBI-6556746, EBI-7418968; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21436032, CC ECO:0000269|PubMed:23217710}; Single-pass membrane protein CC {ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:23217710}. CC Note=Efficient localization to the plasma membrane requires the CC presence of LHFPL5. CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 6: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 7: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 8: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 9: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 10: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 11: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 12: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 13: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 14: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 15: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 16: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 17: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 18: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 19: Cell membrane {ECO:0000250}; CC Single-pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 21: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 22: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 23: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=26; CC Name=1; Synonyms=CD1-1; CC IsoId=Q99PJ1-1; Sequence=Displayed; CC Name=2; Synonyms=CD1-2; CC IsoId=Q99PJ1-2; Sequence=VSP_046580; CC Name=3; Synonyms=CD1-3/5; CC IsoId=Q99PJ1-3; Sequence=VSP_046580, VSP_046592, VSP_046594; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=4; Synonyms=CD1-4; CC IsoId=Q99PJ1-4; Sequence=VSP_046580, VSP_046602; CC Name=5; Synonyms=CD1-6; CC IsoId=Q99PJ1-5; Sequence=VSP_046580, VSP_046591; CC Name=6; Synonyms=CD1-7; CC IsoId=Q99PJ1-6; Sequence=VSP_046580, VSP_046601, VSP_046602; CC Name=7; Synonyms=CD1-8; CC IsoId=Q99PJ1-7; Sequence=VSP_046580, VSP_046581, VSP_046601, CC VSP_046602; CC Name=8; Synonyms=CD1-9; CC IsoId=Q99PJ1-8; Sequence=VSP_046579; CC Name=9; Synonyms=CD1-10; CC IsoId=Q99PJ1-9; Sequence=VSP_046579, VSP_046601; CC Name=10; Synonyms=CD2-1; CC IsoId=Q99PJ1-10; Sequence=VSP_046588, VSP_046605; CC Name=11; Synonyms=CD2-2; CC IsoId=Q99PJ1-11; Sequence=VSP_046580, VSP_046607, VSP_046609; CC Name=12; Synonyms=CD2-3; CC IsoId=Q99PJ1-12; Sequence=VSP_046577, VSP_046588, VSP_046607, CC VSP_046609; CC Name=13; Synonyms=CD2-4; CC IsoId=Q99PJ1-13; Sequence=VSP_046580, VSP_046582, VSP_046583; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=14; Synonyms=CD2-5; CC IsoId=Q99PJ1-14; Sequence=VSP_046580, VSP_046584, VSP_046585; CC Name=15; Synonyms=CD2-6; CC IsoId=Q99PJ1-15; Sequence=VSP_046580, VSP_046587, VSP_046593; CC Name=16; Synonyms=CD2-7; CC IsoId=Q99PJ1-16; Sequence=VSP_046580, VSP_046590, VSP_046596; CC Name=17; Synonyms=CD2-8; CC IsoId=Q99PJ1-17; Sequence=VSP_046580, VSP_046595, VSP_046597; CC Name=18; Synonyms=CD3-1; CC IsoId=Q99PJ1-18; Sequence=VSP_046606, VSP_046611; CC Name=19; Synonyms=CD3-2; CC IsoId=Q99PJ1-19; Sequence=VSP_046580, VSP_046606, VSP_046611; CC Name=20; Synonyms=CD3-3; CC IsoId=Q99PJ1-20; Sequence=VSP_046576, VSP_046600, VSP_046610; CC Name=21; Synonyms=SI-1; CC IsoId=Q99PJ1-21; Sequence=VSP_046598, VSP_046599; CC Name=22; Synonyms=SI-2; CC IsoId=Q99PJ1-22; Sequence=VSP_046580, VSP_046598, VSP_046599; CC Name=23; Synonyms=SI-3; CC IsoId=Q99PJ1-23; Sequence=VSP_046580, VSP_046589, VSP_046598, CC VSP_046599; CC Name=24; Synonyms=C; CC IsoId=Q99PJ1-24; Sequence=VSP_046578, VSP_046608; CC Note=Produced by aberrant splicing sites.; CC Name=25; CC IsoId=Q99PJ1-25; Sequence=VSP_046603; CC Name=26; CC IsoId=Q99PJ1-26; Sequence=VSP_046601, VSP_046604; CC -!- TISSUE SPECIFICITY: Expressed in brain and sensory epithelium of CC the developing inner ear. Expressed in the retina, in the CC photoreceptor inner segments, the outer plexiform layer, the inner CC nuclei layer and the ganglion cell layer and, more diffusely in CC the inner plexiform layer (at protein level). Not detected in the CC retinal pigment epithelium (at protein level). Expressed in the CC spleen, dorsal root ganglion, dorsal aspect of neural tube, floor CC plate and ependymal cells adjacent to the neural canal. CC {ECO:0000269|PubMed:11429292, ECO:0000269|PubMed:16481439, CC ECO:0000269|PubMed:16799054, ECO:0000269|PubMed:17805295}. CC -!- DEVELOPMENTAL STAGE: Highest level of expression is detected at CC embryonic day 16. Alternative splicing isoforms have different CC spatiotemporal expression patterns. In cochlear cultures at the CC equivalent of postnatal day 3, isoforms belonging to the CD1 CC (isoforms 1 through 9) and CD3 (isoforms 18 through 20) groups are CC highly expressed in hair bundles in the basal coils and moderately CC in those in the middle of the apical coil; they are hardly CC detectable in those at the apical end of the apical coil (at CC protein level). At the base of the cultured cochlea, in the more CC mature hair bundles, CD3 group isoforms are restricted to the tips CC of the shorter stereocilia in both inner and outer hair cells. By CC contrast, at the same stage, isoforms belonging to the CD2 group CC (isoforms 10 through 17) are highly expressed in hair bundles in CC the apex of the cochlea and, at lower levels, in those in the CC middle of the apical coil; they are hardly detectable at the base CC of the cochlea (at protein level). In mature hair bundles, CD1 CC group isoforms are distributed fairly evenly along most of the CC length of the stereocilia on auditory hair cells, whereas they are CC concentrated toward the upper third of the hair bundle in CC vestibular hair cells. In both the auditory and the vestibular CC organs, these isoforms are excluded from a region at the very tip CC of each stereocilium (at protein level). In contrast, CD2 group CC isoforms are undetectable in adult cochlear hair cells (at protein CC level). These isoforms are expressed in the entire hair bundle of CC the immature cells in the sensory epithelium of the early CC postnatal vestibule and only in the kinocilium in the more mature CC hair bundles (at protein level). CD3 group isoforms are detected CC in immature vestibular hair bundles, concentrated toward the tip CC of each stereocilium, as early as 15.5 dpc. They also localize to CC the tips of the shorter stereocilia in the mature vestibular hair CC bundles and are not detected at the tips of the stereocilia in the CC tallest row (at protein level). {ECO:0000269|PubMed:16807332}. CC -!- DOMAIN: Cadherin repeats 1 and 2 mediate calcium-dependent CC heterophilic interaction with CDH23. CC {ECO:0000269|PubMed:23135401}. 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. CC {ECO:0000269|PubMed:23135401}. CC -!- DISEASE: Note=Defects in Pcdh15 are the cause of the Ames waltzer CC (av) phenotype. It is characterized by deafness and a balance CC disorder, associated with the degeneration of inner ear CC neuroepithelia. CC -!- SIMILARITY: Contains 11 cadherin domains. {ECO:0000255|PROSITE- CC ProRule:PRU00043}. CC -!- SEQUENCE CAUTION: CC Sequence=ABC79270.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; 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; AF281899; AAG53891.1; -; mRNA. DR EMBL; AY949849; AAY24693.1; -; mRNA. DR EMBL; DQ354396; ABC79259.1; -; mRNA. DR EMBL; DQ354397; ABC79260.1; -; mRNA. DR EMBL; DQ354398; ABC79261.1; -; mRNA. DR EMBL; DQ354399; ABC79262.1; -; mRNA. DR EMBL; DQ354400; ABC79263.1; -; mRNA. DR EMBL; DQ354401; ABC79264.1; -; mRNA. DR EMBL; DQ354402; ABC79265.1; -; mRNA. DR EMBL; DQ354403; ABC79266.1; -; mRNA. DR EMBL; DQ354404; ABC79267.1; -; mRNA. DR EMBL; DQ354405; ABC79268.1; -; mRNA. DR EMBL; DQ354406; ABC79269.1; -; mRNA. DR EMBL; DQ354407; ABC79270.1; ALT_INIT; mRNA. DR EMBL; DQ354408; ABC79271.1; -; mRNA. DR EMBL; DQ354409; ABC79272.1; -; mRNA. DR EMBL; DQ354410; ABC79273.1; -; mRNA. DR EMBL; DQ354411; ABC79274.1; -; mRNA. DR EMBL; DQ354412; ABC79275.1; -; mRNA. DR EMBL; DQ354413; ABC79276.1; -; mRNA. DR EMBL; DQ354414; ABC79277.1; -; mRNA. DR EMBL; DQ354415; ABC79278.1; -; mRNA. DR EMBL; DQ354416; ABC79279.1; -; mRNA. DR EMBL; DQ354417; ABC79280.1; -; mRNA. DR EMBL; DQ354418; ABC79281.1; -; mRNA. DR EMBL; AK139154; BAE23903.1; -; mRNA. DR EMBL; AK141024; BAE24546.1; -; mRNA. DR EMBL; AC108392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC119894; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC121142; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC121602; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC121832; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC123032; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC123809; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC144802; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC147721; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC153858; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC158800; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC159477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC186813; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC188091; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CAAA01110489; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; HQ404375; ADP09331.1; -; mRNA. DR EMBL; HQ420254; ADT91308.1; -; mRNA. DR CCDS; CCDS35934.1; -. [Q99PJ1-1] DR CCDS; CCDS48594.1; -. [Q99PJ1-6] DR CCDS; CCDS48595.1; -. [Q99PJ1-7] DR CCDS; CCDS56711.1; -. [Q99PJ1-10] DR CCDS; CCDS56712.1; -. [Q99PJ1-21] DR CCDS; CCDS56713.1; -. [Q99PJ1-18] DR CCDS; CCDS56714.1; -. [Q99PJ1-22] DR CCDS; CCDS56715.1; -. [Q99PJ1-2] DR CCDS; CCDS56716.1; -. [Q99PJ1-11] DR CCDS; CCDS56717.1; -. [Q99PJ1-19] DR CCDS; CCDS56718.1; -. [Q99PJ1-4] DR CCDS; CCDS56719.1; -. [Q99PJ1-5] DR CCDS; CCDS56720.1; -. [Q99PJ1-8] DR CCDS; CCDS56721.1; -. [Q99PJ1-9] DR RefSeq; NP_001136207.1; NM_001142735.1. [Q99PJ1-2] DR RefSeq; NP_001136208.1; NM_001142736.1. [Q99PJ1-4] DR RefSeq; NP_001136209.1; NM_001142737.1. [Q99PJ1-5] DR RefSeq; NP_001136210.1; NM_001142738.1. [Q99PJ1-7] DR RefSeq; NP_001136211.1; NM_001142739.1. [Q99PJ1-8] DR RefSeq; NP_001136212.1; NM_001142740.1. [Q99PJ1-6] DR RefSeq; NP_001136213.1; NM_001142741.1. [Q99PJ1-9] DR RefSeq; NP_001136214.1; NM_001142742.1. [Q99PJ1-10] DR RefSeq; NP_001136215.1; NM_001142743.1. [Q99PJ1-11] DR RefSeq; NP_001136218.1; NM_001142746.1. [Q99PJ1-18] DR RefSeq; NP_001136219.1; NM_001142747.1. [Q99PJ1-21] DR RefSeq; NP_001136220.1; NM_001142748.1. [Q99PJ1-22] DR RefSeq; NP_001136232.1; NM_001142760.1. [Q99PJ1-19] DR RefSeq; NP_075604.2; NM_023115.3. [Q99PJ1-1] DR RefSeq; XP_006513206.1; XM_006513143.2. [Q99PJ1-1] DR RefSeq; XP_006513219.1; XM_006513156.2. [Q99PJ1-26] DR UniGene; Mm.338933; -. DR PDB; 4APX; X-ray; 1.65 A; B=27-259. DR PDB; 4AQ8; X-ray; 2.63 A; C/D=27-259. DR PDB; 4AQA; X-ray; 1.96 A; B=27-259. DR PDB; 4AQE; X-ray; 2.27 A; B=27-259. DR PDB; 4AXW; X-ray; 2.23 A; B=27-259. DR PDBsum; 4APX; -. DR PDBsum; 4AQ8; -. DR PDBsum; 4AQA; -. DR PDBsum; 4AQE; -. DR PDBsum; 4AXW; -. DR ProteinModelPortal; Q99PJ1; -. DR SMR; Q99PJ1; 27-260. DR BioGrid; 198282; 3. DR DIP; DIP-42151N; -. DR IntAct; Q99PJ1; 2. DR MINT; MINT-1895732; -. DR STRING; 10090.ENSMUSP00000101066; -. DR PhosphoSite; Q99PJ1; -. DR PRIDE; Q99PJ1; -. DR Ensembl; ENSMUST00000092420; ENSMUSP00000090076; ENSMUSG00000052613. [Q99PJ1-6] DR Ensembl; ENSMUST00000105424; ENSMUSP00000101064; ENSMUSG00000052613. [Q99PJ1-2] DR Ensembl; ENSMUST00000105426; ENSMUSP00000101066; ENSMUSG00000052613. [Q99PJ1-4] DR Ensembl; ENSMUST00000105429; ENSMUSP00000101069; ENSMUSG00000052613. [Q99PJ1-5] DR Ensembl; ENSMUST00000124046; ENSMUSP00000121130; ENSMUSG00000052613. [Q99PJ1-12] DR Ensembl; ENSMUST00000125006; ENSMUSP00000120056; ENSMUSG00000052613. [Q99PJ1-22] DR Ensembl; ENSMUST00000125055; ENSMUSP00000114326; ENSMUSG00000052613. [Q99PJ1-3] DR Ensembl; ENSMUST00000125517; ENSMUSP00000115399; ENSMUSG00000052613. [Q99PJ1-16] DR Ensembl; ENSMUST00000126920; ENSMUSP00000121939; ENSMUSG00000052613. [Q99PJ1-8] DR Ensembl; ENSMUST00000129404; ENSMUSP00000117731; ENSMUSG00000052613. [Q99PJ1-9] DR Ensembl; ENSMUST00000131321; ENSMUSP00000122911; ENSMUSG00000052613. [Q99PJ1-4] DR Ensembl; ENSMUST00000131724; ENSMUSP00000122466; ENSMUSG00000052613. [Q99PJ1-11] DR Ensembl; ENSMUST00000134009; ENSMUSP00000120618; ENSMUSG00000052613. [Q99PJ1-23] DR Ensembl; ENSMUST00000136096; ENSMUSP00000121534; ENSMUSG00000052613. [Q99PJ1-3] DR Ensembl; ENSMUST00000144302; ENSMUSP00000122606; ENSMUSG00000052613. [Q99PJ1-13] DR Ensembl; ENSMUST00000146682; ENSMUSP00000134863; ENSMUSG00000052613. [Q99PJ1-20] DR Ensembl; ENSMUST00000147189; ENSMUSP00000122940; ENSMUSG00000052613. [Q99PJ1-7] DR Ensembl; ENSMUST00000151116; ENSMUSP00000119662; ENSMUSG00000052613. [Q99PJ1-10] DR Ensembl; ENSMUST00000152655; ENSMUSP00000118201; ENSMUSG00000052613. [Q99PJ1-17] DR Ensembl; ENSMUST00000152819; ENSMUSP00000123647; ENSMUSG00000052613. [Q99PJ1-15] DR Ensembl; ENSMUST00000155701; ENSMUSP00000135495; ENSMUSG00000052613. [Q99PJ1-14] DR Ensembl; ENSMUST00000177107; ENSMUSP00000135501; ENSMUSG00000052613. [Q99PJ1-18] DR Ensembl; ENSMUST00000177420; ENSMUSP00000135849; ENSMUSG00000052613. [Q99PJ1-21] DR Ensembl; ENSMUST00000191709; ENSMUSP00000142313; ENSMUSG00000052613. [Q99PJ1-25] DR Ensembl; ENSMUST00000191854; ENSMUSP00000141973; ENSMUSG00000052613. [Q99PJ1-19] DR Ensembl; ENSMUST00000193361; ENSMUSP00000141792; ENSMUSG00000052613. [Q99PJ1-1] DR Ensembl; ENSMUST00000193739; ENSMUSP00000142173; ENSMUSG00000052613. [Q99PJ1-26] DR GeneID; 11994; -. DR KEGG; mmu:11994; -. DR UCSC; uc007fpf.2; mouse. [Q99PJ1-21] DR UCSC; uc007fpg.2; mouse. [Q99PJ1-22] DR UCSC; uc007fph.2; mouse. [Q99PJ1-10] DR UCSC; uc007fpi.2; mouse. [Q99PJ1-8] DR UCSC; uc007fpj.2; mouse. [Q99PJ1-9] DR UCSC; uc007fpk.2; mouse. [Q99PJ1-1] DR UCSC; uc007fpl.2; mouse. [Q99PJ1-4] DR UCSC; uc007fpn.2; mouse. [Q99PJ1-6] DR UCSC; uc007fpo.2; mouse. [Q99PJ1-17] DR UCSC; uc007fpq.2; mouse. [Q99PJ1-20] DR UCSC; uc007fpr.2; mouse. [Q99PJ1-11] DR UCSC; uc011xfz.1; mouse. [Q99PJ1-23] DR UCSC; uc011xgb.1; mouse. [Q99PJ1-7] DR UCSC; uc011xgc.1; mouse. [Q99PJ1-5] DR UCSC; uc011xgd.1; mouse. [Q99PJ1-15] DR UCSC; uc011xge.1; mouse. [Q99PJ1-16] DR UCSC; uc011xgf.1; mouse. [Q99PJ1-14] DR UCSC; uc011xgg.1; mouse. [Q99PJ1-18] DR UCSC; uc011xgh.1; mouse. [Q99PJ1-19] DR UCSC; uc033fqa.1; mouse. [Q99PJ1-2] DR CTD; 65217; -. DR MGI; MGI:1891428; Pcdh15. DR eggNOG; NOG253862; -. DR GeneTree; ENSGT00760000118805; -. DR HOGENOM; HOG000186027; -. DR HOVERGEN; HBG053521; -. DR InParanoid; Q99PJ1; -. DR KO; K16500; -. DR OrthoDB; EOG7ZWD0W; -. DR TreeFam; TF326779; -. DR ChiTaRS; Pcdh15; mouse. DR NextBio; 280177; -. DR PRO; PR:Q99PJ1; -. DR Proteomes; UP000000589; Chromosome 10. DR CleanEx; MM_PCDH15; -. DR ExpressionAtlas; Q99PJ1; baseline and differential. DR Genevisible; Q99PJ1; MM. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0016021; C:integral component of membrane; ISS:MGI. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0032420; C:stereocilium; IDA:HGNC. DR GO; GO:0045202; C:synapse; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0007015; P:actin filament organization; IMP:MGI. DR GO; GO:0007628; P:adult walking behavior; IMP:MGI. DR GO; GO:0042491; P:auditory receptor cell differentiation; IMP:MGI. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI. DR GO; GO:0050973; P:detection of mechanical stimulus involved in equilibrioception; IMP:MGI. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI. DR GO; GO:0050957; P:equilibrioception; ISO:MGI. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro. DR GO; GO:0048839; P:inner ear development; IMP:MGI. DR GO; GO:0060122; P:inner ear receptor stereocilium organization; IMP:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:0035058; P:nonmotile primary cilium assembly; IMP:MGI. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:MGI. DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl. DR GO; GO:0060013; P:righting reflex; IMP:MGI. DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:MGI. DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI. DR GO; GO:0001964; P:startle response; IMP:MGI. DR GO; GO:0007601; P:visual perception; IMP:MGI. DR Gene3D; 2.60.40.60; -; 10. DR InterPro; IPR002126; Cadherin. DR InterPro; IPR015919; Cadherin-like. DR InterPro; IPR020894; Cadherin_CS. DR InterPro; IPR030718; Protocadherin-15. DR PANTHER; PTHR24028:SF11; PTHR24028:SF11; 1. DR Pfam; PF00028; Cadherin; 8. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 11. DR SUPFAM; SSF49313; SSF49313; 10. DR PROSITE; PS00232; CADHERIN_1; 4. DR PROSITE; PS50268; CADHERIN_2; 11. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; KW Cell membrane; Complete proteome; Deafness; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Hearing; Membrane; Reference proteome; KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 1943 Protocadherin-15. FT /FTId=PRO_0000003999. FT TOPO_DOM 27 1381 Extracellular. {ECO:0000255}. FT TRANSMEM 1382 1402 Helical. {ECO:0000255}. FT TOPO_DOM 1403 1943 Cytoplasmic. {ECO:0000255}. FT DOMAIN 45 152 Cadherin 1. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 153 270 Cadherin 2. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 283 400 Cadherin 3. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 401 514 Cadherin 4. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 515 621 Cadherin 5. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 622 722 Cadherin 6. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 724 824 Cadherin 7. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 825 931 Cadherin 8. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 932 1040 Cadherin 9. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 1042 1149 Cadherin 10. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 1150 1264 Cadherin 11. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT COMPBIAS 1437 1448 Poly-Pro. FT COMPBIAS 1772 1778 Poly-Pro. FT COMPBIAS 1804 1812 Poly-Pro. FT CARBOHYD 57 57 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 102 102 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 206 206 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 424 424 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 564 564 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 667 667 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 729 729 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 773 773 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 826 826 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 856 856 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 1069 1069 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 1089 1089 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 1180 1180 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 37 125 {ECO:0000269|PubMed:23135401}. FT VAR_SEQ 1 1252 Missing (in isoform 20). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046576. FT VAR_SEQ 1 401 Missing (in isoform 12). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046577. FT VAR_SEQ 31 600 Missing (in isoform 24). FT {ECO:0000303|PubMed:16799054}. FT /FTId=VSP_046578. FT VAR_SEQ 31 57 Missing (in isoform 8 and isoform 9). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046579. FT VAR_SEQ 31 35 Missing (in isoform 2, isoform 3, isoform FT 4, isoform 5, isoform 6, isoform 7, FT isoform 11, isoform 13, isoform 14, FT isoform 15, isoform 16, isoform 17, FT isoform 19, isoform 22 and isoform 23). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046580. FT VAR_SEQ 204 240 Missing (in isoform 7). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046581. FT VAR_SEQ 298 331 EELNPILVTPPIQAIDQDRNIQPPSDRPGILYSI -> DFG FT SLRSGANSWCQGCGGVHRCPSPWRRLLPRRL (in FT isoform 13). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046582. FT VAR_SEQ 332 1943 Missing (in isoform 13). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046583. FT VAR_SEQ 335 339 TPEDY -> RARES (in isoform 14). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046584. FT VAR_SEQ 340 1943 Missing (in isoform 14). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046585. FT VAR_SEQ 372 655 AEQDNGHPLPAFASLHIEILDENNQSPYFTMPSYQGYILES FT APVGATISESLNLTTPLRIVALDKDIEDTKDPELHLFLNDY FT TSVFTVTPTGITRYLTLLQPVDREEQQTYTFLITAFDGVQE FT SEPVVVNIRVMDANDNTPTFPEISYDVYVYTDMSPGDSVIQ FT LTAVDADEGSNGEISYEILVGGKGDFVINKTTGLVSIAPGV FT ELIVGQTYALTVQASDNAPPAERRHSICTVYIEVLPPNNQS FT PPRFPQLMYSLEVSEAMRIGAILLNLQATDREGDPITY -> FT VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRA FT RIFPMIFKKVRGLAEKRGIDLEGEEWRRRLDEEDKDYLQLT FT LDQEEATESTVESEEESSDYTEYTETESEFSESETTEESES FT ETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVV FT EEIQEVKGKREEPPVEEEEEPPLEEEERAEEGEESEAAPMD FT ESTDLEAQDVPEEGSAESVSMERGVESEESESELSSSSSTS FT ESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL FT (in isoform 15). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046587. FT VAR_SEQ 440 440 D -> DVPPGGVP (in isoform 10 and isoform FT 12). {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046588. FT VAR_SEQ 441 961 Missing (in isoform 23). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046589. FT VAR_SEQ 441 725 TKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQT FT YTFLITAFDGVQESEPVVVNIRVMDANDNTPTFPEISYDVY FT VYTDMSPGDSVIQLTAVDADEGSNGEISYEILVGGKGDFVI FT NKTTGLVSIAPGVELIVGQTYALTVQASDNAPPAERRHSIC FT TVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAILLNLQA FT TDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDREST FT DRYILIVTASDGRPDGTSTATVNIVVTDVNDNAPVFDPY FT -> VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTW FT KRARIFPMIFKKVRGLAEKRGIDLEGEEWRRRLDEEDKDYL FT QLTLDQEEATESTVESEEESSDYTEYTETESEFSESETTEE FT SESETPSEEAEESSTPESEESESTESEGEKARKNIVLARRR FT PVVEEIQEVKGKREEPPVEEEEEPPLEEEERAEEGEESEAA FT PMDESTDLEAQDVPEEGSAESVSMERGVESEESESELSSSS FT STSESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL FT (in isoform 16). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046590. FT VAR_SEQ 600 671 RHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAIL FT LNLQATDREGDPITYAIENGDPQRVFNLSET -> S (in FT isoform 5). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046591. FT VAR_SEQ 645 689 ATDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDRES FT TDRY -> HRDSQPREGSRPREHRPLHPHRHSLRWQTGWNL FT NCHCEHSGDGRQ (in isoform 3). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046592. FT VAR_SEQ 656 1943 Missing (in isoform 15). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046593. FT VAR_SEQ 690 1943 Missing (in isoform 3). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046594. FT VAR_SEQ 703 986 TSTATVNIVVTDVNDNAPVFDPYLPRNLSVVEEEANAFVGQ FT VRATDPDAGINGQVHYSLGNFNNLFRITSNGSIYTAVKLNR FT EARDHYELVVVATDGAVHPRHSTLTLYIKVLDIDDNSPVFT FT NSTYTVVVEENLPAGTSFLQIEAKDVDLGANVSYRIRSPEV FT KHLFALHPFTGELSLLRSLDYEAFPDQEASITFLVEAFDIY FT GTMPPGIATVTVIVKDMNDYPPVFSKRIYKGMVAPDAVKGT FT PITTVYAEDADPPGMPASRVRYRVDDVQFPYPASIFDV -> FT VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRA FT RIFPMIFKKVRGLAEKRGIDLEGEEWRRRLDEEDKDYLQLT FT LDQEEATESTVESEEESSDYTEYTETESEFSESETTEESES FT ETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVV FT EEIQEVKGKREEPPVEEEEEPPLEEEERAEEGEESEAAPMD FT ESTDLEAQDVPEEGSAESVSMERGVESEESESELSSSSSTS FT ESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL FT (in isoform 17). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046595. FT VAR_SEQ 726 1943 Missing (in isoform 16). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046596. FT VAR_SEQ 987 1943 Missing (in isoform 17). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046597. FT VAR_SEQ 1131 1176 NTAKVYIEIQDENDHPPVFQKKFYIGGVSEDARMFASVLRV FT KATDR -> LSVIPCSWRTQVSKSLGLELGVPVSHSVESGT FT RTGSSTRAASVPIH (in isoform 21, isoform 22 FT and isoform 23). FT {ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046598. FT VAR_SEQ 1177 1943 Missing (in isoform 21, isoform 22 and FT isoform 23). FT {ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046599. FT VAR_SEQ 1407 1667 FKVRQAECTKTARIQSAMPAAKPAAPVPAAPAPPPPPPPPP FT PGAHLYEELGESAMHNLFLLYHFEQSRGNNSVPEDRSSHRD FT GMAFSSSTTESHEPAHVEGPLKESQPNPARTFSFVPDEDNL FT STHNPLYMESIGQRSTNSDLQPRTDFEELLAPRTQVKSQSL FT RGPREKIQRVWNQSVSFPRRLMWKAPNRPETIDLVEWQITN FT QRAECESARCHPSQRGSSNVLLATEDAHESEKEGGHRDTLI FT VQQTEQLKSLSSGSS -> GGFAPEHQLLRPSLLKPEELSM FT ESGIDPGQEYGQDYYSYEHGYEMPQYGSRRRLLPPAGQEEY FT GEVIGEAEEEYEEEEWARKRMIKLVVDREYESSSPGEDSAP FT ESQRSRTHKPSGRSNVNGNIYIAQNGSVVRTRRACVADNLK FT VPSPGLLGRHLKKLDTLAGTREENVPLNTLFKGPFSTEKAK FT RTPTLVTFAPCPVVAEHSAVKPSGTRLKHTAEQESMVDSRL FT SRESMEFHGDSAPSDEEELWMGPWNSLHIPMTKL (in FT isoform 20). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046600. FT VAR_SEQ 1407 1409 Missing (in isoform 6, isoform 7, isoform FT 9 and isoform 26). FT {ECO:0000303|PubMed:16807332, FT ECO:0000303|PubMed:21436032}. FT /FTId=VSP_046601. FT VAR_SEQ 1461 1463 MHN -> I (in isoform 4, isoform 6 and FT isoform 7). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046602. FT VAR_SEQ 1462 1943 HNLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEP FT AHVEGPLKESQPNPARTFSFVPDEDNLSTHNPLYMESIGQR FT STNSDLQPRTDFEELLAPRTQVKSQSLRGPREKIQRVWNQS FT VSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQ FT RGSSNVLLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGS FT SFSSSWSHFSFSTLPTISRAVELGSEPNVVTSPADCTLELS FT PPLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSIS FT APLPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPIST FT PPTSSLPLPPPLSLPPPPRPPAPRLFPQPPSTSIPSTDSIS FT APAAKCTASATHARETTSTTQPPASNPQWGAEPHRHPKGIL FT RHVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKT FT GMKITHDQSQETLVRVVEGIDVQPHSQSTSL -> YEMPQY FT GSRRRLLPPAGQEEYGEVIGEAEEEYEEEEVEPEKVKKPKV FT EIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVR FT GLAEKRGIDLEGEEWRRRLDEEDKDYLQLTLDQEEATESTV FT ESEEESSDYTEYTETESEFSESETTEESESETPSEEAEESS FT TPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKRE FT EPPVEEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVP FT EEGSAESVSMERGVESEESESELSSSSSTSESLSGGPWGFQ FT VPEYDRRKDEEPKKSPGANSEGYNTAL (in isoform FT 25). {ECO:0000303|PubMed:21436032}. FT /FTId=VSP_046603. FT VAR_SEQ 1462 1943 HNLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEP FT AHVEGPLKESQPNPARTFSFVPDEDNLSTHNPLYMESIGQR FT STNSDLQPRTDFEELLAPRTQVKSQSLRGPREKIQRVWNQS FT VSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQ FT RGSSNVLLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGS FT SFSSSWSHFSFSTLPTISRAVELGSEPNVVTSPADCTLELS FT PPLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSIS FT APLPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPIST FT PPTSSLPLPPPLSLPPPPRPPAPRLFPQPPSTSIPSTDSIS FT APAAKCTASATHARETTSTTQPPASNPQWGAEPHRHPKGIL FT RHVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKT FT GMKITHDQSQETLVRVVEGIDVQPHSQSTSL -> YEMPQY FT GSRRRLLPPAGQEEYGEVIGEAEEEYEEEEWARKRMIKLVV FT DREYESSSPGEDSAPESQRSRTHKPSGRSNVNGNIYIAQNG FT SVVRTRRACVADNLKVPSPGLLGRHLKKLDTLAGTREENVP FT LNTLFKGPFSTEKAKRTPTLVTFAPCPVVAEHSAVKPSGTR FT LKHTAEQESMVDSRLSRESMEFHGDSAPSDEEELWMGPWNS FT LHIPMTKL (in isoform 26). FT {ECO:0000303|PubMed:21436032}. FT /FTId=VSP_046604. FT VAR_SEQ 1463 1943 NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPA FT HVEGPLKESQPNPARTFSFVPDEDNLSTHNPLYMESIGQRS FT TNSDLQPRTDFEELLAPRTQVKSQSLRGPREKIQRVWNQSV FT SFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQR FT GSSNVLLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGSS FT FSSSWSHFSFSTLPTISRAVELGSEPNVVTSPADCTLELSP FT PLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSISA FT PLPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPISTP FT PTSSLPLPPPLSLPPPPRPPAPRLFPQPPSTSIPSTDSISA FT PAAKCTASATHARETTSTTQPPASNPQWGAEPHRHPKGILR FT HVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKTG FT MKITHDQSQETLVRVVEGIDVQPHSQSTSL -> KYEMPQY FT GSRRRLLPPAGQEEYGEVIGEAEEEYEEEEVEPEKVKKPKV FT EIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVR FT GLAEKRGIDLEGEEWRRRLDEEDKDYLQLTLDQEEATESTV FT ESEEESSDYTEYTETESEFSESETTEESESETPSEEAEESS FT TPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKRE FT EPPVEEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVP FT EEGSAESVSMERGVESEESESELSSSSSTSESLSGGPWGFQ FT VPEYDRRKDEEPKKSPGANSEGYNTAL (in isoform FT 10). {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046605. FT VAR_SEQ 1463 1682 NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPA FT HVEGPLKESQPNPARTFSFVPDEDNLSTHNPLYMESIGQRS FT TNSDLQPRTDFEELLAPRTQVKSQSLRGPREKIQRVWNQSV FT SFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQR FT GSSNVLLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGSS FT FSSSWSHFSFSTLPT -> KYEMPQYGSRRRLLPPAGQEEY FT GEVIGEAEEEYEEEEWARKRMIKLVVDREYESSSPGEDSAP FT ESQRSRTHKPSGRSNVNGNIYIAQNGSVVRTRRACVADNLK FT VPSPGLLGRHLKKLDTLAGTREENVPLNTLFKGPFSTEKAK FT RTPTLVTFAPCPVVAEHSAVKPSGTRLKHTAEQESMVDSRL FT SRESMEFHGDSAPSDEEELWMGPWNSLHIPMTKL (in FT isoform 18 and isoform 19). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046606. FT VAR_SEQ 1463 1523 NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPA FT HVEGPLKESQPNPARTFSFV -> KSYPWNLGLILARNMDK FT IITVMSMGMRCPSMEVAVDCCHLLDRRNTAKSLVKLKRNMK FT KKR (in isoform 11 and isoform 12). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046607. FT VAR_SEQ 1464 1473 Missing (in isoform 24). FT {ECO:0000303|PubMed:16799054}. FT /FTId=VSP_046608. FT VAR_SEQ 1524 1943 Missing (in isoform 11 and isoform 12). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046609. FT VAR_SEQ 1668 1943 Missing (in isoform 20). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046610. FT VAR_SEQ 1683 1943 Missing (in isoform 18 and isoform 19). FT {ECO:0000303|PubMed:16807332}. FT /FTId=VSP_046611. FT MUTAGEN 48 48 I->A: Strongly reduced interaction with FT CDH23. {ECO:0000269|PubMed:23135401}. FT MUTAGEN 139 139 R->G: Impaired interaction with CDH23. FT {ECO:0000269|PubMed:23135401}. FT CONFLICT 608 608 I -> T (in Ref. 1; AAG53891, 2; AAY24693 FT and 3; ABC79259/ABC79260/ABC79261/ FT ABC79262/ABC79264/ABC79265/ABC79266/ FT ABC79267/ABC79268/ABC79269/ABC79270/ FT ABC79276/ABC79277). {ECO:0000305}. FT CONFLICT 901 901 V -> A (in Ref. 1; AAG53891, 2; AAY24693 FT and 3; ABC79259/ABC79261/ABC79263/ FT ABC79264/ABC79265/ABC79266/ABC79267/ FT ABC79268/ABC79269/ABC79270/ABC79276/ FT ABC79277). {ECO:0000305}. FT CONFLICT 1748 1748 S -> F (in Ref. 1; AAG53891, 2; AAY24693 FT and 3; ABC79259/ABC79261/ABC79263/ FT ABC79264/ABC79265/ABC79266/ABC79267). FT {ECO:0000305}. FT CONFLICT 1848 1848 S -> F (in Ref. 1; AAG53891, 2; AAY24693 FT and 3; ABC79259/ABC79261/ABC79263/ FT ABC79264/ABC79265/ABC79266/ABC79267). FT {ECO:0000305}. FT CONFLICT 1859 1859 W -> G (in Ref. 4; BAE24546). FT {ECO:0000305}. FT TURN 27 30 {ECO:0000244|PDB:4APX}. FT HELIX 31 34 {ECO:0000244|PDB:4APX}. FT STRAND 38 41 {ECO:0000244|PDB:4APX}. FT STRAND 45 52 {ECO:0000244|PDB:4APX}. FT STRAND 60 63 {ECO:0000244|PDB:4APX}. FT STRAND 67 69 {ECO:0000244|PDB:4APX}. FT STRAND 71 75 {ECO:0000244|PDB:4APX}. FT STRAND 77 84 {ECO:0000244|PDB:4APX}. FT HELIX 86 88 {ECO:0000244|PDB:4APX}. FT STRAND 90 93 {ECO:0000244|PDB:4APX}. FT TURN 94 97 {ECO:0000244|PDB:4APX}. FT STRAND 98 101 {ECO:0000244|PDB:4APX}. FT TURN 112 114 {ECO:0000244|PDB:4APX}. FT STRAND 118 127 {ECO:0000244|PDB:4APX}. FT TURN 128 130 {ECO:0000244|PDB:4APX}. FT STRAND 133 143 {ECO:0000244|PDB:4APX}. FT STRAND 151 155 {ECO:0000244|PDB:4APX}. FT STRAND 157 162 {ECO:0000244|PDB:4APX}. FT STRAND 170 172 {ECO:0000244|PDB:4APX}. FT TURN 174 179 {ECO:0000244|PDB:4APX}. FT STRAND 180 182 {ECO:0000244|PDB:4APX}. FT STRAND 184 186 {ECO:0000244|PDB:4AQ8}. FT HELIX 187 190 {ECO:0000244|PDB:4APX}. FT STRAND 192 197 {ECO:0000244|PDB:4APX}. FT HELIX 205 208 {ECO:0000244|PDB:4APX}. FT TURN 214 216 {ECO:0000244|PDB:4APX}. FT STRAND 219 221 {ECO:0000244|PDB:4APX}. FT TURN 227 229 {ECO:0000244|PDB:4APX}. FT STRAND 232 241 {ECO:0000244|PDB:4APX}. FT HELIX 246 248 {ECO:0000244|PDB:4APX}. FT STRAND 251 259 {ECO:0000244|PDB:4APX}. SQ SEQUENCE 1943 AA; 214738 MW; 6FD6836082655855 CRC64; MFLQFAVWKC LPHGILIASL LVVSWGQYDD DWQYEDCKLA RGGPPATIVA IDEESRNGTI LVDNMLIKGT AGGPDPTIEL SLKDNVDYWV LLDPVKQMLF LNSTGRVLDR DPPMNIHSIV VQVQCVNKKV GTVIYHEVRI VVRDRNDNSP TFKHESYYAT VNELTPVGTT IFTGFSGDNG ATDIDDGPNG QIEYVIQYNP EDPTSNDTFE IPLMLTGNVV LRKRLNYEDK TRYYVIIQAN DRAQNLNERR TTTTTLTVDV LDGDDLGPMF LPCVLVPNTR DCRPLTYQAA IPELRTPEEL NPILVTPPIQ AIDQDRNIQP PSDRPGILYS ILVGTPEDYP RFFHMHPRTA ELTLLEPVNR DFHQKFDLVI KAEQDNGHPL PAFASLHIEI LDENNQSPYF TMPSYQGYIL ESAPVGATIS ESLNLTTPLR IVALDKDIED TKDPELHLFL NDYTSVFTVT PTGITRYLTL LQPVDREEQQ TYTFLITAFD GVQESEPVVV NIRVMDANDN TPTFPEISYD VYVYTDMSPG DSVIQLTAVD ADEGSNGEIS YEILVGGKGD FVINKTTGLV SIAPGVELIV GQTYALTVQA SDNAPPAERR HSICTVYIEV LPPNNQSPPR FPQLMYSLEV SEAMRIGAIL LNLQATDREG DPITYAIENG DPQRVFNLSE TTGILSLGKA LDRESTDRYI LIVTASDGRP DGTSTATVNI VVTDVNDNAP VFDPYLPRNL SVVEEEANAF VGQVRATDPD AGINGQVHYS LGNFNNLFRI TSNGSIYTAV KLNREARDHY ELVVVATDGA VHPRHSTLTL YIKVLDIDDN SPVFTNSTYT VVVEENLPAG TSFLQIEAKD VDLGANVSYR IRSPEVKHLF ALHPFTGELS LLRSLDYEAF PDQEASITFL VEAFDIYGTM PPGIATVTVI VKDMNDYPPV FSKRIYKGMV APDAVKGTPI TTVYAEDADP PGMPASRVRY RVDDVQFPYP ASIFDVEEDS GRVVTRVNLN EEPTTIFKLV VVAFDDGEPV MSSSATVRIL VLHPGEIPRF TQEEYRPPPV SELAARGTVV GVISAAAINQ SIVYSIVAGN EEDKFGINNV TGVIYVNSPL DYETRTSYVL RVQADSLEVV LANLRVPSKS NTAKVYIEIQ DENDHPPVFQ KKFYIGGVSE DARMFASVLR VKATDRDTGN YSAMAYRLII PPIKEGKEGF VVETYTGLIK TAMLFHNMRR SYFKFQVIAT DDYGKGLSGK ADVLVSVVNQ LDMQVIVSNV PPTLVEKKIE DLTEILDRYV QEQIPGAKVV VESIGARRHG DAYSLEDYSK CDLTVYAIDP QTNRAIDRNE LFKFLDGKLL DINKDFQPYY GEGGRILEIR TPEAVTSIKK RGESLGYTEG ALLALAFIII LCCIPAILVV LVSYRQFKVR QAECTKTARI QSAMPAAKPA APVPAAPAPP PPPPPPPPGA HLYEELGESA MHNLFLLYHF EQSRGNNSVP EDRSSHRDGM AFSSSTTESH EPAHVEGPLK ESQPNPARTF SFVPDEDNLS THNPLYMESI GQRSTNSDLQ PRTDFEELLA PRTQVKSQSL RGPREKIQRV WNQSVSFPRR LMWKAPNRPE TIDLVEWQIT NQRAECESAR CHPSQRGSSN VLLATEDAHE SEKEGGHRDT LIVQQTEQLK SLSSGSSFSS SWSHFSFSTL PTISRAVELG SEPNVVTSPA DCTLELSPPL RPRILNSLSS KRETPTCASD TEPKRNSFEI APHPPSISAP LPHPPLPRPP IAFTTFPLPL SPPNPPPPQL VTFSLPISTP PTSSLPLPPP LSLPPPPRPP APRLFPQPPS TSIPSTDSIS APAAKCTASA THARETTSTT QPPASNPQWG AEPHRHPKGI LRHVKNLAEL EKSVSNMYSH IEKNCPPADP SKLHTFCPAE KTGMKITHDQ SQETLVRVVE GIDVQPHSQS TSL //