ID PCD15_MOUSE Reviewed; 1943 AA. AC Q99PJ1; D6RCH0; E9Q7D7; E9Q7R1; E9Q7R2; F6KJX4; F6KKG6; F6R5Z7; F6RBV2; AC F6U3Q6; F6UPC9; F6VPR3; F6WUN7; F6X715; F6XPA1; F6Y0A5; F6YP25; F6YZQ9; AC F7ASH0; F7CIN1; F7D5J8; F7DFU0; F8VQ61; H3BKS0; Q0ZM15; Q0ZM16; Q0ZM18; AC Q0ZM19; Q0ZM20; Q0ZM21; Q0ZM22; Q0ZM23; Q0ZM24; Q0ZM25; Q0ZM26; Q0ZM27; AC Q0ZM28; Q0ZM29; Q0ZM30; Q0ZM31; Q0ZM32; Q0ZM33; Q0ZM34; Q0ZM35; Q0ZM37; AC Q2VQG7; Q3URZ1; Q3UTS7; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2013, sequence version 3. DT 27-MAR-2024, entry version 180. DE RecName: Full=Protocadherin-15; DE Flags: Precursor; GN Name=Pcdh15; 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] (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., Takada Y., RA 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; 12; RP 13; 14; 15; 16; 17; 18; 19; 20; 21; 22 AND 23), AND DEVELOPMENTAL 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., Behra M., RA Burgess S.M., Lilley K.S., Wilcox E.R., Riazuddin S., Griffith A.J., RA Frolenkov G.I., Belyantseva I.A., Richardson G.P., Friedman T.B.; RT "The tip-link antigen, a protein associated with the transduction complex RT 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., 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 [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., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1368-1943 (ISOFORMS 25 AND 26), INTERACTION RP WITH USH1G, AND SUBCELLULAR LOCATION. RC STRAIN=SWR/J; 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., Avan P., RA 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 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 SPECTROMETRY. RC STRAIN=C57BL/6J; 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., Hasson T., RA Geleoc G.S., Gillespie P.G., Williams D., Holt J.R., Muller U.; RT "Physical and functional interaction between protocadherin 15 and myosin RT 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 in RT 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., Johnson K.R., RA 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 IDENTIFICATION IN A COMPLEX WITH LHFPL5 AND PCDH15. RX PubMed=25467981; DOI=10.1016/j.neuron.2014.10.041; RA Zhao B., Wu Z., Grillet N., Yan L., Xiong W., Harkins-Perry S., Mueller U.; RT "TMIE is an essential component of the mechanotransduction machinery of RT cochlear hair cells."; RL Neuron 84:954-967(2014). RN [14] RP INTERACTION WITH TMC1 AND TMC2. RX PubMed=25114259; DOI=10.1073/pnas.1402152111; RA Maeda R., Kindt K.S., Mo W., Morgan C.P., Erickson T., Zhao H., RA Clemens-Grisham R., Barr-Gillespie P.G., Nicolson T.; RT "Tip-link protein protocadherin 15 interacts with transmembrane channel- RT like proteins TMC1 and TMC2."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12907-12912(2014). RN [15] RP INTERACTION WITH TOMT. RX PubMed=28504928; DOI=10.7554/elife.24318; RA Cunningham C.L., Wu Z., Jafari A., Zhao B., Schrode K., Harkins-Perry S., RA Lauer A., Mueller U.; RT "The murine catecholamine methyltransferase mTOMT is essential for RT mechanotransduction by cochlear hair cells."; RL Elife 6:0-0(2017). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 27-259 IN COMPLEX WITH CALCIUM RP IONS AND CDH23, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF ILE-48 AND RP 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 inner CC ear neuroepithelial cell elaboration and cochlear function. Probably CC involved in the maintenance of normal retinal function. CC -!- SUBUNIT: Antiparallel heterodimer with CDH23 (PubMed:23135401, CC PubMed:17805295). Found in a complex with TMIE and LHFPL5 CC (PubMed:25467981). Interacts with LHFPL5/TMHS; this interaction is CC required for efficient localization to hair bundles (PubMed:23217710). CC Interacts with MYO7A (PubMed:16481439). Interacts with USH1G; this CC interaction may recruit USH1G to the plasma membrane (PubMed:21436032). CC Interacts with TOMT (PubMed:28504928). Isoforms CD1 and CD3 interact CC with TMC1 (via N-terminus) and TMC2 (via N-terminus) (PubMed:25114259). CC {ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:17805295, CC ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:23135401, CC ECO:0000269|PubMed:23217710, ECO:0000269|PubMed:25114259, CC ECO:0000269|PubMed:25467981, ECO:0000269|PubMed:28504928}. CC -!- INTERACTION: CC Q99PJ1; Q99PF4-1: Cdh23; NbExp=10; IntAct=EBI-6556746, EBI-15656347; CC Q99PJ1; Q9ES64: Ush1c; NbExp=3; IntAct=EBI-6556746, EBI-7418968; CC Q99PJ1; Q9ES64-3: Ush1c; NbExp=2; IntAct=EBI-6556746, EBI-7418919; 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}; Single- CC pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000250}; Single- CC pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000250}; Single- CC pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000250}; Single- CC pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane {ECO:0000250}; Single- CC pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cell membrane {ECO:0000250}; Single- CC pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cell membrane {ECO:0000250}; Single- CC pass type I membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 9]: Cell membrane {ECO:0000250}; Single- CC 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 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 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 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 the CC developing inner ear. Expressed in the retina, in the photoreceptor CC inner segments, the outer plexiform layer, the inner nuclei layer and CC the ganglion cell layer and, more diffusely in the inner plexiform CC layer (at protein level). Not detected in the retinal pigment CC epithelium (at protein level). Expressed in the spleen, dorsal root CC ganglion, dorsal aspect of neural tube, floor plate and ependymal cells CC adjacent to the neural canal. {ECO:0000269|PubMed:11429292, CC ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:16799054, CC 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 (isoforms CC 1 through 9) and CD3 (isoforms 18 through 20) groups are highly CC expressed in hair bundles in the basal coils and moderately in those in CC the middle of the apical coil; they are hardly detectable in those at CC the apical end of the apical coil (at protein level). At the base of CC the cultured cochlea, in the more mature hair bundles, CD3 group CC isoforms are restricted to the tips of the shorter stereocilia in both CC inner and outer hair cells. By contrast, at the same stage, isoforms CC belonging to the CD2 group (isoforms 10 through 17) are highly CC expressed in hair bundles in the apex of the cochlea and, at lower CC levels, in those in the middle of the apical coil; they are hardly CC detectable at the base of the cochlea (at protein level). In mature CC hair bundles, CD1 group isoforms are distributed fairly evenly along CC most of the length of the stereocilia on auditory hair cells, whereas CC they are concentrated toward the upper third of the hair bundle in CC vestibular hair cells. In both the auditory and the vestibular organs, CC these isoforms are excluded from a region at the very tip of each CC stereocilium (at protein level). In contrast, CD2 group isoforms are CC undetectable in adult cochlear hair cells (at protein level). These CC isoforms are expressed in the entire hair bundle of the immature cells CC in the sensory epithelium of the early postnatal vestibule and only in CC the kinocilium in the more mature hair bundles (at protein level). CD3 CC group isoforms are detected in immature vestibular hair bundles, CC concentrated toward the tip of each stereocilium, as early as 15.5 dpc. CC They also localize to the tips of the shorter stereocilia in the mature CC vestibular hair bundles and are not detected at the tips of the CC stereocilia in the tallest row (at protein level). CC {ECO:0000269|PubMed:16807332}. CC -!- DOMAIN: Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic CC interaction with CDH23. {ECO:0000269|PubMed:23135401}. CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each CC cadherin domain and rigidify the connections, imparting a strong CC curvature to the full-length ectodomain. {ECO:0000269|PubMed:23135401}. CC -!- DISEASE: Note=Defects in Pcdh15 are the cause of the Ames waltzer (av) CC phenotype. It is characterized by deafness and a balance disorder, CC associated with the degeneration of inner ear neuroepithelia. CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 13]: May be produced at very low levels due to CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 24]: Produced by aberrant splicing sites. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABC79270.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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_006513219.1; XM_006513156.3. [Q99PJ1-26] 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 PDB; 4XXW; X-ray; 2.26 A; A/B=36-259. DR PDB; 5KJ4; X-ray; 3.35 A; A/B/C/D=924-1149. DR PDB; 5TPK; X-ray; 2.00 A; A=715-923. DR PDB; 5W1D; X-ray; 3.35 A; A=401-818. DR PDB; 6BWN; X-ray; 2.94 A; A=615-818. DR PDB; 6C10; X-ray; 1.40 A; A=1144-1381. DR PDB; 6C13; EM; 11.33 A; A/B=821-1465. DR PDB; 6C14; EM; 4.50 A; A/C=1144-1465. DR PDB; 6CV7; X-ray; 1.69 A; A=27-395. DR PDB; 6EET; X-ray; 3.23 A; A=924-1379. DR PDB; 6N22; X-ray; 2.40 A; A=27-265. DR PDBsum; 4APX; -. DR PDBsum; 4AQ8; -. DR PDBsum; 4AQA; -. DR PDBsum; 4AQE; -. DR PDBsum; 4AXW; -. DR PDBsum; 4XXW; -. DR PDBsum; 5KJ4; -. DR PDBsum; 5TPK; -. DR PDBsum; 5W1D; -. DR PDBsum; 6BWN; -. DR PDBsum; 6C10; -. DR PDBsum; 6C13; -. DR PDBsum; 6C14; -. DR PDBsum; 6CV7; -. DR PDBsum; 6EET; -. DR PDBsum; 6N22; -. DR AlphaFoldDB; Q99PJ1; -. DR EMDB; EMD-7327; -. DR EMDB; EMD-7328; -. DR SMR; Q99PJ1; -. DR BioGRID; 198282; 3. DR DIP; DIP-42151N; -. DR IntAct; Q99PJ1; 3. DR MINT; Q99PJ1; -. DR STRING; 10090.ENSMUSP00000141792; -. DR GlyCosmos; Q99PJ1; 13 sites, No reported glycans. DR GlyGen; Q99PJ1; 18 sites. DR iPTMnet; Q99PJ1; -. DR PhosphoSitePlus; Q99PJ1; -. DR PaxDb; 10090-ENSMUSP00000101066; -. DR ProteomicsDB; 288267; -. [Q99PJ1-1] DR ProteomicsDB; 288268; -. [Q99PJ1-2] DR ProteomicsDB; 288269; -. [Q99PJ1-3] DR ProteomicsDB; 288270; -. [Q99PJ1-4] DR ProteomicsDB; 288271; -. [Q99PJ1-5] DR ProteomicsDB; 288272; -. [Q99PJ1-6] DR ProteomicsDB; 288273; -. [Q99PJ1-7] DR ProteomicsDB; 288274; -. [Q99PJ1-8] DR ProteomicsDB; 288275; -. [Q99PJ1-9] DR ProteomicsDB; 288276; -. [Q99PJ1-10] DR ProteomicsDB; 288277; -. [Q99PJ1-11] DR ProteomicsDB; 288278; -. [Q99PJ1-12] DR ProteomicsDB; 288279; -. [Q99PJ1-13] DR ProteomicsDB; 289304; -. [Q99PJ1-14] DR ProteomicsDB; 289305; -. [Q99PJ1-15] DR ProteomicsDB; 289306; -. [Q99PJ1-16] DR ProteomicsDB; 289307; -. [Q99PJ1-17] DR ProteomicsDB; 289308; -. [Q99PJ1-18] DR ProteomicsDB; 289309; -. [Q99PJ1-19] DR ProteomicsDB; 289310; -. [Q99PJ1-20] DR ProteomicsDB; 289311; -. [Q99PJ1-21] DR ProteomicsDB; 289312; -. [Q99PJ1-22] DR ProteomicsDB; 289313; -. [Q99PJ1-23] DR ProteomicsDB; 289314; -. [Q99PJ1-24] DR ProteomicsDB; 289315; -. [Q99PJ1-25] DR ProteomicsDB; 289316; -. [Q99PJ1-26] DR Antibodypedia; 27955; 115 antibodies from 20 providers. DR DNASU; 11994; -. DR Ensembl; ENSMUST00000092420.13; ENSMUSP00000090076.7; ENSMUSG00000052613.17. [Q99PJ1-6] DR Ensembl; ENSMUST00000105424.10; ENSMUSP00000101064.4; ENSMUSG00000052613.17. [Q99PJ1-2] DR Ensembl; ENSMUST00000105426.10; ENSMUSP00000101066.5; ENSMUSG00000052613.17. [Q99PJ1-4] DR Ensembl; ENSMUST00000105429.10; ENSMUSP00000101069.4; ENSMUSG00000052613.17. [Q99PJ1-5] DR Ensembl; ENSMUST00000124046.8; ENSMUSP00000121130.2; ENSMUSG00000052613.17. [Q99PJ1-12] DR Ensembl; ENSMUST00000125006.9; ENSMUSP00000120056.3; ENSMUSG00000052613.17. [Q99PJ1-22] DR Ensembl; ENSMUST00000125055.9; ENSMUSP00000114326.3; ENSMUSG00000052613.17. [Q99PJ1-3] DR Ensembl; ENSMUST00000125517.9; ENSMUSP00000115399.3; ENSMUSG00000052613.17. [Q99PJ1-16] DR Ensembl; ENSMUST00000126920.9; ENSMUSP00000121939.3; ENSMUSG00000052613.17. [Q99PJ1-8] DR Ensembl; ENSMUST00000129404.9; ENSMUSP00000117731.3; ENSMUSG00000052613.17. [Q99PJ1-9] DR Ensembl; ENSMUST00000131321.9; ENSMUSP00000122911.3; ENSMUSG00000052613.17. [Q99PJ1-4] DR Ensembl; ENSMUST00000131724.9; ENSMUSP00000122466.3; ENSMUSG00000052613.17. [Q99PJ1-11] DR Ensembl; ENSMUST00000134009.9; ENSMUSP00000120618.3; ENSMUSG00000052613.17. [Q99PJ1-23] DR Ensembl; ENSMUST00000136096.9; ENSMUSP00000121534.3; ENSMUSG00000052613.17. [Q99PJ1-3] DR Ensembl; ENSMUST00000144302.9; ENSMUSP00000122606.3; ENSMUSG00000052613.17. [Q99PJ1-13] DR Ensembl; ENSMUST00000146682.8; ENSMUSP00000134863.2; ENSMUSG00000052613.17. [Q99PJ1-20] DR Ensembl; ENSMUST00000147189.9; ENSMUSP00000122940.3; ENSMUSG00000052613.17. [Q99PJ1-7] DR Ensembl; ENSMUST00000151116.9; ENSMUSP00000119662.3; ENSMUSG00000052613.17. [Q99PJ1-10] DR Ensembl; ENSMUST00000152655.9; ENSMUSP00000118201.3; ENSMUSG00000052613.17. [Q99PJ1-17] DR Ensembl; ENSMUST00000152819.9; ENSMUSP00000123647.3; ENSMUSG00000052613.17. [Q99PJ1-15] DR Ensembl; ENSMUST00000155701.9; ENSMUSP00000135495.2; ENSMUSG00000052613.17. [Q99PJ1-14] DR Ensembl; ENSMUST00000177107.8; ENSMUSP00000135501.2; ENSMUSG00000052613.17. [Q99PJ1-18] DR Ensembl; ENSMUST00000177420.7; ENSMUSP00000135849.2; ENSMUSG00000052613.17. [Q99PJ1-21] DR Ensembl; ENSMUST00000191709.6; ENSMUSP00000142313.2; ENSMUSG00000052613.17. [Q99PJ1-25] DR Ensembl; ENSMUST00000191854.6; ENSMUSP00000141973.2; ENSMUSG00000052613.17. [Q99PJ1-19] DR Ensembl; ENSMUST00000193361.6; ENSMUSP00000141792.2; ENSMUSG00000052613.17. [Q99PJ1-1] DR Ensembl; ENSMUST00000193739.6; ENSMUSP00000142173.2; ENSMUSG00000052613.17. [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 AGR; MGI:1891428; -. DR CTD; 65217; -. DR MGI; MGI:1891428; Pcdh15. DR VEuPathDB; HostDB:ENSMUSG00000052613; -. DR eggNOG; KOG3594; Eukaryota. DR GeneTree; ENSGT00940000156675; -. DR HOGENOM; CLU_001945_0_0_1; -. DR InParanoid; Q99PJ1; -. DR OrthoDB; 5353563at2759; -. DR PhylomeDB; Q99PJ1; -. DR TreeFam; TF326779; -. DR BioGRID-ORCS; 11994; 3 hits in 76 CRISPR screens. DR ChiTaRS; Pcdh15; mouse. DR PRO; PR:Q99PJ1; -. DR Proteomes; UP000000589; Chromosome 10. DR RNAct; Q99PJ1; Protein. DR Bgee; ENSMUSG00000052613; Expressed in retinal neural layer and 127 other cell types or tissues. DR ExpressionAtlas; Q99PJ1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0016020; C: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-UCL. 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:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI. DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central. 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:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI. DR GO; GO:0048839; P:inner ear development; IMP:MGI. DR GO; GO:0060122; P:inner ear receptor cell 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:1905515; P:non-motile cilium assembly; IMP:MGI. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:MGI. DR GO; GO:0051592; P:response to calcium ion; ISO:MGI. 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 CDD; cd11304; Cadherin_repeat; 9. DR Gene3D; 2.60.40.3430; -; 1. DR Gene3D; 2.60.40.60; Cadherins; 10. DR InterPro; IPR002126; Cadherin-like_dom. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR020894; Cadherin_CS. DR InterPro; IPR041149; EC_dom. DR InterPro; IPR030718; EC_dom_sf. DR PANTHER; PTHR24026:SF126; CADHERIN-89D; 1. DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1. DR Pfam; PF00028; Cadherin; 8. DR Pfam; PF18432; ECD; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 11. DR SUPFAM; SSF49313; Cadherin-like; 10. DR PROSITE; PS00232; CADHERIN_1; 4. DR PROSITE; PS50268; CADHERIN_2; 11. DR Genevisible; Q99PJ1; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane; KW Deafness; Direct protein sequencing; Disulfide bond; Glycoprotein; Hearing; KW Membrane; Reference proteome; Repeat; Secreted; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..1943 FT /note="Protocadherin-15" FT /id="PRO_0000003999" FT TOPO_DOM 27..1381 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1382..1402 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1403..1943 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 45..152 FT /note="Cadherin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 153..270 FT /note="Cadherin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 283..400 FT /note="Cadherin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 401..514 FT /note="Cadherin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 515..621 FT /note="Cadherin 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 622..722 FT /note="Cadherin 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 724..824 FT /note="Cadherin 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 825..931 FT /note="Cadherin 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 932..1040 FT /note="Cadherin 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 1042..1149 FT /note="Cadherin 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 1150..1264 FT /note="Cadherin 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT REGION 1425..1453 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1475..1533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1714..1865 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1430..1451 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1514..1533 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1714..1733 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1745..1784 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1791..1819 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1820..1857 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 57 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 206 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 424 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 564 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 667 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 729 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 773 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 826 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 856 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1069 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1089 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1180 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 37..125 FT /evidence="ECO:0000269|PubMed:23135401" FT VAR_SEQ 1..1252 FT /note="Missing (in isoform 20)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046576" FT VAR_SEQ 1..401 FT /note="Missing (in isoform 12)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046577" FT VAR_SEQ 31..600 FT /note="Missing (in isoform 24)" FT /evidence="ECO:0000303|PubMed:16799054" FT /id="VSP_046578" FT VAR_SEQ 31..57 FT /note="Missing (in isoform 8 and isoform 9)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046579" FT VAR_SEQ 31..35 FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform FT 5, isoform 6, isoform 7, isoform 11, isoform 13, isoform FT 14, isoform 15, isoform 16, isoform 17, isoform 19, isoform FT 22 and isoform 23)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046580" FT VAR_SEQ 204..240 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046581" FT VAR_SEQ 298..331 FT /note="EELNPILVTPPIQAIDQDRNIQPPSDRPGILYSI -> DFGSLRSGANSWCQ FT GCGGVHRCPSPWRRLLPRRL (in isoform 13)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046582" FT VAR_SEQ 332..1943 FT /note="Missing (in isoform 13)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046583" FT VAR_SEQ 335..339 FT /note="TPEDY -> RARES (in isoform 14)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046584" FT VAR_SEQ 340..1943 FT /note="Missing (in isoform 14)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046585" FT VAR_SEQ 372..655 FT /note="AEQDNGHPLPAFASLHIEILDENNQSPYFTMPSYQGYILESAPVGATISESL FT NLTTPLRIVALDKDIEDTKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQTY FT TFLITAFDGVQESEPVVVNIRVMDANDNTPTFPEISYDVYVYTDMSPGDSVIQLTAVDA FT DEGSNGEISYEILVGGKGDFVINKTTGLVSIAPGVELIVGQTYALTVQASDNAPPAERR FT HSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAILLNLQATDREGDPITY -> FT VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVRGLAEKRG FT IDLEGEEWRRRLDEEDKDYLQLTLDQEEATESTVESEEESSDYTEYTETESEFSESETT FT EESESETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKREEP FT PVEEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVPEEGSAESVSMERGVESEESE FT SELSSSSSTSESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL (in FT isoform 15)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046587" FT VAR_SEQ 440 FT /note="D -> DVPPGGVP (in isoform 10 and isoform 12)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046588" FT VAR_SEQ 441..961 FT /note="Missing (in isoform 23)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046589" FT VAR_SEQ 441..725 FT /note="TKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQTYTFLITAFDGV FT QESEPVVVNIRVMDANDNTPTFPEISYDVYVYTDMSPGDSVIQLTAVDADEGSNGEISY FT EILVGGKGDFVINKTTGLVSIAPGVELIVGQTYALTVQASDNAPPAERRHSICTVYIEV FT LPPNNQSPPRFPQLMYSLEVSEAMRIGAILLNLQATDREGDPITYAIENGDPQRVFNLS FT ETTGILSLGKALDRESTDRYILIVTASDGRPDGTSTATVNIVVTDVNDNAPVFDPY -> FT VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVRGLAEKRG FT IDLEGEEWRRRLDEEDKDYLQLTLDQEEATESTVESEEESSDYTEYTETESEFSESETT FT EESESETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKREEP FT PVEEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVPEEGSAESVSMERGVESEESE FT SELSSSSSTSESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL (in FT isoform 16)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046590" FT VAR_SEQ 600..671 FT /note="RHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAILLNLQATDREGD FT PITYAIENGDPQRVFNLSET -> S (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046591" FT VAR_SEQ 645..689 FT /note="ATDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDRESTDRY -> HRD FT SQPREGSRPREHRPLHPHRHSLRWQTGWNLNCHCEHSGDGRQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046592" FT VAR_SEQ 656..1943 FT /note="Missing (in isoform 15)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046593" FT VAR_SEQ 690..1943 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046594" FT VAR_SEQ 703..986 FT /note="TSTATVNIVVTDVNDNAPVFDPYLPRNLSVVEEEANAFVGQVRATDPDAGIN FT GQVHYSLGNFNNLFRITSNGSIYTAVKLNREARDHYELVVVATDGAVHPRHSTLTLYIK FT VLDIDDNSPVFTNSTYTVVVEENLPAGTSFLQIEAKDVDLGANVSYRIRSPEVKHLFAL FT HPFTGELSLLRSLDYEAFPDQEASITFLVEAFDIYGTMPPGIATVTVIVKDMNDYPPVF FT SKRIYKGMVAPDAVKGTPITTVYAEDADPPGMPASRVRYRVDDVQFPYPASIFDV -> FT VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVRGLAEKRG FT IDLEGEEWRRRLDEEDKDYLQLTLDQEEATESTVESEEESSDYTEYTETESEFSESETT FT EESESETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKREEP FT PVEEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVPEEGSAESVSMERGVESEESE FT SELSSSSSTSESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL (in FT isoform 17)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046595" FT VAR_SEQ 726..1943 FT /note="Missing (in isoform 16)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046596" FT VAR_SEQ 987..1943 FT /note="Missing (in isoform 17)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046597" FT VAR_SEQ 1131..1176 FT /note="NTAKVYIEIQDENDHPPVFQKKFYIGGVSEDARMFASVLRVKATDR -> LS FT VIPCSWRTQVSKSLGLELGVPVSHSVESGTRTGSSTRAASVPIH (in isoform FT 21, isoform 22 and isoform 23)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:16807332" FT /id="VSP_046598" FT VAR_SEQ 1177..1943 FT /note="Missing (in isoform 21, isoform 22 and isoform 23)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:16807332" FT /id="VSP_046599" FT VAR_SEQ 1407..1667 FT /note="FKVRQAECTKTARIQSAMPAAKPAAPVPAAPAPPPPPPPPPPGAHLYEELGE FT SAMHNLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLKESQPNPA FT RTFSFVPDEDNLSTHNPLYMESIGQRSTNSDLQPRTDFEELLAPRTQVKSQSLRGPREK FT IQRVWNQSVSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQRGSSNVLLAT FT EDAHESEKEGGHRDTLIVQQTEQLKSLSSGSS -> GGFAPEHQLLRPSLLKPEELSME FT SGIDPGQEYGQDYYSYEHGYEMPQYGSRRRLLPPAGQEEYGEVIGEAEEEYEEEEWARK FT RMIKLVVDREYESSSPGEDSAPESQRSRTHKPSGRSNVNGNIYIAQNGSVVRTRRACVA FT DNLKVPSPGLLGRHLKKLDTLAGTREENVPLNTLFKGPFSTEKAKRTPTLVTFAPCPVV FT AEHSAVKPSGTRLKHTAEQESMVDSRLSRESMEFHGDSAPSDEEELWMGPWNSLHIPMT FT KL (in isoform 20)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046600" FT VAR_SEQ 1407..1409 FT /note="Missing (in isoform 6, isoform 7, isoform 9 and FT isoform 26)" FT /evidence="ECO:0000303|PubMed:16807332, FT ECO:0000303|PubMed:21436032" FT /id="VSP_046601" FT VAR_SEQ 1461..1463 FT /note="MHN -> I (in isoform 4, isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046602" FT VAR_SEQ 1462..1943 FT /note="HNLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLKESQ FT PNPARTFSFVPDEDNLSTHNPLYMESIGQRSTNSDLQPRTDFEELLAPRTQVKSQSLRG FT PREKIQRVWNQSVSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQRGSSNV FT LLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGSSFSSSWSHFSFSTLPTISRAVELG FT SEPNVVTSPADCTLELSPPLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSISA FT PLPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPISTPPTSSLPLPPPLSLPPPPR FT PPAPRLFPQPPSTSIPSTDSISAPAAKCTASATHARETTSTTQPPASNPQWGAEPHRHP FT KGILRHVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKTGMKITHDQSQETLV FT RVVEGIDVQPHSQSTSL -> YEMPQYGSRRRLLPPAGQEEYGEVIGEAEEEYEEEEVE FT PEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVRGLAEKRGID FT LEGEEWRRRLDEEDKDYLQLTLDQEEATESTVESEEESSDYTEYTETESEFSESETTEE FT SESETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKREEPPV FT EEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVPEEGSAESVSMERGVESEESESE FT LSSSSSTSESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL (in isoform FT 25)" FT /evidence="ECO:0000303|PubMed:21436032" FT /id="VSP_046603" FT VAR_SEQ 1462..1943 FT /note="HNLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLKESQ FT PNPARTFSFVPDEDNLSTHNPLYMESIGQRSTNSDLQPRTDFEELLAPRTQVKSQSLRG FT PREKIQRVWNQSVSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQRGSSNV FT LLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGSSFSSSWSHFSFSTLPTISRAVELG FT SEPNVVTSPADCTLELSPPLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSISA FT PLPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPISTPPTSSLPLPPPLSLPPPPR FT PPAPRLFPQPPSTSIPSTDSISAPAAKCTASATHARETTSTTQPPASNPQWGAEPHRHP FT KGILRHVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKTGMKITHDQSQETLV FT RVVEGIDVQPHSQSTSL -> YEMPQYGSRRRLLPPAGQEEYGEVIGEAEEEYEEEEWA FT RKRMIKLVVDREYESSSPGEDSAPESQRSRTHKPSGRSNVNGNIYIAQNGSVVRTRRAC FT VADNLKVPSPGLLGRHLKKLDTLAGTREENVPLNTLFKGPFSTEKAKRTPTLVTFAPCP FT VVAEHSAVKPSGTRLKHTAEQESMVDSRLSRESMEFHGDSAPSDEEELWMGPWNSLHIP FT MTKL (in isoform 26)" FT /evidence="ECO:0000303|PubMed:21436032" FT /id="VSP_046604" FT VAR_SEQ 1463..1943 FT /note="NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLKESQP FT NPARTFSFVPDEDNLSTHNPLYMESIGQRSTNSDLQPRTDFEELLAPRTQVKSQSLRGP FT REKIQRVWNQSVSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQRGSSNVL FT LATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGSSFSSSWSHFSFSTLPTISRAVELGS FT EPNVVTSPADCTLELSPPLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSISAP FT LPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPISTPPTSSLPLPPPLSLPPPPRP FT PAPRLFPQPPSTSIPSTDSISAPAAKCTASATHARETTSTTQPPASNPQWGAEPHRHPK FT GILRHVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKTGMKITHDQSQETLVR FT VVEGIDVQPHSQSTSL -> KYEMPQYGSRRRLLPPAGQEEYGEVIGEAEEEYEEEEVE FT PEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVRGLAEKRGID FT LEGEEWRRRLDEEDKDYLQLTLDQEEATESTVESEEESSDYTEYTETESEFSESETTEE FT SESETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKREEPPV FT EEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVPEEGSAESVSMERGVESEESESE FT LSSSSSTSESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL (in isoform FT 10)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046605" FT VAR_SEQ 1463..1682 FT /note="NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLKESQP FT NPARTFSFVPDEDNLSTHNPLYMESIGQRSTNSDLQPRTDFEELLAPRTQVKSQSLRGP FT REKIQRVWNQSVSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQRGSSNVL FT LATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGSSFSSSWSHFSFSTLPT -> KYEMP FT QYGSRRRLLPPAGQEEYGEVIGEAEEEYEEEEWARKRMIKLVVDREYESSSPGEDSAPE FT SQRSRTHKPSGRSNVNGNIYIAQNGSVVRTRRACVADNLKVPSPGLLGRHLKKLDTLAG FT TREENVPLNTLFKGPFSTEKAKRTPTLVTFAPCPVVAEHSAVKPSGTRLKHTAEQESMV FT DSRLSRESMEFHGDSAPSDEEELWMGPWNSLHIPMTKL (in isoform 18 and FT isoform 19)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046606" FT VAR_SEQ 1463..1523 FT /note="NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLKESQP FT NPARTFSFV -> KSYPWNLGLILARNMDKIITVMSMGMRCPSMEVAVDCCHLLDRRNT FT AKSLVKLKRNMKKKR (in isoform 11 and isoform 12)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046607" FT VAR_SEQ 1464..1473 FT /note="Missing (in isoform 24)" FT /evidence="ECO:0000303|PubMed:16799054" FT /id="VSP_046608" FT VAR_SEQ 1524..1943 FT /note="Missing (in isoform 11 and isoform 12)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046609" FT VAR_SEQ 1668..1943 FT /note="Missing (in isoform 20)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046610" FT VAR_SEQ 1683..1943 FT /note="Missing (in isoform 18 and isoform 19)" FT /evidence="ECO:0000303|PubMed:16807332" FT /id="VSP_046611" FT MUTAGEN 48 FT /note="I->A: Strongly reduced interaction with CDH23." FT /evidence="ECO:0000269|PubMed:23135401" FT MUTAGEN 139 FT /note="R->G: Impaired interaction with CDH23." FT /evidence="ECO:0000269|PubMed:23135401" FT CONFLICT 608 FT /note="I -> T (in Ref. 1; AAG53891, 2; AAY24693 and 3; FT ABC79259/ABC79260/ABC79261/ABC79262/ABC79264/ABC79265/ABC79266/ABC79267/ABC79268/ABC79269/ABC79270/ABC79276/ABC79277)" FT /evidence="ECO:0000305" FT CONFLICT 901 FT /note="V -> A (in Ref. 1; AAG53891, 2; AAY24693 and 3; FT ABC79259/ABC79261/ABC79263/ABC79264/ABC79265/ABC79266/ABC79267/ABC79268/ABC79269/ABC79270/ABC79276/ABC79277)" FT /evidence="ECO:0000305" FT CONFLICT 1748 FT /note="S -> F (in Ref. 1; AAG53891, 2; AAY24693 and 3; FT ABC79259/ABC79261/ABC79263/ABC79264/ABC79265/ABC79266/ABC79267)" FT /evidence="ECO:0000305" FT CONFLICT 1848 FT /note="S -> F (in Ref. 1; AAG53891, 2; AAY24693 and 3; FT ABC79259/ABC79261/ABC79263/ABC79264/ABC79265/ABC79266/ABC79267)" FT /evidence="ECO:0000305" FT CONFLICT 1859 FT /note="W -> G (in Ref. 4; BAE24546)" FT /evidence="ECO:0000305" FT TURN 27..30 FT /evidence="ECO:0007829|PDB:4APX" FT HELIX 31..34 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 77..84 FT /evidence="ECO:0007829|PDB:4APX" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:4APX" FT TURN 94..97 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:4APX" FT TURN 112..114 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 118..127 FT /evidence="ECO:0007829|PDB:4APX" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 133..143 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 151..155 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 157..162 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:4APX" FT TURN 174..179 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:4AQ8" FT HELIX 187..190 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:4APX" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:4APX" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:4APX" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 232..241 FT /evidence="ECO:0007829|PDB:4APX" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 251..259 FT /evidence="ECO:0007829|PDB:4APX" FT STRAND 268..275 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 286..292 FT /evidence="ECO:0007829|PDB:6CV7" FT HELIX 297..300 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 310..314 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:6CV7" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 327..336 FT /evidence="ECO:0007829|PDB:6CV7" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:6CV7" FT TURN 347..349 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 352..356 FT /evidence="ECO:0007829|PDB:6CV7" FT TURN 360..362 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 365..377 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 382..391 FT /evidence="ECO:0007829|PDB:6CV7" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 408..410 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 420..422 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 447..452 FT /evidence="ECO:0007829|PDB:5W1D" FT TURN 454..456 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 457..459 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 461..466 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 468..472 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 483..489 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 498..501 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 517..524 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 532..535 FT /evidence="ECO:0007829|PDB:5W1D" FT TURN 544..547 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 549..557 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 560..563 FT /evidence="ECO:0007829|PDB:5W1D" FT TURN 565..567 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 569..572 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 583..592 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 601..611 FT /evidence="ECO:0007829|PDB:5W1D" FT HELIX 613..615 FT /evidence="ECO:0007829|PDB:5W1D" FT STRAND 626..631 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 639..642 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 654..660 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 666..668 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 670..672 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 674..677 FT /evidence="ECO:0007829|PDB:6BWN" FT TURN 683..685 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 688..696 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 703..713 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 724..726 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 728..735 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 740..743 FT /evidence="ECO:0007829|PDB:5TPK" FT HELIX 752..755 FT /evidence="ECO:0007829|PDB:6BWN" FT STRAND 757..763 FT /evidence="ECO:0007829|PDB:5TPK" FT TURN 765..767 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 768..770 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 774..780 FT /evidence="ECO:0007829|PDB:5TPK" FT TURN 784..786 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 789..798 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 800..802 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 805..815 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 823..825 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 827..834 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 842..845 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 857..861 FT /evidence="ECO:0007829|PDB:5TPK" FT HELIX 864..866 FT /evidence="ECO:0007829|PDB:5TPK" FT TURN 867..869 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 870..872 FT /evidence="ECO:0007829|PDB:5TPK" FT TURN 874..876 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 878..883 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 896..905 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 913..922 FT /evidence="ECO:0007829|PDB:5TPK" FT STRAND 930..932 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 934..940 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 949..952 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 955..957 FT /evidence="ECO:0007829|PDB:5KJ4" FT STRAND 961..963 FT /evidence="ECO:0007829|PDB:6EET" FT HELIX 964..966 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 969..973 FT /evidence="ECO:0007829|PDB:6EET" FT HELIX 978..983 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 984..986 FT /evidence="ECO:0007829|PDB:6EET" FT TURN 988..990 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 992..997 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1006..1014 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1017..1019 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1022..1031 FT /evidence="ECO:0007829|PDB:6EET" FT HELIX 1034..1036 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1039..1041 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1043..1045 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1059..1062 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1072..1079 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1085..1088 FT /evidence="ECO:0007829|PDB:6EET" FT TURN 1089..1092 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1093..1096 FT /evidence="ECO:0007829|PDB:6EET" FT TURN 1102..1104 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1106..1116 FT /evidence="ECO:0007829|PDB:6EET" FT HELIX 1117..1122 FT /evidence="ECO:0007829|PDB:6EET" FT TURN 1129..1131 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1132..1140 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1147..1150 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1152..1159 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1167..1170 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1173..1175 FT /evidence="ECO:0007829|PDB:6C10" FT TURN 1176..1178 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1179..1182 FT /evidence="ECO:0007829|PDB:6EET" FT STRAND 1185..1189 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1194..1196 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1200..1202 FT /evidence="ECO:0007829|PDB:6C10" FT TURN 1204..1206 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1208..1211 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1222..1230 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1232..1234 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1238..1248 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1250..1252 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1254..1260 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1262..1267 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1269..1283 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1288..1300 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1301..1303 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1305..1318 FT /evidence="ECO:0007829|PDB:6C10" FT TURN 1320..1322 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1323..1325 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1328..1336 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1339..1350 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1356..1360 FT /evidence="ECO:0007829|PDB:6C10" FT HELIX 1363..1370 FT /evidence="ECO:0007829|PDB:6C10" FT STRAND 1374..1376 FT /evidence="ECO:0007829|PDB:6C10" 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 //