PCD15_MOUSE
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 03-AUG-2022, entry version 171.
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};
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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 SMR; Q99PJ1; -.
DR BioGRID; 198282; 3.
DR DIP; DIP-42151N; -.
DR IntAct; Q99PJ1; 3.
DR MINT; Q99PJ1; -.
DR STRING; 10090.ENSMUSP00000101066; -.
DR GlyGen; Q99PJ1; 18 sites.
DR iPTMnet; Q99PJ1; -.
DR PhosphoSitePlus; Q99PJ1; -.
DR PaxDb; Q99PJ1; -.
DR PRIDE; Q99PJ1; -.
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; 99 antibodies from 20 providers.
DR DNASU; 11994; -.
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 VEuPathDB; HostDB:ENSMUSG00000052613; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000156675; -.
DR HOGENOM; CLU_001945_0_0_1; -.
DR InParanoid; Q99PJ1; -.
DR OrthoDB; 21247at2759; -.
DR PhylomeDB; Q99PJ1; -.
DR TreeFam; TF326779; -.
DR BioGRID-ORCS; 11994; 3 hits in 71 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 125 other tissues.
DR ExpressionAtlas; Q99PJ1; baseline and differential.
DR Genevisible; Q99PJ1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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 InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR041149; EC_dom.
DR InterPro; IPR030718; Protocadherin-15.
DR PANTHER; PTHR24028:SF11; PTHR24028:SF11; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF18432; ECD; 1.
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; 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/
FT ABC79266/ABC79267/ABC79268/ABC79269/ABC79270/ABC79276/
FT 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/
FT 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/
FT 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/
FT 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
