CAD23_MOUSE
ID CAD23_MOUSE Reviewed; 3354 AA.
AC Q99PF4; E9QP63; Q5QGS3; Q5QGS4; Q5QGS7; Q5QGS8; Q99NH1; Q9D4N9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cadherin-23;
DE AltName: Full=Otocadherin;
DE Flags: Precursor;
GN Name=Cdh23;
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], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=C57BL/6J;
RX PubMed=11138008; DOI=10.1038/83660;
RA Di Palma F., Holme R.H., Bryda E.C., Belyantseva I.A., Pellegrino R.,
RA Kachar B., Steel K.P., Noben-Trauth K.;
RT "Mutations in Cdh23, encoding a new type of cadherin, cause stereocilia
RT disorganization in waltzer, the mouse model for Usher syndrome type 1D.";
RL Nat. Genet. 27:103-107(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11386759; DOI=10.1006/geno.2001.6554;
RA Wilson S.M., Householder D.B., Coppola V., Tessarollo L., Fritzsch B.,
RA Lee E.-C., Goss D., Carlson G.A., Copeland N.G., Jenkins N.A.;
RT "Mutations in Cdh23 cause nonsyndromic hearing loss in waltzer mice.";
RL Genomics 74:228-233(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORMS B1; B2; C1 AND C2).
RC STRAIN=C57BL/6J;
RX PubMed=15882574; DOI=10.1016/j.ydbio.2005.01.015;
RA Lagziel A., Ahmed Z.M., Schultz J.M., Morell R.J., Belyantseva I.A.,
RA Friedman T.B.;
RT "Spatiotemporal pattern and isoforms of cadherin 23 in wild type and
RT waltzer mice during inner ear hair cell development.";
RL Dev. Biol. 280:295-306(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 GENOMIC ORGANIZATION, ALTERNATIVE SPLICING, VARIANT WALTZER
RP 2718-ASN--PRO-2720 DEL, AND VARIANTS PRO-5; VAL-229; LYS-891; ILE-1137;
RP ARG-1236; VAL-2025; VAL-2026; THR-2217; HIS-2222; ARG-2270 AND ALA-2617.
RC STRAIN=C57BL/6J, and CAST/EiJ;
RX PubMed=11750125; DOI=10.1016/s0378-1119(01)00761-2;
RA Di Palma F., Pellegrino R., Noben-Trauth K.;
RT "Genomic structure, alternative splice forms and normal and mutant alleles
RT of cadherin 23 (Cdh23).";
RL Gene 281:31-41(2001).
RN [7]
RP INTERACTION WITH PCDH15.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH CAMSAP3.
RX PubMed=27349180; DOI=10.1038/srep28706;
RA Takahashi S., Mui V.J., Rosenberg S.K., Homma K., Cheatham M.A., Zheng J.;
RT "Cadherin 23-C regulates microtubule networks by modifying CAMSAP3's
RT function.";
RL Sci. Rep. 6:28706-28706(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 24-228 IN COMPLEX WITH CALCIUM.
RX PubMed=20399731; DOI=10.1016/j.neuron.2010.03.028;
RA Sotomayor M., Weihofen W.A., Gaudet R., Corey D.P.;
RT "Structural determinants of cadherin-23 function in hearing and deafness.";
RL Neuron 66:85-100(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 24-233 IN COMPLEX WITH CALCIUM,
RP MUTAGENESIS OF ASN-26 AND ARG-27, AND INTERACTION WITH PCDH15.
RX PubMed=20498078; DOI=10.1073/pnas.1006284107;
RA Elledge H.M., Kazmierczak P., Clark P., Joseph J.S., Kolatkar A., Kuhn P.,
RA Muller U.;
RT "Structure of the N terminus of cadherin 23 reveals a new adhesion
RT mechanism for a subset of cadherin superfamily members.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10708-10712(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 24-228 IN COMPLEX WITH CALCIUM
RP IONS AND PCDH15, SUBUNIT, AND MUTAGENESIS OF LEU-168.
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: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells. CDH23 is required for establishing and/or maintaining
CC the proper organization of the stereocilia bundle of hair cells in the
CC cochlea and the vestibule during late embryonic/early postnatal
CC development. It is part of the functional network formed by USH1C,
CC USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear
CC hair cells. Required for normal hearing. {ECO:0000269|PubMed:11138008}.
CC -!- SUBUNIT: Interacts with USH1C and USH1G (By similarity). antiparallel
CC heterodimer with PCDH15. Isoform C1: Interacts with CAMSAP3; leading to
CC inhibit CAMSAP3 ability to induce microtubule bundle formation
CC (PubMed:27349180). {ECO:0000250|UniProtKB:Q9H251,
CC ECO:0000269|PubMed:17805295, ECO:0000269|PubMed:20399731,
CC ECO:0000269|PubMed:20498078, ECO:0000269|PubMed:23135401,
CC ECO:0000269|PubMed:27349180}.
CC -!- INTERACTION:
CC Q99PF4; Q9ES64-3: Ush1c; NbExp=2; IntAct=EBI-7419021, EBI-7418919;
CC Q99PF4-1; Q99PJ1: Pcdh15; NbExp=10; IntAct=EBI-15656347, EBI-6556746;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q99PF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99PF4-2; Sequence=VSP_000648;
CC Name=C1;
CC IsoId=Q99PF4-3; Sequence=VSP_059242, VSP_059244;
CC Name=B2;
CC IsoId=Q99PF4-4; Sequence=VSP_059243, VSP_000648;
CC Name=B1;
CC IsoId=Q99PF4-5; Sequence=VSP_059243;
CC Name=C2;
CC IsoId=Q99PF4-6; Sequence=VSP_059242, VSP_000648;
CC -!- TISSUE SPECIFICITY: In adult animals relatively high levels of
CC expression are found in testis, skeletal muscle, heart, eye and thymus,
CC and lower expression in kidney, lung and brain. Found in the sensory
CC hair cells of the inner ear. {ECO:0000269|PubMed:11138008}.
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.
CC {ECO:0000250|UniProtKB:P12830}.
CC -!- DOMAIN: Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic
CC interaction with PCDH15. {ECO:0000269|PubMed:23135401}.
CC -!- DISEASE: Note=Defects in Cdh23 are the cause of waltzer (v) phenotype.
CC Waltzer mice are characterized by deafness and vestibular dysfunction
CC due to degeneration of the neuroepithelium within the inner ear.
CC {ECO:0000269|PubMed:11138008, ECO:0000269|PubMed:11750125}.
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; AF308939; AAG52817.1; -; mRNA.
DR EMBL; AY026062; AAK07670.1; -; mRNA.
DR EMBL; AY563159; AAT72159.1; -; mRNA.
DR EMBL; AY563160; AAT72160.1; -; mRNA.
DR EMBL; AY563163; AAT72163.1; -; mRNA.
DR EMBL; AY563164; AAT72164.1; -; mRNA.
DR EMBL; AK016365; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC079082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_075859.2; NM_023370.3.
DR RefSeq; XP_006513665.1; XM_006513602.2.
DR RefSeq; XP_017169418.1; XM_017313929.1.
DR PDB; 2WBX; X-ray; 1.50 A; A=24-124.
DR PDB; 2WCP; X-ray; 1.98 A; A=24-228.
DR PDB; 2WD0; X-ray; 2.74 A; A/C=24-228.
DR PDB; 2WHV; X-ray; 2.36 A; A=24-228.
DR PDB; 3MVS; X-ray; 1.10 A; A=24-233.
DR PDB; 4APX; X-ray; 1.65 A; A=24-228.
DR PDB; 4AQ8; X-ray; 2.63 A; A/B=24-228.
DR PDB; 4AQA; X-ray; 1.96 A; A=24-228.
DR PDB; 4AQE; X-ray; 2.27 A; A=24-228.
DR PDB; 4AXW; X-ray; 2.23 A; A=24-228.
DR PDB; 4XXW; X-ray; 2.26 A; C/D=24-228.
DR PDB; 5I8D; X-ray; 2.69 A; A=1949-2289.
DR PDB; 5TFK; X-ray; 2.80 A; A=1949-2289.
DR PDB; 5TFL; X-ray; 3.56 A; A/B=666-886.
DR PDB; 5ULU; X-ray; 2.85 A; A=1955-2289.
DR PDB; 5UN2; X-ray; 2.96 A; A=1955-2289.
DR PDB; 5UZ8; X-ray; 1.85 A; A=2288-2607.
DR PDB; 5VH2; X-ray; 2.84 A; A/B/C/D=1201-1412.
DR PDB; 5VT8; X-ray; 2.92 A; A/B/C/D=2504-2715.
DR PDB; 5WJM; X-ray; 2.90 A; A=1739-1954.
DR PDB; 6N2E; X-ray; 2.90 A; C/D=24-228.
DR PDBsum; 2WBX; -.
DR PDBsum; 2WCP; -.
DR PDBsum; 2WD0; -.
DR PDBsum; 2WHV; -.
DR PDBsum; 3MVS; -.
DR PDBsum; 4APX; -.
DR PDBsum; 4AQ8; -.
DR PDBsum; 4AQA; -.
DR PDBsum; 4AQE; -.
DR PDBsum; 4AXW; -.
DR PDBsum; 4XXW; -.
DR PDBsum; 5I8D; -.
DR PDBsum; 5TFK; -.
DR PDBsum; 5TFL; -.
DR PDBsum; 5ULU; -.
DR PDBsum; 5UN2; -.
DR PDBsum; 5UZ8; -.
DR PDBsum; 5VH2; -.
DR PDBsum; 5VT8; -.
DR PDBsum; 5WJM; -.
DR PDBsum; 6N2E; -.
DR SMR; Q99PF4; -.
DR BioGRID; 204475; 3.
DR CORUM; Q99PF4; -.
DR DIP; DIP-42152N; -.
DR IntAct; Q99PF4; 3.
DR MINT; Q99PF4; -.
DR STRING; 10090.ENSMUSP00000101101; -.
DR GlyGen; Q99PF4; 42 sites.
DR iPTMnet; Q99PF4; -.
DR PhosphoSitePlus; Q99PF4; -.
DR jPOST; Q99PF4; -.
DR PaxDb; Q99PF4; -.
DR PRIDE; Q99PF4; -.
DR ProteomicsDB; 273572; -. [Q99PF4-1]
DR ProteomicsDB; 273573; -. [Q99PF4-2]
DR ProteomicsDB; 273574; -. [Q99PF4-3]
DR ProteomicsDB; 273575; -. [Q99PF4-4]
DR ProteomicsDB; 273576; -. [Q99PF4-5]
DR ProteomicsDB; 273577; -. [Q99PF4-6]
DR ABCD; Q99PF4; 1 sequenced antibody.
DR Antibodypedia; 2330; 277 antibodies from 35 providers.
DR DNASU; 22295; -.
DR Ensembl; ENSMUST00000105461; ENSMUSP00000101101; ENSMUSG00000012819. [Q99PF4-1]
DR Ensembl; ENSMUST00000105463; ENSMUSP00000101103; ENSMUSG00000012819. [Q99PF4-2]
DR GeneID; 22295; -.
DR KEGG; mmu:22295; -.
DR UCSC; uc033fpl.1; mouse. [Q99PF4-1]
DR CTD; 64072; -.
DR MGI; MGI:1890219; Cdh23.
DR VEuPathDB; HostDB:ENSMUSG00000012819; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155245; -.
DR InParanoid; Q99PF4; -.
DR OMA; ATDQCPK; -.
DR OrthoDB; 17702at2759; -.
DR PhylomeDB; Q99PF4; -.
DR TreeFam; TF316403; -.
DR BioGRID-ORCS; 22295; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Cdh23; mouse.
DR EvolutionaryTrace; Q99PF4; -.
DR PRO; PR:Q99PF4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99PF4; protein.
DR Bgee; ENSMUSG00000012819; Expressed in spermatid and 63 other tissues.
DR ExpressionAtlas; Q99PF4; baseline and differential.
DR Genevisible; Q99PF4; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0098683; C:cochlear hair cell ribbon synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0060091; C:kinocilium; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032420; C:stereocilium; IDA:HGNC-UCL.
DR GO; GO:0032426; C:stereocilium tip; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:MGI.
DR GO; GO:0007155; P:cell adhesion; TAS:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
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:0042472; P:inner ear morphogenesis; 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:0045494; P:photoreceptor cell maintenance; ISO:MGI.
DR GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IMP:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR033030; CDH23.
DR PANTHER; PTHR24025:SF18; PTHR24025:SF18; 1.
DR Pfam; PF00028; Cadherin; 25.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 26.
DR SUPFAM; SSF49313; SSF49313; 27.
DR PROSITE; PS00232; CADHERIN_1; 17.
DR PROSITE; PS50268; CADHERIN_2; 27.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Deafness; Disease variant; Glycoprotein; Hearing; Membrane; Metal-binding;
KW Non-syndromic deafness; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..3354
FT /note="Cadherin-23"
FT /id="PRO_0000003825"
FT TOPO_DOM 24..3064
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3065..3085
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3086..3354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 133..236
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 237..348
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 349..460
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 461..561
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 562..671
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 672..784
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 779..890
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 891..995
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 996..1102
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1103..1208
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1210..1313
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1314..1418
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1420..1527
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1529..1634
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1635..1744
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1745..1851
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1852..1959
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1960..2069
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2070..2174
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2175..2293
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2297..2402
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2403..2509
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2510..2611
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2614..2722
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2729..2846
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2847..2975
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 155
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 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1001
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1018
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2014
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2896
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..3128
FT /note="MRYSLVTCYAVLWLLMLVPGSWGQVNRLPFFTNHFFDTYLLISEDTPVGSSV
FT TQLLARDMDNDPLVFGVSGEEASRFFAVEPDTGVVWLRQPLDRETKSEFTVEFSVSDHQ
FT GVITRKVNIQVGDVNDNAPTFHNQPYSVRIPENTPVGTPIFIVNATDPDLGAGGSVLYS
FT FQPPSPFFAIDSARGIVTVIQELDYEVTQAYQLTVNATDQDKTRPLSTLANLAIIITDM
FT QDMDPIFINLPYSTNIYEHSPPGTTVRVITAVDQDKGRPRGIGYTIVSGNTNSIFALDY
FT ISGALTLNGLLDRENPLYSHGFILTVKGTELNDDRTPSDATVTTTFNILVIDINDNAPE
FT FNSSEYSVAITELAQVGFALPLFIQVVDKDEDLGLNSMFEVYLVGNNSHHFIISPTSVQ
FT GKADIRIRVAIPLDYETVDRYDFDLFANESVPDHVGYAKVKITLINENDNRPIFSQPLY
FT NVSLYENITVGTSVLTVLATDNDVGTFGEVNYFFSDDPDRFSLDKDTGLIMLIARLDYE
FT LIQRFTLTVIARDGGGEETTGRVRINVLDVNDNVPTFQKDAYVGALRENEPSVTQLVRL
FT RATDEDSPPNNLITYSIVNASAFGSYFDISIYEGYGVISVSRPLDYEQIPNGLIYLTVM
FT AKDAGNPPLYSTVPVTIEVFDENDNPPTFSKPAYFVSVLENIMAGATVLFLNATDLDRS
FT REYGQESIIYSLEGSSQFRINARSGEITTTSLLDRETKSEYILIVRAVDGGVGHNQKTG
FT IATVNVTLLDINDNHPTWKDAPYYINLVEMTPPDSDVTTVVAVDPDLGENGTLVYSIHP
FT PNKFYSLNSTTGKIRTTHVMLDRENPDPVEAELMRKIIVSVTDCGRPPLKATSSATVFV
FT NLLDLNDNDPTFRNLPFVAEILEGTPAGVSVYQVVAIDLDEGLNGLVSYRMQVGMPRMD
FT FVINSTSGVVTTTAELDRERIAEYQLRVVASDAGTPTKSSTSTLTVRVLDVNDETPTFF
FT PAVYNVSVSEDVPREFRVVWLNCTDNDVGLNAELSYFITAGNVDGKFSVGYRDAVVRTV
FT VGLDRETTAAYTLVLEAIDNGPVGKRRTGTATVFVTVLDVNDNRPIFLQSSYEASVPED
FT IPEGHSIVQLKATDADEGEFGRVWYRILHGNHGNNFRIHVGSGLLMRGPRPLDRERNSS
FT HVLMVEAYNHDLGPMRSSVRVIVYVEDVNDEAPVFTQQQYNRLGLRETAGIGTSVIVVR
FT ATDKDTGDGGLVNYRILSGAEGKFEIDESTGLIVTVDYLDYETKTSYLMNVSATDGAPP
FT FNQGFCSVYVTLLNELDEAVQFSNASYEAVIMENLALGTEIVRVQAYSIDNLNQITYRF
FT DAYTSAQAKALFKIDAITGVITVKGLVDREKGDFYTLTVVADDGGPKVDSTVKVYITVL
FT DENDNSPRFDFTSDSAISVPEDCPVGQRVATVKARDPDAGSNGQVVFSLASGNIAGAFE
FT IITSNDSIGEVFVAKPLDREELDHYILKVVASDRGTPPRKKDHILQVTILDVNDNPPVI
FT ESPFGYNVSVNENVGGGTSVVQVRATDRDIGINSVLSYYITEGNEDMTFRMDRISGEIA
FT TRPAPPDRERQNFYHLVVTVEDEGTPTLSATTHVYVTIVDENDNAPVFQQPHYEVVLDE
FT GPDTINTSLITVQALDLDEGPNGTVTYAIVAGNIINTFRINKHTGVITAAKELDYEISH
FT GRYTLIVTATDQCPILSHRLTSTTTVLVNVNDINDNVPTFPRDYEGPFDVTEGQPGPRV
FT WTFLAHDRDSGPNGQVEYSVVDGDPLGEFVISPVEGVLRVRKDVELDRETIAFYNLTIC
FT ARDRGVPPLSSTMLVGIRVLDINDNDPVLLNLPMNVTISENSPVSSFVAHVLASDADSG
FT CNALLTFNITAGNRERAFFINATTGIVTVNRPLDRERIPEYRLTVSVKDNPENPRIARK
FT DFDLLLVSLADENDNHPLFTEGTYQAEVMENSPAGTPLTVLNGPILALDADEDVYAVVT
FT YQLLGTHSDLFVIDNSTGVVTVRSGIIIDREAFSPPFLELLLLAEDIGQLNGTAHLFIT
FT ILDDNDNWPTFSPPTYTVHLLENCPPGFSVLQVTATDEDSGLNGELVYRIEAGAQDRFL
FT IHPVTGVIRVGNATIDREEQESYRLTVVATDRGTVPLSGTAIVTILIDDINDSRPEFLN
FT PIQTVSVLESAEPGTIIANVTAIDLDLNPKLEYHIISIVAKDDTDRLVPDQEDAFAVNI
FT NTGSVMVKSPLNRELVATYEVTLSVIDNASDLPEHSVSVPNAKLTVNILDVNDNTPQFK
FT PFGITYYTERVLEGATPGTTLIAVAAVDPDKGLNGLITYTLLDLTPPGYVQLEDSSAGK
FT VIANRTVDYEEVHWLNFTVRASDNGSPPRAAEIPVYLEIVDINDNNPIFDQPSYQEAVF
FT EDIAVGTVILRVTATDADSGNFALIEYSLVDGEGKFAINPNTGDISVLSSLDREKKDHY
FT ILTALAKDNPGDVASNRRENSVQVVIRVLDVNDCRPQFSKPQFSTSVYENEPAGTSVIT
FT MLATDQDEGSNSQLTYSLEGPGMEAFSVDMDSGLVTTQRPLQSYERFNLTVVATDGGEP
FT PLWGTTMLLVEVIDVNDNRPVFVRPPNGTILHIKEEIPLRSNVYEVYATDNDEGLNGAV
FT RYSFLKTTGNRDWEYFTIDPISGLIQTAQRLDREKQAVYSLILVASDLGQPVPYETMQP
FT LQVALEDIDDNEPLFVRPPKGSPQYQLLTVPEHSPRGTLVGNVTGAVDADEGPNAIVYY
FT FIAAGDEDKNFHLQPDGRLLVLRDLDRETEATFSFIVKASSNRSWTPPRGPSPALDLLT
FT DLTLQEVRVVLEDINDQPPRFTKAEYTAGVATDAKVGSELIQVLALDADIGNNSLVFYG
FT ILAIHYFRALANDSEDVGQVFTMGSVDGILRTFDLFMAYSPGYFVVDIVARDLAGHNDT
FT AIIGIYILRDDQRVKIVINEIPDRVRGFEEEFIRLLSNITGAIVNTDDVQFHVDMKGRV
FT NFAQTELLIHVVNRDTNRILDVDRVIQMIDENKEQLRNLFRNYNVLDVQPAISVQLPDD
FT MSALQMAIIVLAILLFLAAMLFVLMNWYYRTIHKRKLKAIVAGSAGNRGFIDIMDMPNT
FT NKYSFDGS -> MLLPNYRA (in isoform C1 and isoform C2)"
FT /id="VSP_059242"
FT VAR_SEQ 1..2240
FT /note="Missing (in isoform B2 and isoform B1)"
FT /id="VSP_059243"
FT VAR_SEQ 3212..3246
FT /note="Missing (in isoform 2, isoform B2 and isoform C2)"
FT /evidence="ECO:0000303|PubMed:11386759"
FT /id="VSP_000648"
FT VAR_SEQ 3247
FT /note="L -> EL (in isoform C1)"
FT /id="VSP_059244"
FT VARIANT 5
FT /note="L -> P (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 229
FT /note="M -> V (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 891
FT /note="R -> K (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 1137
FT /note="V -> I (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 1236
FT /note="K -> R (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 2025
FT /note="I -> V (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 2026
FT /note="I -> V (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 2217
FT /note="K -> T (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 2222
FT /note="R -> H (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 2270
FT /note="H -> R (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 2617
FT /note="G -> A (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT VARIANT 2718..2720
FT /note="Missing (in waltzer)"
FT /evidence="ECO:0000269|PubMed:11750125"
FT MUTAGEN 26
FT /note="N->I: Strongly reduced affinity for PCDH15."
FT /evidence="ECO:0000269|PubMed:20498078"
FT MUTAGEN 27
FT /note="R->I: Strongly reduced affinity for PCDH15."
FT /evidence="ECO:0000269|PubMed:20498078"
FT MUTAGEN 168
FT /note="L->G: Strongly reduced interaction with PCDH15."
FT /evidence="ECO:0000269|PubMed:23135401"
FT CONFLICT 94
FT /note="D -> G (in Ref. 2; AAK07670)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..143
FT /note="PE -> TQ (in Ref. 2; AAK07670)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..251
FT /note="HSPP -> QLTVNAT (in Ref. 2; AAK07670)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="D -> N (in Ref. 1; AAG52817 and 2; AAK07670)"
FT /evidence="ECO:0000305"
FT CONFLICT 3128
FT /note="S -> A (in Ref. 1; AAG52817, 2; AAK07670 and 3;
FT AAT72163/AAT72164)"
FT /evidence="ECO:0000305"
FT CONFLICT 3262
FT /note="G -> S (in Ref. 1; AAG52817)"
FT /evidence="ECO:0000305"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3MVS"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3MVS"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3MVS"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4APX"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:3MVS"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3MVS"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3MVS"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 217..227
FT /evidence="ECO:0007829|PDB:3MVS"
FT STRAND 1207..1209
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1211..1219
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1227..1230
FT /evidence="ECO:0007829|PDB:5VH2"
FT HELIX 1239..1242
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1244..1250
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1255..1258
FT /evidence="ECO:0007829|PDB:5VH2"
FT TURN 1260..1262
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1264..1267
FT /evidence="ECO:0007829|PDB:5VH2"
FT TURN 1273..1275
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1277..1289
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1294..1304
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1311..1316
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1318..1323
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1331..1334
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1337..1339
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1347..1350
FT /evidence="ECO:0007829|PDB:5VH2"
FT HELIX 1356..1361
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1362..1364
FT /evidence="ECO:0007829|PDB:5VH2"
FT TURN 1366..1368
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1370..1373
FT /evidence="ECO:0007829|PDB:5VH2"
FT HELIX 1379..1381
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1383..1392
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1394..1398
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1400..1409
FT /evidence="ECO:0007829|PDB:5VH2"
FT STRAND 1747..1755
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1762..1765
FT /evidence="ECO:0007829|PDB:5WJM"
FT HELIX 1774..1777
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1780..1786
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1792..1794
FT /evidence="ECO:0007829|PDB:5WJM"
FT TURN 1796..1798
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1800..1803
FT /evidence="ECO:0007829|PDB:5WJM"
FT TURN 1811..1813
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1815..1824
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1826..1829
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1832..1842
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1850..1853
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1855..1861
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1869..1872
FT /evidence="ECO:0007829|PDB:5WJM"
FT HELIX 1881..1884
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1886..1892
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1899..1901
FT /evidence="ECO:0007829|PDB:5WJM"
FT TURN 1903..1905
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1907..1910
FT /evidence="ECO:0007829|PDB:5WJM"
FT TURN 1916..1918
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1921..1930
FT /evidence="ECO:0007829|PDB:5WJM"
FT HELIX 1935..1937
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1940..1950
FT /evidence="ECO:0007829|PDB:5WJM"
FT STRAND 1958..1960
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 1962..1969
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 1979..1983
FT /evidence="ECO:0007829|PDB:5I8D"
FT HELIX 1993..1996
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 1999..2004
FT /evidence="ECO:0007829|PDB:5I8D"
FT HELIX 2007..2009
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2010..2012
FT /evidence="ECO:0007829|PDB:5I8D"
FT TURN 2014..2016
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2019..2021
FT /evidence="ECO:0007829|PDB:5I8D"
FT HELIX 2029..2031
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2036..2044
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2050..2060
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2068..2081
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2087..2090
FT /evidence="ECO:0007829|PDB:5I8D"
FT HELIX 2099..2101
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2105..2111
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2115..2118
FT /evidence="ECO:0007829|PDB:5I8D"
FT TURN 2120..2122
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2124..2127
FT /evidence="ECO:0007829|PDB:5I8D"
FT TURN 2134..2136
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2138..2147
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2150..2152
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2155..2165
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2173..2176
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2178..2184
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2192..2195
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2202..2204
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2207..2217
FT /evidence="ECO:0007829|PDB:5I8D"
FT TURN 2219..2221
FT /evidence="ECO:0007829|PDB:5UN2"
FT STRAND 2223..2225
FT /evidence="ECO:0007829|PDB:5TFK"
FT STRAND 2230..2233
FT /evidence="ECO:0007829|PDB:5I8D"
FT TURN 2235..2237
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2239..2242
FT /evidence="ECO:0007829|PDB:5I8D"
FT TURN 2248..2250
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2252..2262
FT /evidence="ECO:0007829|PDB:5I8D"
FT HELIX 2268..2270
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2277..2284
FT /evidence="ECO:0007829|PDB:5I8D"
FT STRAND 2292..2295
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2301..2306
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2314..2318
FT /evidence="ECO:0007829|PDB:5UZ8"
FT HELIX 2326..2329
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2332..2347
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2351..2358
FT /evidence="ECO:0007829|PDB:5UZ8"
FT TURN 2362..2364
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2366..2375
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2378..2380
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2383..2393
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2401..2405
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2407..2412
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2420..2423
FT /evidence="ECO:0007829|PDB:5UZ8"
FT HELIX 2432..2435
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2437..2442
FT /evidence="ECO:0007829|PDB:5UZ8"
FT TURN 2445..2447
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2448..2450
FT /evidence="ECO:0007829|PDB:5UZ8"
FT TURN 2452..2454
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2456..2459
FT /evidence="ECO:0007829|PDB:5UZ8"
FT TURN 2465..2467
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2469..2480
FT /evidence="ECO:0007829|PDB:5UZ8"
FT HELIX 2485..2487
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2490..2500
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2510..2519
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2527..2530
FT /evidence="ECO:0007829|PDB:5UZ8"
FT HELIX 2539..2542
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2545..2550
FT /evidence="ECO:0007829|PDB:5UZ8"
FT HELIX 2553..2555
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2556..2558
FT /evidence="ECO:0007829|PDB:5UZ8"
FT TURN 2560..2562
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2564..2569
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2576..2584
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2586..2589
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2592..2602
FT /evidence="ECO:0007829|PDB:5UZ8"
FT STRAND 2610..2614
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2616..2623
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2631..2634
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2636..2638
FT /evidence="ECO:0007829|PDB:5VT8"
FT HELIX 2643..2646
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2648..2652
FT /evidence="ECO:0007829|PDB:5VT8"
FT HELIX 2660..2663
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2664..2666
FT /evidence="ECO:0007829|PDB:5VT8"
FT TURN 2668..2670
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2672..2675
FT /evidence="ECO:0007829|PDB:5VT8"
FT TURN 2681..2683
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2685..2695
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2698..2700
FT /evidence="ECO:0007829|PDB:5VT8"
FT STRAND 2703..2713
FT /evidence="ECO:0007829|PDB:5VT8"
SQ SEQUENCE 3354 AA; 369623 MW; 6ADFABF6A5001DC0 CRC64;
MRYSLVTCYA VLWLLMLVPG SWGQVNRLPF FTNHFFDTYL LISEDTPVGS SVTQLLARDM
DNDPLVFGVS GEEASRFFAV EPDTGVVWLR QPLDRETKSE FTVEFSVSDH QGVITRKVNI
QVGDVNDNAP TFHNQPYSVR IPENTPVGTP IFIVNATDPD LGAGGSVLYS FQPPSPFFAI
DSARGIVTVI QELDYEVTQA YQLTVNATDQ DKTRPLSTLA NLAIIITDMQ DMDPIFINLP
YSTNIYEHSP PGTTVRVITA VDQDKGRPRG IGYTIVSGNT NSIFALDYIS GALTLNGLLD
RENPLYSHGF ILTVKGTELN DDRTPSDATV TTTFNILVID INDNAPEFNS SEYSVAITEL
AQVGFALPLF IQVVDKDEDL GLNSMFEVYL VGNNSHHFII SPTSVQGKAD IRIRVAIPLD
YETVDRYDFD LFANESVPDH VGYAKVKITL INENDNRPIF SQPLYNVSLY ENITVGTSVL
TVLATDNDVG TFGEVNYFFS DDPDRFSLDK DTGLIMLIAR LDYELIQRFT LTVIARDGGG
EETTGRVRIN VLDVNDNVPT FQKDAYVGAL RENEPSVTQL VRLRATDEDS PPNNLITYSI
VNASAFGSYF DISIYEGYGV ISVSRPLDYE QIPNGLIYLT VMAKDAGNPP LYSTVPVTIE
VFDENDNPPT FSKPAYFVSV LENIMAGATV LFLNATDLDR SREYGQESII YSLEGSSQFR
INARSGEITT TSLLDRETKS EYILIVRAVD GGVGHNQKTG IATVNVTLLD INDNHPTWKD
APYYINLVEM TPPDSDVTTV VAVDPDLGEN GTLVYSIHPP NKFYSLNSTT GKIRTTHVML
DRENPDPVEA ELMRKIIVSV TDCGRPPLKA TSSATVFVNL LDLNDNDPTF RNLPFVAEIL
EGTPAGVSVY QVVAIDLDEG LNGLVSYRMQ VGMPRMDFVI NSTSGVVTTT AELDRERIAE
YQLRVVASDA GTPTKSSTST LTVRVLDVND ETPTFFPAVY NVSVSEDVPR EFRVVWLNCT
DNDVGLNAEL SYFITAGNVD GKFSVGYRDA VVRTVVGLDR ETTAAYTLVL EAIDNGPVGK
RRTGTATVFV TVLDVNDNRP IFLQSSYEAS VPEDIPEGHS IVQLKATDAD EGEFGRVWYR
ILHGNHGNNF RIHVGSGLLM RGPRPLDRER NSSHVLMVEA YNHDLGPMRS SVRVIVYVED
VNDEAPVFTQ QQYNRLGLRE TAGIGTSVIV VRATDKDTGD GGLVNYRILS GAEGKFEIDE
STGLIVTVDY LDYETKTSYL MNVSATDGAP PFNQGFCSVY VTLLNELDEA VQFSNASYEA
VIMENLALGT EIVRVQAYSI DNLNQITYRF DAYTSAQAKA LFKIDAITGV ITVKGLVDRE
KGDFYTLTVV ADDGGPKVDS TVKVYITVLD ENDNSPRFDF TSDSAISVPE DCPVGQRVAT
VKARDPDAGS NGQVVFSLAS GNIAGAFEII TSNDSIGEVF VAKPLDREEL DHYILKVVAS
DRGTPPRKKD HILQVTILDV NDNPPVIESP FGYNVSVNEN VGGGTSVVQV RATDRDIGIN
SVLSYYITEG NEDMTFRMDR ISGEIATRPA PPDRERQNFY HLVVTVEDEG TPTLSATTHV
YVTIVDENDN APVFQQPHYE VVLDEGPDTI NTSLITVQAL DLDEGPNGTV TYAIVAGNII
NTFRINKHTG VITAAKELDY EISHGRYTLI VTATDQCPIL SHRLTSTTTV LVNVNDINDN
VPTFPRDYEG PFDVTEGQPG PRVWTFLAHD RDSGPNGQVE YSVVDGDPLG EFVISPVEGV
LRVRKDVELD RETIAFYNLT ICARDRGVPP LSSTMLVGIR VLDINDNDPV LLNLPMNVTI
SENSPVSSFV AHVLASDADS GCNALLTFNI TAGNRERAFF INATTGIVTV NRPLDRERIP
EYRLTVSVKD NPENPRIARK DFDLLLVSLA DENDNHPLFT EGTYQAEVME NSPAGTPLTV
LNGPILALDA DEDVYAVVTY QLLGTHSDLF VIDNSTGVVT VRSGIIIDRE AFSPPFLELL
LLAEDIGQLN GTAHLFITIL DDNDNWPTFS PPTYTVHLLE NCPPGFSVLQ VTATDEDSGL
NGELVYRIEA GAQDRFLIHP VTGVIRVGNA TIDREEQESY RLTVVATDRG TVPLSGTAIV
TILIDDINDS RPEFLNPIQT VSVLESAEPG TIIANVTAID LDLNPKLEYH IISIVAKDDT
DRLVPDQEDA FAVNINTGSV MVKSPLNREL VATYEVTLSV IDNASDLPEH SVSVPNAKLT
VNILDVNDNT PQFKPFGITY YTERVLEGAT PGTTLIAVAA VDPDKGLNGL ITYTLLDLTP
PGYVQLEDSS AGKVIANRTV DYEEVHWLNF TVRASDNGSP PRAAEIPVYL EIVDINDNNP
IFDQPSYQEA VFEDIAVGTV ILRVTATDAD SGNFALIEYS LVDGEGKFAI NPNTGDISVL
SSLDREKKDH YILTALAKDN PGDVASNRRE NSVQVVIRVL DVNDCRPQFS KPQFSTSVYE
NEPAGTSVIT MLATDQDEGS NSQLTYSLEG PGMEAFSVDM DSGLVTTQRP LQSYERFNLT
VVATDGGEPP LWGTTMLLVE VIDVNDNRPV FVRPPNGTIL HIKEEIPLRS NVYEVYATDN
DEGLNGAVRY SFLKTTGNRD WEYFTIDPIS GLIQTAQRLD REKQAVYSLI LVASDLGQPV
PYETMQPLQV ALEDIDDNEP LFVRPPKGSP QYQLLTVPEH SPRGTLVGNV TGAVDADEGP
NAIVYYFIAA GDEDKNFHLQ PDGRLLVLRD LDRETEATFS FIVKASSNRS WTPPRGPSPA
LDLLTDLTLQ EVRVVLEDIN DQPPRFTKAE YTAGVATDAK VGSELIQVLA LDADIGNNSL
VFYGILAIHY FRALANDSED VGQVFTMGSV DGILRTFDLF MAYSPGYFVV DIVARDLAGH
NDTAIIGIYI LRDDQRVKIV INEIPDRVRG FEEEFIRLLS NITGAIVNTD DVQFHVDMKG
RVNFAQTELL IHVVNRDTNR ILDVDRVIQM IDENKEQLRN LFRNYNVLDV QPAISVQLPD
DMSALQMAII VLAILLFLAA MLFVLMNWYY RTIHKRKLKA IVAGSAGNRG FIDIMDMPNT
NKYSFDGSNP VWLDPFCRNL ELAAQAEHED DLPENLSEIA DLWNSPTRTH GTFGREPAAV
KPDDDRYLRA AIQEYDNIAK LGQIIREGPI KGSLLKVVLE DYLRLKKLFA QRMVQKASSC
HSSISELIHT DLEEEPGDHS PGQGSLRFRH KPPMELKGQD GIHMVHGSTG TLLATDLNSL
PEDDQKGLDR SLETLTASEA TAFERNARTE SAKSTPLHKL RDVIMESPLE ITEL
