ID   CADH3_HUMAN             Reviewed;         829 AA.
AC   P22223; B2R6F4; Q05DI6;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Cadherin-3;
DE   AltName: Full=Placental cadherin;
DE            Short=P-cadherin;
DE   Flags: Precursor;
GN   Name=CDH3; Synonyms=CDHP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-563.
RX   PubMed=2793940; DOI=10.1083/jcb.109.4.1787;
RA   Shimoyama Y., Yoshida T., Terada M., Shimosato Y., Abe O., Hirohashi S.;
RT   "Molecular cloning of a human Ca2+-dependent cell-cell adhesion molecule
RT   homologous to mouse placental cadherin: its low expression in human
RT   placental tissues.";
RL   J. Cell Biol. 109:1787-1794(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-563.
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-563.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   MET-237.
RC   TISSUE=Skin, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RC   TISSUE=Fetal brain;
RX   PubMed=9815605;
RA   Jarrard D.F., Paul R., Van Bokhoven A., Nguyen S.H., Bova G.S.,
RA   Wheelock M.J., Johnson K.R., Schalken J., Bussemakers M., Isaacs W.B.;
RT   "P-cadherin is a basal cell-specific epithelial marker that is not
RT   expressed in prostate cancer.";
RL   Clin. Cancer Res. 3:2121-2128(1997).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=2702654;
RA   Shimoyama Y., Hirohashi S., Hirano S., Noguchi M., Shimosato Y.,
RA   Takeichi M., Abe O.;
RT   "Cadherin cell-adhesion molecules in human epithelial tissues and
RT   carcinomas.";
RL   Cancer Res. 49:2128-2133(1989).
RN   [7]
RP   INTERACTION WITH CDCP1.
RX   PubMed=16007225; DOI=10.1038/sj.onc.1208582;
RA   Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.;
RT   "Adhesion signaling by a novel mitotic substrate of src kinases.";
RL   Oncogene 24:5333-5343(2005).
RN   [8]
RP   INVOLVEMENT IN HJMD.
RX   PubMed=11544476; DOI=10.1038/ng716;
RA   Sprecher E., Bergman R., Richard G., Lurie R., Shalev S., Petronius D.,
RA   Shalata A., Anbinder Y., Leibu R., Perlman I., Cohen N., Szargel R.;
RT   "Hypotrichosis with juvenile macular dystrophy is caused by a mutation in
RT   CDH3, encoding P-cadherin.";
RL   Nat. Genet. 29:134-136(2001).
RN   [9]
RP   INTERACTION WITH CTNNB1.
RX   PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
RA   Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
RT   "Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
RL   Mol. Cell 24:293-300(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   VARIANT HJMD HIS-503.
RX   PubMed=12445216; DOI=10.1046/j.1523-1747.2002.19528.x;
RA   Indelman M., Bergman R., Lurie R., Richard G., Miller B., Petronius D.,
RA   Ciubutaro D., Leibu R., Sprecher E.;
RT   "A missense mutation in CDH3, encoding P-cadherin, causes hypotrichosis
RT   with juvenile macular dystrophy.";
RL   J. Invest. Dermatol. 119:1210-1213(2002).
RN   [12]
RP   VARIANT EEMS ILE-322, AND VARIANT HIS-563.
RX   PubMed=15805154; DOI=10.1136/jmg.2004.027821;
RA   Kjaer K.W., Hansen L., Schwabe G.C., Marques-de-Faria A.P., Eiberg H.,
RA   Mundlos S., Tommerup N., Rosenberg T.;
RT   "Distinct CDH3 mutations cause ectodermal dysplasia, ectrodactyly, macular
RT   dystrophy (EEM syndrome).";
RL   J. Med. Genet. 42:292-298(2005).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC       preferentially interact with themselves in a homophilic manner in
CC       connecting cells; cadherins may thus contribute to the sorting of
CC       heterogeneous cell types.
CC   -!- SUBUNIT: Interacts with CDCP1 and CTNNB1. {ECO:0000269|PubMed:16007225,
CC       ECO:0000269|PubMed:17052462}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P22223-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P22223-2; Sequence=VSP_024820;
CC   -!- TISSUE SPECIFICITY: Expressed in some normal epithelial tissues and in
CC       some carcinoma cell lines. {ECO:0000269|PubMed:2702654}.
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:0000250}.
CC   -!- DISEASE: Hypotrichosis congenital with juvenile macular dystrophy
CC       (HJMD) [MIM:601553]: A disorder characterized by congenital
CC       hypotrichosis, early hair loss, and severe degenerative changes of the
CC       retinal macula that culminate in blindness during the second to third
CC       decade of life. {ECO:0000269|PubMed:11544476,
CC       ECO:0000269|PubMed:12445216}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Ectodermal dysplasia, ectrodactyly, and macular dystrophy
CC       syndrome (EEMS) [MIM:225280]: A form of ectodermal dysplasia, a
CC       heterogeneous group of disorders due to abnormal development of two or
CC       more ectodermal structures. It is an autosomal recessive condition
CC       characterized by features of ectodermal dysplasia such as sparse
CC       eyebrows and scalp hair, and selective tooth agenesis associated with
CC       macular dystrophy and ectrodactyly. {ECO:0000269|PubMed:15805154}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- WEB RESOURCE: Name=Mutations of the CDH3 gene; Note=Retina
CC       International's Scientific Newsletter;
CC       URL="https://www.retina-international.org/files/sci-news/cdh3mut.htm";
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DR   EMBL; X63629; CAA45177.1; -; mRNA.
DR   EMBL; AK312554; BAG35451.1; -; mRNA.
DR   EMBL; CH471092; EAW83238.1; -; Genomic_DNA.
DR   EMBL; BC014462; AAH14462.1; -; mRNA.
DR   EMBL; BC041846; AAH41846.1; -; mRNA.
DR   EMBL; X95824; CAA65093.1; -; Genomic_DNA.
DR   CCDS; CCDS10868.1; -. [P22223-1]
DR   CCDS; CCDS82004.1; -. [P22223-2]
DR   PIR; A33659; IJHUCP.
DR   RefSeq; NP_001304124.1; NM_001317195.1. [P22223-2]
DR   RefSeq; NP_001304125.1; NM_001317196.1.
DR   RefSeq; NP_001784.2; NM_001793.5. [P22223-1]
DR   PDB; 4OY9; X-ray; 1.62 A; A=108-320.
DR   PDB; 4ZML; X-ray; 1.85 A; A=108-320.
DR   PDB; 4ZMN; X-ray; 2.60 A; A=108-338.
DR   PDB; 4ZMO; X-ray; 2.48 A; A=108-320.
DR   PDB; 4ZMP; X-ray; 2.15 A; A=108-320.
DR   PDB; 4ZMQ; X-ray; 2.20 A; A/B=108-320.
DR   PDB; 4ZMT; X-ray; 2.70 A; A/B/C/D/E/F=108-338.
DR   PDB; 4ZMV; X-ray; 2.40 A; A/B=108-320.
DR   PDB; 4ZMW; X-ray; 2.30 A; A/B=108-320.
DR   PDB; 4ZMX; X-ray; 3.10 A; A/B=108-320.
DR   PDB; 4ZMY; X-ray; 1.50 A; A=108-320.
DR   PDB; 4ZMZ; X-ray; 2.05 A; A=107-320.
DR   PDB; 5JYL; X-ray; 2.55 A; A/C=108-207.
DR   PDB; 5JYM; X-ray; 2.45 A; A/C=108-320.
DR   PDB; 6ZTB; X-ray; 1.40 A; I=108-324.
DR   PDB; 6ZTR; X-ray; 2.10 A; I/J=108-324.
DR   PDB; 7CME; X-ray; 2.45 A; A/B=108-320.
DR   PDB; 7CMF; X-ray; 2.30 A; A=107-320.
DR   PDB; 8HYI; X-ray; 2.85 A; A/B=108-320.
DR   PDBsum; 4OY9; -.
DR   PDBsum; 4ZML; -.
DR   PDBsum; 4ZMN; -.
DR   PDBsum; 4ZMO; -.
DR   PDBsum; 4ZMP; -.
DR   PDBsum; 4ZMQ; -.
DR   PDBsum; 4ZMT; -.
DR   PDBsum; 4ZMV; -.
DR   PDBsum; 4ZMW; -.
DR   PDBsum; 4ZMX; -.
DR   PDBsum; 4ZMY; -.
DR   PDBsum; 4ZMZ; -.
DR   PDBsum; 5JYL; -.
DR   PDBsum; 5JYM; -.
DR   PDBsum; 6ZTB; -.
DR   PDBsum; 6ZTR; -.
DR   PDBsum; 7CME; -.
DR   PDBsum; 7CMF; -.
DR   PDBsum; 8HYI; -.
DR   AlphaFoldDB; P22223; -.
DR   SMR; P22223; -.
DR   BioGRID; 107436; 33.
DR   IntAct; P22223; 11.
DR   STRING; 9606.ENSP00000264012; -.
DR   ChEMBL; CHEMBL3989384; -.
DR   GlyCosmos; P22223; 2 sites, No reported glycans.
DR   GlyGen; P22223; 2 sites.
DR   iPTMnet; P22223; -.
DR   PhosphoSitePlus; P22223; -.
DR   BioMuta; CDH3; -.
DR   DMDM; 146345382; -.
DR   EPD; P22223; -.
DR   jPOST; P22223; -.
DR   MassIVE; P22223; -.
DR   MaxQB; P22223; -.
DR   PaxDb; 9606-ENSP00000264012; -.
DR   PeptideAtlas; P22223; -.
DR   ProteomicsDB; 53966; -. [P22223-1]
DR   ProteomicsDB; 53967; -. [P22223-2]
DR   Pumba; P22223; -.
DR   ABCD; P22223; 42 sequenced antibodies.
DR   Antibodypedia; 942; 1048 antibodies from 41 providers.
DR   DNASU; 1001; -.
DR   Ensembl; ENST00000264012.9; ENSP00000264012.4; ENSG00000062038.15. [P22223-1]
DR   Ensembl; ENST00000429102.6; ENSP00000398485.2; ENSG00000062038.15. [P22223-2]
DR   GeneID; 1001; -.
DR   KEGG; hsa:1001; -.
DR   MANE-Select; ENST00000264012.9; ENSP00000264012.4; NM_001793.6; NP_001784.2.
DR   UCSC; uc002ewf.3; human. [P22223-1]
DR   AGR; HGNC:1762; -.
DR   CTD; 1001; -.
DR   DisGeNET; 1001; -.
DR   GeneCards; CDH3; -.
DR   HGNC; HGNC:1762; CDH3.
DR   HPA; ENSG00000062038; Tissue enhanced (choroid plexus, ovary).
DR   MalaCards; CDH3; -.
DR   MIM; 114021; gene.
DR   MIM; 225280; phenotype.
DR   MIM; 601553; phenotype.
DR   neXtProt; NX_P22223; -.
DR   OpenTargets; ENSG00000062038; -.
DR   Orphanet; 1897; EEM syndrome.
DR   Orphanet; 1573; Hypotrichosis with juvenile macular degeneration.
DR   PharmGKB; PA26299; -.
DR   VEuPathDB; HostDB:ENSG00000062038; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000154848; -.
DR   HOGENOM; CLU_005284_2_0_1; -.
DR   InParanoid; P22223; -.
DR   OMA; EAQNQHT; -.
DR   OrthoDB; 5306553at2759; -.
DR   PhylomeDB; P22223; -.
DR   TreeFam; TF316817; -.
DR   PathwayCommons; P22223; -.
DR   Reactome; R-HSA-418990; Adherens junctions interactions.
DR   SignaLink; P22223; -.
DR   SIGNOR; P22223; -.
DR   BioGRID-ORCS; 1001; 10 hits in 1151 CRISPR screens.
DR   ChiTaRS; CDH3; human.
DR   GeneWiki; CDH3_(gene); -.
DR   GenomeRNAi; 1001; -.
DR   Pharos; P22223; Tbio.
DR   PRO; PR:P22223; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P22223; Protein.
DR   Bgee; ENSG00000062038; Expressed in secondary oocyte and 140 other cell types or tissues.
DR   ExpressionAtlas; P22223; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   GO; GO:0022405; P:hair cycle process; IMP:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0031424; P:keratinization; IMP:UniProtKB.
DR   GO; GO:0051796; P:negative regulation of timing of catagen; IMP:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:UniProtKB.
DR   GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IMP:UniProtKB.
DR   GO; GO:1902910; P:positive regulation of melanosome transport; IMP:UniProtKB.
DR   GO; GO:0032773; P:positive regulation of tyrosinase activity; IMP:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0001895; P:retina homeostasis; IMP:UniProtKB.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd11304; Cadherin_repeat; 3.
DR   Gene3D; 2.60.40.60; Cadherins; 5.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR014868; Cadherin_pro_dom.
DR   InterPro; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF444; CADHERIN-3; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 4.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 4.
DR   SMART; SM01055; Cadherin_pro; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
DR   Genevisible; P22223; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Disease variant; Ectodermal dysplasia;
KW   Glycoprotein; Hypotrichosis; Membrane; Metal-binding; Reference proteome;
KW   Repeat; Sensory transduction; Signal; Transmembrane; Transmembrane helix;
KW   Vision.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..107
FT                   /id="PRO_0000003745"
FT   CHAIN           108..829
FT                   /note="Cadherin-3"
FT                   /id="PRO_0000003746"
FT   TOPO_DOM        108..654
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        655..677
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        678..829
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          108..215
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          216..328
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          329..440
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          441..546
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          547..650
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         761..829
FT                   /note="NLKAANTDPTAPPYDTLLVFDYEGSGSDAASLSSLTSSASDQDQDYDYLNEW
FT                   GSRFKKLADMYGGGEDD -> GRGERGSQRGNGGLQLARGRTRRS (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024820"
FT   VARIANT         237
FT                   /note="V -> M (in dbSNP:rs17854171)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_031929"
FT   VARIANT         322
FT                   /note="N -> I (in EEMS; dbSNP:rs121434543)"
FT                   /evidence="ECO:0000269|PubMed:15805154"
FT                   /id="VAR_033010"
FT   VARIANT         477
FT                   /note="R -> H (in dbSNP:rs34494880)"
FT                   /id="VAR_031930"
FT   VARIANT         503
FT                   /note="R -> H (in HJMD; dbSNP:rs121434542)"
FT                   /evidence="ECO:0000269|PubMed:12445216"
FT                   /id="VAR_015422"
FT   VARIANT         563
FT                   /note="Q -> H (in dbSNP:rs1126933)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15805154, ECO:0000269|PubMed:2793940,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_031931"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:4ZMQ"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   HELIX           134..137
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   TURN            175..177
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          179..189
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:4ZMT"
FT   STRAND          199..206
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          214..216
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          218..225
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          233..236
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          246..249
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          254..262
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:4ZMP"
FT   STRAND          269..272
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   TURN            274..276
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          278..281
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   TURN            288..290
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          293..301
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   HELIX           303..305
FT                   /evidence="ECO:0007829|PDB:6ZTB"
FT   STRAND          309..319
FT                   /evidence="ECO:0007829|PDB:6ZTB"
SQ   SEQUENCE   829 AA;  91418 MW;  7C03C8536CD98C7B CRC64;
     MGLPRGPLAS LLLLQVCWLQ CAASEPCRAV FREAEVTLEA GGAEQEPGQA LGKVFMGCPG
     QEPALFSTDN DDFTVRNGET VQERRSLKER NPLKIFPSKR ILRRHKRDWV VAPISVPENG
     KGPFPQRLNQ LKSNKDRDTK IFYSITGPGA DSPPEGVFAV EKETGWLLLN KPLDREEIAK
     YELFGHAVSE NGASVEDPMN ISIIVTDQND HKPKFTQDTF RGSVLEGVLP GTSVMQVTAT
     DEDDAIYTYN GVVAYSIHSQ EPKDPHDLMF TIHRSTGTIS VISSGLDREK VPEYTLTIQA
     TDMDGDGSTT TAVAVVEILD ANDNAPMFDP QKYEAHVPEN AVGHEVQRLT VTDLDAPNSP
     AWRATYLIMG GDDGDHFTIT THPESNQGIL TTRKGLDFEA KNQHTLYVEV TNEAPFVLKL
     PTSTATIVVH VEDVNEAPVF VPPSKVVEVQ EGIPTGEPVC VYTAEDPDKE NQKISYRILR
     DPAGWLAMDP DSGQVTAVGT LDREDEQFVR NNIYEVMVLA MDNGSPPTTG TGTLLLTLID
     VNDHGPVPEP RQITICNQSP VRQVLNITDK DLSPHTSPFQ AQLTDDSDIY WTAEVNEEGD
     TVVLSLKKFL KQDTYDVHLS LSDHGNKEQL TVIRATVCDC HGHVETCPGP WKGGFILPVL
     GAVLALLFLL LVLLLLVRKK RKIKEPLLLP EDDTRDNVFY YGEEGGGEED QDYDITQLHR
     GLEARPEVVL RNDVAPTIIP TPMYRPRPAN PDEIGNFIIE NLKAANTDPT APPYDTLLVF
     DYEGSGSDAA SLSSLTSSAS DQDQDYDYLN EWGSRFKKLA DMYGGGEDD
//