CAD13_HUMAN
ID CAD13_HUMAN Reviewed; 713 AA.
AC P55290; A8W476; A8W477; B7Z590; C9JRI6; J3KN62; Q6GTW4; Q8TBX3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Cadherin-13;
DE AltName: Full=Heart cadherin;
DE Short=H-cadherin;
DE AltName: Full=P105;
DE AltName: Full=Truncated cadherin;
DE Short=T-cad;
DE Short=T-cadherin;
DE Flags: Precursor;
GN Name=CDH13; Synonyms=CDHH;
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).
RC TISSUE=Fetal brain;
RX PubMed=7982033; DOI=10.3109/15419069409014199;
RA Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S.;
RT "Cloning of five human cadherins clarifies characteristic features of
RT cadherin extracellular domain and provides further evidence for two
RT structurally different types of cadherin.";
RL Cell Adhes. Commun. 2:15-26(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8673923; DOI=10.1038/nm0796-776;
RA Lee S.W.;
RT "H-cadherin, a novel cadherin with growth inhibitory functions and
RT diminished expression in human breast cancer.";
RL Nat. Med. 2:776-782(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9737784; DOI=10.1007/s004390050790;
RA Sato M., Mori Y., Sakurada A., Fujimura S., Horii A.;
RT "The H-cadherin (CDH13) gene is inactivated in human lung cancer.";
RL Hum. Genet. 103:96-101(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA Liu Q.-R., Liu J.J., Zhu X.-G., Uhl G.R.;
RT "Differential alternative splicing of Cadherin 13 gene in aging and
RT Alzheimer's disease.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, 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 [8]
RP PROTEIN SEQUENCE OF 140-149; 162-169 AND 284-287 (ISOFORM 1).
RC TISSUE=Aorta;
RX PubMed=9468307; DOI=10.1016/s0014-5793(97)01562-7;
RA Tkachuk V.A., Bochkov V.N., Philippova M.P., Stambolsky D.V.,
RA Kuzmenko E.S., Sidorova M.V., Molokoedov A.S., Spirov V.G., Resink T.J.;
RT "Identification of an atypical lipoprotein-binding protein from human
RT aortic smooth muscle as T-cadherin.";
RL FEBS Lett. 421:208-212(1998).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=10737605; DOI=10.1046/j.1471-4159.2000.0741489.x;
RA Takeuchi T., Misaki A., Liang S.-B., Tachibana A., Hayashi N., Sonobe H.,
RA Ohtsuki Y.;
RT "Expression of T-cadherin (CDH13, H-Cadherin) in human brain and its
RT characteristics as a negative growth regulator of epidermal growth factor
RT in neuroblastoma cells.";
RL J. Neurochem. 74:1489-1497(2000).
RN [10]
RP CHARACTERIZATION.
RX PubMed=11027617; DOI=10.1006/bbrc.2000.3465;
RA Niermann T., Kern F., Erne P., Resink T.;
RT "The glycosyl phosphatidylinositol anchor of human T-cadherin binds
RT lipoproteins.";
RL Biochem. Biophys. Res. Commun. 276:1240-1247(2000).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-500 AND ASN-638.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17566972; DOI=10.1002/pmic.200700068;
RA Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K.,
RA Arizmendi J.M., Jensen O.N., Matthiesen R.;
RT "Computational approach for identification and characterization of GPI-
RT anchored peptides in proteomics experiments.";
RL Proteomics 7:1951-1960(2007).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-530 AND ASN-638.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP VARIANTS CYS-65; VAL-103; ARG-113; TRP-246; GLN-367; THR-376 AND ARG-643.
RX PubMed=21220648; DOI=10.1001/archneurol.2010.351;
RA Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D.,
RA Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A.,
RA Rouleau G.A.;
RT "Resequencing of 29 candidate genes in patients with familial and sporadic
RT amyotrophic lateral sclerosis.";
RL Arch. Neurol. 68:587-593(2011).
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. May act as a negative regulator of neural
CC cell growth. {ECO:0000269|PubMed:10737605}.
CC -!- SUBUNIT: By contrast to classical cadherins, homodimerization in trans
CC is not mediated by cadherin EC1 domain strand-swapping, but instead
CC through a homophilic adhesive interface which joins two elongated EC1-
CC EC2 domains through a region near their Ca2+-binding sites to form a
CC tetrahedral, X-like shape. {ECO:0000250}.
CC -!- INTERACTION:
CC P55290; P42858: HTT; NbExp=6; IntAct=EBI-7205595, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P55290-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55290-2; Sequence=VSP_042696, VSP_042697;
CC Name=3;
CC IsoId=P55290-3; Sequence=VSP_042794, VSP_042795;
CC Name=4;
CC IsoId=P55290-4; Sequence=VSP_046714;
CC Name=5;
CC IsoId=P55290-5; Sequence=VSP_053739;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart. In the CNS, expressed in
CC cerebral cortex, medulla, hippocampus, amygdala, thalamus and
CC substantia nigra. No expression detected in cerebellum or spinal cord.
CC {ECO:0000269|PubMed:10737605, ECO:0000269|PubMed:8673923}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher levels in adult brain than in
CC developing brain. {ECO:0000269|PubMed:10737605}.
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 -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CDH13ID40018ch16q23.html";
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DR EMBL; L34058; AAA35624.1; -; mRNA.
DR EMBL; U59289; AAB18912.1; -; mRNA.
DR EMBL; U59288; AAB18911.1; -; mRNA.
DR EMBL; AB001103; BAA32411.1; -; Genomic_DNA.
DR EMBL; EU190357; ABW97440.1; -; mRNA.
DR EMBL; EU190358; ABW97441.1; -; mRNA.
DR EMBL; AK298612; BAH12826.1; -; mRNA.
DR EMBL; AC009028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028624; AAH28624.1; -; mRNA.
DR EMBL; BC030653; AAH30653.1; -; mRNA.
DR CCDS; CCDS56009.1; -. [P55290-3]
DR CCDS; CCDS56010.1; -. [P55290-2]
DR CCDS; CCDS58485.1; -. [P55290-4]
DR CCDS; CCDS58486.1; -. [P55290-1]
DR CCDS; CCDS58487.1; -. [P55290-5]
DR PIR; B38992; B38992.
DR RefSeq; NP_001207418.1; NM_001220489.1. [P55290-5]
DR RefSeq; NP_001207420.1; NM_001220491.1. [P55290-2]
DR RefSeq; NP_001207421.1; NM_001220492.1. [P55290-3]
DR RefSeq; NP_001248.1; NM_001257.4. [P55290-1]
DR PDB; 2V37; NMR; -; A=139-243.
DR PDBsum; 2V37; -.
DR AlphaFoldDB; P55290; -.
DR BMRB; P55290; -.
DR SMR; P55290; -.
DR BioGRID; 107447; 33.
DR IntAct; P55290; 32.
DR MINT; P55290; -.
DR STRING; 9606.ENSP00000268613; -.
DR GlyConnect; 1921; 15 N-Linked glycans (5 sites).
DR GlyGen; P55290; 9 sites, 15 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P55290; -.
DR PhosphoSitePlus; P55290; -.
DR SwissPalm; P55290; -.
DR BioMuta; CDH13; -.
DR DMDM; 1705552; -.
DR CPTAC; CPTAC-656; -.
DR CPTAC; non-CPTAC-2636; -.
DR EPD; P55290; -.
DR jPOST; P55290; -.
DR MassIVE; P55290; -.
DR MaxQB; P55290; -.
DR PaxDb; P55290; -.
DR PeptideAtlas; P55290; -.
DR PRIDE; P55290; -.
DR ProteomicsDB; 56840; -. [P55290-1]
DR ProteomicsDB; 56841; -. [P55290-2]
DR ProteomicsDB; 56842; -. [P55290-3]
DR ProteomicsDB; 6668; -.
DR TopDownProteomics; P55290-1; -. [P55290-1]
DR Antibodypedia; 667; 644 antibodies from 42 providers.
DR DNASU; 1012; -.
DR Ensembl; ENST00000268613.14; ENSP00000268613.10; ENSG00000140945.17. [P55290-4]
DR Ensembl; ENST00000428848.7; ENSP00000394557.3; ENSG00000140945.17. [P55290-5]
DR Ensembl; ENST00000431540.7; ENSP00000408632.3; ENSG00000140945.17. [P55290-2]
DR Ensembl; ENST00000565636.5; ENSP00000456491.1; ENSG00000140945.17. [P55290-3]
DR Ensembl; ENST00000567109.6; ENSP00000479395.1; ENSG00000140945.17. [P55290-1]
DR GeneID; 1012; -.
DR KEGG; hsa:1012; -.
DR MANE-Select; ENST00000567109.6; ENSP00000479395.1; NM_001257.5; NP_001248.1.
DR UCSC; uc002fgx.4; human. [P55290-1]
DR CTD; 1012; -.
DR DisGeNET; 1012; -.
DR GeneCards; CDH13; -.
DR HGNC; HGNC:1753; CDH13.
DR HPA; ENSG00000140945; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MIM; 601364; gene.
DR neXtProt; NX_P55290; -.
DR OpenTargets; ENSG00000140945; -.
DR PharmGKB; PA26287; -.
DR VEuPathDB; HostDB:ENSG00000140945; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155218; -.
DR HOGENOM; CLU_1532021_0_0_1; -.
DR InParanoid; P55290; -.
DR OMA; VCTCKKS; -.
DR PhylomeDB; P55290; -.
DR PathwayCommons; P55290; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; P55290; -.
DR SIGNOR; P55290; -.
DR BioGRID-ORCS; 1012; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; CDH13; human.
DR EvolutionaryTrace; P55290; -.
DR GeneWiki; T-cadherin; -.
DR GenomeRNAi; 1012; -.
DR Pharos; P55290; Tbio.
DR PRO; PR:P55290; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P55290; protein.
DR Bgee; ENSG00000140945; Expressed in descending thoracic aorta and 114 other tissues.
DR ExpressionAtlas; P55290; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0055100; F:adiponectin binding; ISS:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0071813; F:lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0043542; P:endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:BHF-UCL.
DR GO; GO:0043616; P:keratinocyte proliferation; IDA:BHF-UCL.
DR GO; GO:0030032; P:lamellipodium assembly; IDA:BHF-UCL.
DR GO; GO:0051668; P:localization within membrane; IMP:BHF-UCL.
DR GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IDA:BHF-UCL.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:BHF-UCL.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0016601; P:Rac protein signal transduction; IMP:BHF-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:BHF-UCL.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:BHF-UCL.
DR GO; GO:0002040; P:sprouting angiogenesis; IDA:BHF-UCL.
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; IPR033216; CDH13.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF80; PTHR24027:SF80; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..138
FT /id="PRO_0000003793"
FT CHAIN 139..693
FT /note="Cadherin-13"
FT /id="PRO_0000003794"
FT PROPEP 694..713
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000003795"
FT DOMAIN 139..245
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 246..363
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 364..477
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 478..585
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 584..694
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT LIPID 693
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..14
FT /note="MQPRTPLVLCVLLS -> MKTPPGASSRTKCSRELRSFCAFSCPRAKQPTCT
FT AWFPQQEHPSENGPQMPGRDPPAASTM (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_046714"
FT VAR_SEQ 123..161
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053739"
FT VAR_SEQ 162..190
FT /note="VVDSDRPERSKFRLTGKGVDQEPKGIFRI -> RTHNPINSELLLNEGITAD
FT LNPCITILAI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_042696"
FT VAR_SEQ 162..175
FT /note="VVDSDRPERSKFRL -> MKIWQVLCLARWLT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_042794"
FT VAR_SEQ 176..713
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_042795"
FT VAR_SEQ 191..713
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_042697"
FT VARIANT 65
FT /note="R -> C (in a patient with amyotrophic lateral
FT sclerosis; dbSNP:rs368685803)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065747"
FT VARIANT 103
FT /note="A -> V (in a patient with amyotrophic lateral
FT sclerosis; dbSNP:rs199539898)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065748"
FT VARIANT 113
FT /note="G -> R (in a patient with amyotrophic lateral
FT sclerosis; dbSNP:rs183971768)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065749"
FT VARIANT 121
FT /note="L -> S (in dbSNP:rs7197352)"
FT /id="VAR_030632"
FT VARIANT 246
FT /note="R -> W (in a patient with amyotrophic lateral
FT sclerosis; dbSNP:rs377210458)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065750"
FT VARIANT 367
FT /note="E -> Q (in a patient with amyotrophic lateral
FT sclerosis; dbSNP:rs200000145)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065751"
FT VARIANT 376
FT /note="A -> T (in dbSNP:rs35549391)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065752"
FT VARIANT 643
FT /note="L -> R (in dbSNP:rs34106627)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065753"
FT CONFLICT 199
FT /note="V -> M (in Ref. 4; AAH28624/AAH30653)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="Q -> R (in Ref. 4; AAH28624/AAH30653)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="T -> A (in Ref. 4; AAH28624/AAH30653)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="P -> T (in Ref. 4; AAH28624/AAH30653)"
FT /evidence="ECO:0000305"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2V37"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2V37"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2V37"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 224..236
FT /evidence="ECO:0007829|PDB:2V37"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2V37"
SQ SEQUENCE 713 AA; 78287 MW; CEB662D77824CB60 CRC64;
MQPRTPLVLC VLLSQVLLLT SAEDLDCTPG FQQKVFHINQ PAEFIEDQSI LNLTFSDCKG
NDKLRYEVSS PYFKVNSDGG LVALRNITAV GKTLFVHART PHAEDMAELV IVGGKDIQGS
LQDIFKFART SPVPRQKRSI VVSPILIPEN QRQPFPRDVG KVVDSDRPER SKFRLTGKGV
DQEPKGIFRI NENTGSVSVT RTLDREVIAV YQLFVETTDV NGKTLEGPVP LEVIVIDQND
NRPIFREGPY IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY
IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT IMIDDKNDHS
PKFTKKEFQA TVEEGAVGVI VNLTVEDKDD PTTGAWRAAY TIINGNPGQS FEIHTNPQTN
EGMLSVVKPL DYEISAFHTL LIKVENEDPL VPDVSYGPSS TATVHITVLD VNEGPVFYPD
PMMVTRQEDL SVGSVLLTVN ATDPDSLQHQ TIRYSVYKDP AGWLNINPIN GTVDTTAVLD
RESPFVDNSV YTALFLAIDS GNPPATGTGT LLITLEDVND NAPFIYPTVA EVCDDAKNLS
VVILGASDKD LHPNTDPFKF EIHKQAVPDK VWKISKINNT HALVSLLQNL NKANYNLPIM
VTDSGKPPMT NITDLRVQVC SCRNSKVDCN AAGALRFSLP SVLLLSLFSL ACL
