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 27-MAR-2024, entry version 209. 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="https://atlasgeneticsoncology.org/gene/40018/CDH13"; 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; 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; 37. DR IntAct; P55290; 36. DR MINT; P55290; -. DR STRING; 9606.ENSP00000268613; -. DR GlyConnect; 1921; 15 N-Linked glycans (5 sites). DR GlyCosmos; P55290; 9 sites, 16 glycans. DR GlyGen; P55290; 11 sites, 15 N-linked glycans (5 sites), 2 O-linked glycans (3 sites). 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; 9606-ENSP00000268613; -. DR PeptideAtlas; P55290; -. DR ProteomicsDB; 56840; -. [P55290-1] DR ProteomicsDB; 56841; -. [P55290-2] DR ProteomicsDB; 56842; -. [P55290-3] DR ProteomicsDB; 6668; -. DR Pumba; P55290; -. DR TopDownProteomics; P55290-1; -. [P55290-1] DR Antibodypedia; 667; 697 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 AGR; HGNC:1753; -. 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; QVCICKK; -. DR OrthoDB; 5306553at2759; -. DR PhylomeDB; P55290; -. DR PathwayCommons; P55290; -. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR SignaLink; P55290; -. DR SIGNOR; P55290; -. DR BioGRID-ORCS; 1012; 16 hits in 1155 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 115 other cell types or tissues. DR ExpressionAtlas; P55290; 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: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:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. 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:0042802; F:identical protein binding; IEA:Ensembl. 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:0034332; P:adherens junction organization; IBA:GO_Central. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL. 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: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 CDD; cd11304; Cadherin_repeat; 5. DR Gene3D; 2.60.40.60; Cadherins; 6. 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 PANTHER; PTHR24027:SF80; CADHERIN-13; 1. DR PANTHER; PTHR24027; CADHERIN-23; 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; Cadherin-like; 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 //