ID   CAD11_HUMAN             Reviewed;         796 AA.
AC   P55287; A8K5D6; A8MZC8; B7WP28; Q15065; Q15066; Q9UQ93; Q9UQ94;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   04-NOV-2026, entry version 199.
DE   RecName: Full=Cadherin-11;
DE   AltName: Full=OSF-4;
DE   AltName: Full=Osteoblast cadherin;
DE            Short=OB-cadherin;
DE   Flags: Precursor;
GN   Name=CDH11;
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=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] (ISOFORMS 1 AND 2), AND VARIANTS ILE-275 AND
RP   ALA-373.
RC   TISSUE=Osteosarcoma;
RX   PubMed=8163513; DOI=10.1016/s0021-9258(17)32685-6;
RA   Okazaki M., Takeshita S., Kawai S., Kikuno R., Tsujimura A., Kudo A.,
RA   Amann E.;
RT   "Molecular cloning and characterization of OB-cadherin, a new member of
RT   cadherin family expressed in osteoblasts.";
RL   J. Biol. Chem. 269:12092-12098(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-373.
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 269-796 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=2059658; DOI=10.1091/mbc.2.4.261;
RA   Suzuki S., Sano K., Tanihara H.;
RT   "Diversity of the cadherin family: evidence for eight new cadherins in
RT   nervous tissue.";
RL   Cell Regul. 2:261-270(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 600-668.
RA   Kools P.F.J., Hogendoorn P.C.W., Bovee J.V.M.G., van Roy F.;
RT   "Alternative cadherin-11 transcripts encoding truncated adhesion molecules
RT   are detectable in both human cancer and normal cells.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   CHROMOSOMAL TRANSLOCATION WITH USP6.
RX   PubMed=15026324; DOI=10.1158/0008-5472.can-03-2827;
RA   Oliveira A.M., Hsi B.L., Weremowicz S., Rosenberg A.E., Dal Cin P.,
RA   Joseph N., Bridge J.A., Perez-Atayde A.R., Fletcher J.A.;
RT   "USP6 (Tre2) fusion oncogenes in aneurysmal bone cyst.";
RL   Cancer Res. 64:1920-1923(2004).
RN   [8]
RP   INVOLVEMENT IN ESWS.
RX   PubMed=28988429; DOI=10.1002/ajmg.a.38495;
RA   Taskiran E.Z., Karaosmanoglu B., Kosukcu C., Dogan O.A.,
RA   Taylan-Sekeroglu H., Simsek-Kiper P.O., Utine E.G., Boduroglu K.,
RA   Alikasifoglu M.;
RT   "Homozygous indel mutation in CDH11 as the probable cause of Elsahy-Waters
RT   syndrome.";
RL   Am. J. Med. Genet. A 173:3143-3152(2017).
RN   [9]
RP   INVOLVEMENT IN ESWS, AND VARIANT ESWS 232-TYR--SER-796 DEL.
RX   PubMed=29271567; DOI=10.1002/ajmg.a.38568;
RA   Harms F.L., Nampoothiri S., Anazi S., Yesodharan D., Alawi M., Kutsche K.,
RA   Alkuraya F.S.;
RT   "Elsahy-Waters syndrome is caused by biallelic mutations in CDH11.";
RL   Am. J. Med. Genet. A 176:477-482(2018).
RN   [10]
RP   VARIANTS TBHS2 SER-55; LYS-140; ASN-260; GLU-260; ILE-262; LEU-266;
RP   GLN-279; TRP-327 AND GLU-374, INVOLVEMENT IN TBHS2, CHARACTERIZATION OF
RP   VARIANTS TBHS2 SER-55; LYS-140; ASN-260; ILE-262; GLN-279 AND TRP-327,
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=33811546; DOI=10.1007/s00439-021-02274-3;
RA   Li D., March M.E., Fortugno P., Cox L.L., Matsuoka L.S., Monetta R.,
RA   Seiler C., Pyle L.C., Bedoukian E.C., Sanchez-Soler M.J., Caluseriu O.,
RA   Grand K., Tam A., Aycinena A.R.P., Camerota L., Guo Y., Sleiman P.,
RA   Callewaert B., Kumps C., Dheedene A., Buckley M., Kirk E.P., Turner A.,
RA   Kamien B., Patel C., Wilson M., Roscioli T., Christodoulou J., Cox T.C.,
RA   Zackai E.H., Brancati F., Hakonarson H., Bhoj E.J.;
RT   "Pathogenic variants in CDH11 impair cell adhesion and cause Teebi
RT   hypertelorism syndrome.";
RL   Hum. Genet. 140:1061-1076(2021).
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. Required for proper focal adhesion assembly
CC       (PubMed:33811546). Involved in the regulation of cell migration
CC       (PubMed:33811546). {ECO:0000269|PubMed:33811546}.
CC   -!- SUBUNIT: Interacts with PCDH8. {ECO:0000250}.
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=P55287-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P55287-2; Sequence=VSP_000640, VSP_000641;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in brain but also found in other
CC       tissues. Expressed in neuroblasts. In the embryo from 67 to 72 days of
CC       gestation, detected at high levels in facial mesenchyme including the
CC       central palatal mesenchyme, dental mesenchyme, the eye and optic
CC       muscle, and the tongue (at protein level) (PubMed:33811546).
CC       {ECO:0000269|PubMed:33811546}.
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: Note=A chromosomal aberration involving CDH11 is a common
CC       genetic feature of aneurysmal bone cyst, a benign osseous neoplasm.
CC       Translocation t(16;17)(q22;p13) with USP6. The translocation generates
CC       a fusion gene in which the strong CDH11 promoter is fused to the entire
CC       USP6 coding sequence, resulting in USP6 transcriptional up-regulation.
CC   -!- DISEASE: Elsahy-Waters syndrome (ESWS) [MIM:211380]: An autosomal
CC       recessive syndrome characterized by moderate intellectual disability,
CC       hypospadias and characteristic craniofacial morphology, which includes
CC       brachycephaly, facial asymmetry, exotropia, hypertelorism, telechantus,
CC       broad nose, concave nasal ridge, underdeveloped mid-face, prognathism,
CC       and radicular dentin dysplasia. {ECO:0000269|PubMed:28988429,
CC       ECO:0000269|PubMed:29271567}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Teebi hypertelorism syndrome 2 (TBHS2) [MIM:619736]: A form of
CC       Teebi hypertelorism syndrome, a syndrome characterized by an abnormally
CC       increased distance between ocular orbits, and facial features that can
CC       resemble craniofrontonasal dysplasia such as prominent forehead,
CC       widow's peak, heavy and broad eyebrows, long palpebral fissures,
CC       ptosis, high and broad nasal bridge, short nose, low-set ears, natal
CC       teeth, thin upper lip and a grooved chin. Some affected individuals
CC       have limb, urogenital, umbilical and cardiac defects. Developmental
CC       delay and/or impaired intellectual development have been observed in
CC       some patients. TBHS2 inheritance is autosomal dominant.
CC       {ECO:0000269|PubMed:33811546}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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DR   EMBL; L34056; AAA35622.1; -; mRNA.
DR   EMBL; D21254; BAA04798.1; -; mRNA.
DR   EMBL; D21255; BAA04799.1; -; mRNA.
DR   EMBL; AK291251; BAF83940.1; -; mRNA.
DR   EMBL; AC010533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF060370; AAD27755.1; -; Genomic_DNA.
DR   EMBL; AF060369; AAD27755.1; JOINED; Genomic_DNA.
DR   EMBL; AF060370; AAD27756.1; -; Genomic_DNA.
DR   EMBL; AF060369; AAD27756.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS10803.1; -. [P55287-1]
DR   CCDS; CCDS81993.1; -. [P55287-2]
DR   PIR; A38992; A38992.
DR   RefSeq; NP_001295321.1; NM_001308392.2. [P55287-2]
DR   RefSeq; NP_001788.2; NM_001797.4. [P55287-1]
DR   RefSeq; XP_054235325.1; XM_054379350.1. [P55287-1]
DR   RefSeq; XP_054235326.1; XM_054379351.1. [P55287-2]
DR   AlphaFoldDB; P55287; -.
DR   SMR; P55287; -.
DR   BioGRID; 107444; 13.
DR   CORUM; P55287; -.
DR   FunCoup; P55287; 360.
DR   IntAct; P55287; 23.
DR   NDEx; IQUERY-CP-CDH11; 8 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000268603; -.
DR   DrugBank; DB00482; Celecoxib.
DR   GlyCosmos; P55287; 4 sites, 3 glycans.
DR   GlyGen; P55287; 5 sites, 3 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P55287; -.
DR   PhosphoSitePlus; P55287; -.
DR   BioMuta; CDH11; -.
DR   DMDM; 146345381; -.
DR   jPOST; P55287; -.
DR   MassIVE; P55287; -.
DR   PaxDb; 9606-ENSP00000268603; -.
DR   PeptideAtlas; P55287; -.
DR   ProteomicsDB; 56837; -. [P55287-1]
DR   ProteomicsDB; 56838; -. [P55287-2]
DR   ABCD; P55287; 16 sequenced antibodies.
DR   Antibodypedia; 4584; 905 antibodies from 41 providers.
DR   DNASU; 1009; -.
DR   Ensembl; ENST00000268603.9; ENSP00000268603.4; ENSG00000140937.15. [P55287-1]
DR   Ensembl; ENST00000394156.7; ENSP00000377711.3; ENSG00000140937.15. [P55287-2]
DR   GeneID; 1009; -.
DR   KEGG; hsa:1009; -.
DR   MANE-Select; ENST00000268603.9; ENSP00000268603.4; NM_001797.4; NP_001788.2.
DR   UCSC; uc002eoi.4; human. [P55287-1]
DR   AGR; HGNC:1750; -.
DR   ClinPGx; PA26284; -.
DR   CTD; 1009; -.
DR   DisGeNET; 1009; -.
DR   GeneCards; CDH11; -.
DR   HGNC; HGNC:1750; CDH11.
DR   HPA; ENSG00000140937; Tissue enhanced (ovary, placenta).
DR   MalaCards; CDH11; -.
DR   MIM; 211380; phenotype.
DR   MIM; 600023; gene.
DR   MIM; 619736; phenotype.
DR   OpenTargets; ENSG00000140937; -.
DR   Orphanet; 1299; Branchioskeletogenital syndrome.
DR   VEuPathDB; HostDB:ENSG00000140937; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000153691; -.
DR   HOGENOM; CLU_005284_4_3_1; -.
DR   InParanoid; P55287; -.
DR   OMA; AAEIXIV; -.
DR   OrthoDB; 8188793at2759; -.
DR   PAN-GO; P55287; 10 GO annotations based on evolutionary models.
DR   PhylomeDB; P55287; -.
DR   PathwayCommons; P55287; -.
DR   Reactome; R-HSA-418990; Adherens junctions interactions.
DR   Reactome; R-HSA-9759811; Regulation of CDH11 mRNA translation by microRNAs. [P55287-2]
DR   Reactome; R-HSA-9762292; Regulation of CDH11 function. [P55287-2]
DR   Reactome; R-HSA-9833576; CDH11 homotypic and heterotypic interactions.
DR   Reactome; R-HSA-9958810; SRC activates STAT3 in a quantitative manner, through Cadherin-11 (CDH11), RAC1 and gp130 (IL6ST).
DR   Reactome; R-HSA-9958825; Activation of STAT3 by cadherin engagement.
DR   SignaLink; P55287; -.
DR   SIGNOR; P55287; -.
DR   Agora; ENSG00000140937; -.
DR   BioGRID-ORCS; 1009; 16 hits in 1149 CRISPR screens.
DR   ChiTaRS; CDH11; human.
DR   GeneWiki; CDH11; -.
DR   GenomeRNAi; 1009; -.
DR   Pharos; P55287; Tbio.
DR   PRO; PR:P55287; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P55287; protein.
DR   Bgee; ENSG00000140937; Expressed in periodontal ligament and 195 other cell types or tissues.
DR   ExpressionAtlas; P55287; 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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR   GO; GO:0003189; P:aortic valve formation; ISS:BHF-UCL.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0016477; P:cell migration; ISS: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:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
DR   GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; IEA:InterPro.
DR   GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0001503; P:ossification; NAS:UniProtKB.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   CDD; cd11304; Cadherin_repeat; 4.
DR   FunFam; 4.10.900.10:FF:000001; Cadherin 2; 1.
DR   FunFam; 2.60.40.60:FF:000008; Cadherin 24; 1.
DR   FunFam; 2.60.40.60:FF:000009; Cadherin 24; 1.
DR   FunFam; 2.60.40.60:FF:000012; Cadherin 24; 1.
DR   FunFam; 2.60.40.60:FF:000017; Cadherin 24; 1.
DR   FunFam; 2.60.40.60:FF:000014; Cadherin 8; 1.
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; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027:SF85; CADHERIN-11; 1.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 4.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin-like; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Chromosomal rearrangement; Cleavage on pair of basic residues; Deafness;
KW   Disease variant; Glycoprotein; Intellectual disability; Membrane;
KW   Metal-binding; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..53
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003785"
FT   CHAIN           54..796
FT                   /note="Cadherin-11"
FT                   /id="PRO_0000003786"
FT   TOPO_DOM        54..617
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        618..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        641..796
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          54..159
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          160..268
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          269..383
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          384..486
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          487..612
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   MOD_RES         788
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55288"
FT   MOD_RES         791
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P55288"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        540
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         632..693
FT                   /note="VIVVLFVTLRRQKKEPLIVFEEEDVRENIITYDDEGGGEEDTEAFDIATLQN
FT                   PDGINGFIPR -> GCPSLMEPPSPREDMRLLYLGFQLMLFSYVKVNRRFCLLGVFIKL
FT                   PFLYVVATESPTTLTSL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8163513"
FT                   /id="VSP_000640"
FT   VAR_SEQ         694..796
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8163513"
FT                   /id="VSP_000641"
FT   VARIANT         55
FT                   /note="W -> S (in TBHS2; results in loss of cell adhesion
FT                   as shown by a cell-substrate adhesion assay;
FT                   dbSNP:rs2142528709)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086894"
FT   VARIANT         140
FT                   /note="E -> K (in TBHS2; results in loss of cell adhesion
FT                   as shown by a cell-substrate adhesion assay)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086895"
FT   VARIANT         232..796
FT                   /note="Missing (in ESWS)"
FT                   /evidence="ECO:0000269|PubMed:29271567"
FT                   /id="VAR_080481"
FT   VARIANT         255
FT                   /note="T -> M (in dbSNP:rs35195)"
FT                   /id="VAR_031945"
FT   VARIANT         260
FT                   /note="D -> E (in TBHS2; dbSNP:rs1000294766)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086896"
FT   VARIANT         260
FT                   /note="D -> N (in TBHS2; results in decreased cell adhesion
FT                   as shown by a cell-substrate adhesion assay;
FT                   dbSNP:rs2142492118)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086897"
FT   VARIANT         262
FT                   /note="N -> I (in TBHS2; results in decreased cell adhesion
FT                   as shown by a cell-substrate adhesion assay)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086898"
FT   VARIANT         266
FT                   /note="P -> L (in TBHS2; dbSNP:rs1426094439)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086899"
FT   VARIANT         275
FT                   /note="M -> I (in dbSNP:rs1130821)"
FT                   /evidence="ECO:0000269|PubMed:8163513"
FT                   /id="VAR_031946"
FT   VARIANT         279
FT                   /note="E -> Q (in TBHS2; results in increased cell
FT                   migration as shown by an in vitro wound closure assay using
FT                   patient cells; dbSNP:rs2142481275)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086900"
FT   VARIANT         327
FT                   /note="G -> W (in TBHS2; results in loss of cell adhesion
FT                   as shown by a cell-substrate adhesion assay;
FT                   dbSNP:rs2142480699)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086901"
FT   VARIANT         373
FT                   /note="S -> A (in dbSNP:rs35213)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:8163513"
FT                   /id="VAR_031947"
FT   VARIANT         374
FT                   /note="V -> E (in TBHS2; dbSNP:rs2142459670)"
FT                   /evidence="ECO:0000269|PubMed:33811546"
FT                   /id="VAR_086902"
FT   CONFLICT        271..272
FT                   /note="SV -> RL (in Ref. 1; AAA35622 and 5; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340
FT                   /note="K -> E (in Ref. 1; AAA35622 and 5; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471
FT                   /note="K -> Q (in Ref. 1; AAA35622 and 5; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   796 AA;  87965 MW;  E17090EC95C59936 CRC64;
     MKENYCLQAA LVCLGMLCHS HAFAPERRGH LRPSFHGHHE KGKEGQVLQR SKRGWVWNQF
     FVIEEYTGPD PVLVGRLHSD IDSGDGNIKY ILSGEGAGTI FVIDDKSGNI HATKTLDREE
     RAQYTLMAQA VDRDTNRPLE PPSEFIVKVQ DINDNPPEFL HETYHANVPE RSNVGTSVIQ
     VTASDADDPT YGNSAKLVYS ILEGQPYFSV EAQTGIIRTA LPNMDREAKE EYHVVIQAKD
     MGGHMGGLSG TTKVTITLTD VNDNPPKFPQ SVYQMSVSEA AVPGEEVGRV KAKDPDIGEN
     GLVTYNIVDG DGMESFEITT DYETQEGVIK LKKPVDFETK RAYSLKVEAA NVHIDPKFIS
     NGPFKDTVTV KISVEDADEP PMFLAPSYIH EVQENAAAGT VVGRVHAKDP DAANSPIRYS
     IDRHTDLDRF FTINPEDGFI KTTKPLDREE TAWLNITVFA AEIHNRHQEA KVPVAIRVLD
     VNDNAPKFAA PYEGFICESD QTKPLSNQPI VTISADDKDD TANGPRFIFS LPPEIIHNPN
     FTVRDNRDNT AGVYARRGGF SRQKQDLYLL PIVISDGGIP PMSSTNTLTI KVCGCDVNGA
     LLSCNAEAYI LNAGLSTGAL IAILACIVIL LVIVVLFVTL RRQKKEPLIV FEEEDVRENI
     ITYDDEGGGE EDTEAFDIAT LQNPDGINGF IPRKDIKPEY QYMPRPGLRP APNSVDVDDF
     INTRIQEADN DPTAPPYDSI QIYGYEGRGS VAGSLSSLES ATTDSDLDYD YLQNWGPRFK
     KLADLYGSKD TFDDDS
//