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   08-JUN-2016, entry version 139.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=7982033;
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
RP   AND ALA-373.
RC   TISSUE=Osteosarcoma;
RX   PubMed=8163513;
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
RT   of 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
RP   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   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.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   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;
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
RT   molecules 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).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types.
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
CC       other tissues. Expressed in neuroblasts.
CC   -!- DOMAIN: Three calcium ions are usually bound at the interface of
CC       each cadherin domain and rigidify the connections, imparting a
CC       strong 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
CC       neoplasm. Translocation t(16;17)(q22;p13) with USP6. The
CC       translocation generates a fusion gene in which the strong CDH11
CC       promoter is fused to the entire USP6 coding sequence, resulting in
CC       USP6 transcriptional up-regulation.
CC   -!- SIMILARITY: Contains 5 cadherin domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00043}.
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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   PIR; A38992; A38992.
DR   RefSeq; NP_001295321.1; NM_001308392.1. [P55287-2]
DR   RefSeq; NP_001788.2; NM_001797.3. [P55287-1]
DR   RefSeq; XP_005255818.1; XM_005255761.2. [P55287-1]
DR   RefSeq; XP_005255819.1; XM_005255762.1. [P55287-1]
DR   RefSeq; XP_005255820.1; XM_005255763.1. [P55287-1]
DR   RefSeq; XP_011521105.1; XM_011522803.1. [P55287-1]
DR   UniGene; Hs.116471; -.
DR   UniGene; Hs.596112; -.
DR   ProteinModelPortal; P55287; -.
DR   SMR; P55287; 54-593, 691-787.
DR   BioGrid; 107444; 2.
DR   IntAct; P55287; 5.
DR   MINT; MINT-1180975; -.
DR   STRING; 9606.ENSP00000268603; -.
DR   iPTMnet; P55287; -.
DR   PhosphoSite; P55287; -.
DR   BioMuta; CDH11; -.
DR   DMDM; 146345381; -.
DR   MaxQB; P55287; -.
DR   PaxDb; P55287; -.
DR   PRIDE; P55287; -.
DR   Ensembl; ENST00000268603; ENSP00000268603; ENSG00000140937. [P55287-1]
DR   Ensembl; ENST00000394156; ENSP00000377711; ENSG00000140937. [P55287-2]
DR   GeneID; 1009; -.
DR   KEGG; hsa:1009; -.
DR   UCSC; uc002eoi.4; human. [P55287-1]
DR   CTD; 1009; -.
DR   GeneCards; CDH11; -.
DR   H-InvDB; HIX0013098; -.
DR   HGNC; HGNC:1750; CDH11.
DR   HPA; CAB013072; -.
DR   MIM; 600023; gene.
DR   neXtProt; NX_P55287; -.
DR   PharmGKB; PA26284; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   eggNOG; ENOG410XQHI; LUCA.
DR   GeneTree; ENSGT00760000118954; -.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; P55287; -.
DR   KO; K06803; -.
DR   OMA; HENYHAN; -.
DR   OrthoDB; EOG7GBFW7; -.
DR   PhylomeDB; P55287; -.
DR   TreeFam; TF329887; -.
DR   Reactome; R-HSA-418990; Adherens junctions interactions.
DR   SIGNOR; P55287; -.
DR   ChiTaRS; CDH11; human.
DR   GeneWiki; CDH11; -.
DR   GenomeRNAi; 1009; -.
DR   PRO; PR:P55287; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; P55287; -.
DR   CleanEx; HS_CDH11; -.
DR   ExpressionAtlas; P55287; baseline and differential.
DR   Genevisible; P55287; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0021957; P:corticospinal tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0001503; P:ossification; NAS:UniProtKB.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   Gene3D; 2.60.40.60; -; 5.
DR   Gene3D; 4.10.900.10; -; 1.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   InterPro; IPR027397; Catenin_binding_dom.
DR   Pfam; PF00028; Cadherin; 4.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; SSF49313; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Chromosomal rearrangement; Cleavage on pair of basic residues;
KW   Complete proteome; Glycoprotein; Membrane; Metal-binding;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23     53       {ECO:0000255}.
FT                                /FTId=PRO_0000003785.
FT   CHAIN        54    796       Cadherin-11.
FT                                /FTId=PRO_0000003786.
FT   TOPO_DOM     54    617       Extracellular. {ECO:0000255}.
FT   TRANSMEM    618    640       Helical. {ECO:0000255}.
FT   TOPO_DOM    641    796       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       54    159       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      160    268       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      269    383       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      384    486       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      487    612       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   MOD_RES     788    788       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P55288}.
FT   MOD_RES     791    791       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P55288}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    540    540       N-linked (GlcNAc...). {ECO:0000255}.
FT   VAR_SEQ     632    693       VIVVLFVTLRRQKKEPLIVFEEEDVRENIITYDDEGGGEED
FT                                TEAFDIATLQNPDGINGFIPR -> GCPSLMEPPSPREDMR
FT                                LLYLGFQLMLFSYVKVNRRFCLLGVFIKLPFLYVVATESPT
FT                                TLTSL (in isoform 2).
FT                                {ECO:0000303|PubMed:8163513}.
FT                                /FTId=VSP_000640.
FT   VAR_SEQ     694    796       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:8163513}.
FT                                /FTId=VSP_000641.
FT   VARIANT     255    255       T -> M (in dbSNP:rs35195).
FT                                /FTId=VAR_031945.
FT   VARIANT     275    275       M -> I (in dbSNP:rs1130821).
FT                                {ECO:0000269|PubMed:8163513}.
FT                                /FTId=VAR_031946.
FT   VARIANT     373    373       S -> A (in dbSNP:rs35213).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:8163513}.
FT                                /FTId=VAR_031947.
FT   CONFLICT    271    272       SV -> RL (in Ref. 1; AAA35622 and 5; no
FT                                nucleotide entry). {ECO:0000305}.
FT   CONFLICT    340    340       K -> E (in Ref. 1; AAA35622 and 5; no
FT                                nucleotide entry). {ECO:0000305}.
FT   CONFLICT    471    471       K -> Q (in Ref. 1; AAA35622 and 5; no
FT                                nucleotide entry). {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
//