ID B3DGG4_DANRE Unreviewed; 800 AA. AC B3DGG4; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 22-APR-2020, entry version 100. DE SubName: Full=Cadherin 11, osteoblast {ECO:0000313|EMBL:AAI63442.1}; DE SubName: Full=Cadherin 11, type 2, OB-cadherin (osteoblast) {ECO:0000313|Ensembl:ENSDARP00000006449}; DE SubName: Full=Cdh11 protein {ECO:0000313|EMBL:AAI62388.1}; GN Name=cdh11 {ECO:0000313|EMBL:AAI62388.1, GN ECO:0000313|Ensembl:ENSDARP00000006449, GN ECO:0000313|ZFIN:ZDB-GENE-980526-170}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI62388.1}; RN [1] {ECO:0000313|EMBL:AAI62388.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSDARP00000006449} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000006449}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSDARP00000006449, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000006449, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [4] {ECO:0000313|Ensembl:ENSDARP00000151942} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000143868}; RG Ensembl; RL Submitted (APR-2018) to UniProtKB. CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. CC {ECO:0000256|RuleBase:RU004357}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU003318, CC ECO:0000256|SAAS:SAAS00544042}; Single-pass type I membrane protein CC {ECO:0000256|RuleBase:RU003318, ECO:0000256|SAAS:SAAS00544042}. 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; CT025913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC162388; AAI62388.1; -; mRNA. DR EMBL; BC162403; AAI62403.1; -; mRNA. DR EMBL; BC163442; AAI63442.1; -; mRNA. DR RefSeq; NP_571289.1; NM_131214.1. DR RefSeq; XP_005166503.1; XM_005166446.3. DR STRING; 7955.ENSDARP00000006449; -. DR Ensembl; ENSDART00000002279; ENSDARP00000006449; ENSDARG00000021442. DR Ensembl; ENSDART00000174592; ENSDARP00000143868; ENSDARG00000021442. DR Ensembl; ENSDART00000179758; ENSDARP00000153918; ENSDARG00000021442. DR Ensembl; ENSDART00000183602; ENSDARP00000151942; ENSDARG00000021442. DR GeneID; 30461; -. DR KEGG; dre:30461; -. DR CTD; 1009; -. DR ZFIN; ZDB-GENE-980526-170; cdh11. DR eggNOG; KOG3594; Eukaryota. DR eggNOG; ENOG410XQHI; LUCA. DR GeneTree; ENSGT00940000153691; -. DR HOGENOM; CLU_005284_3_1_1; -. DR KO; K06803; -. DR OMA; HENYHAN; -. DR OrthoDB; 188978at2759; -. DR TreeFam; TF329887; -. DR Reactome; R-DRE-418990; Adherens junctions interactions. DR Proteomes; UP000000437; Chromosome 7. DR Bgee; ENSDARG00000021442; Expressed in multi-cellular organism and 25 other tissues. DR GO; GO:0005912; C:adherens junction; IBA:GO_Central. DR GO; GO:0016342; C:catenin complex; IBA:GO_Central. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0008092; F:cytoskeletal protein 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:0000902; P:cell morphogenesis; IBA:GO_Central. DR GO; GO:0098609; P:cell-cell adhesion; 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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central. DR GO; GO:0007275; P:multicellular organism development; IBA:GO_Central. DR GO; GO:0048840; P:otolith development; IMP:ZFIN. DR GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:ZFIN. DR Gene3D; 4.10.900.10; -; 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_cytoplasmic-dom. DR InterPro; IPR027397; Catenin_binding_dom_sf. DR PANTHER; PTHR24027; PTHR24027; 1. DR Pfam; PF00028; Cadherin; 5. 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; 2. PE 2: Evidence at transcript level; KW Calcium {ECO:0000256|RuleBase:RU003318, ECO:0000256|SAAS:SAAS00020193}; KW Cell adhesion {ECO:0000256|RuleBase:RU003318, KW ECO:0000256|SAAS:SAAS00307165}; KW Cell membrane {ECO:0000256|SAAS:SAAS00307127}; KW Membrane {ECO:0000256|SAAS:SAAS00020159, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Repeat {ECO:0000256|SAAS:SAAS00226229}; Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU003318, KW ECO:0000256|SAAS:SAAS00556032, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00554877, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..800 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015087193" FT TRANSMEM 613..644 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 84..165 FT /note="CA" FT /evidence="ECO:0000259|SMART:SM00112" FT DOMAIN 189..274 FT /note="CA" FT /evidence="ECO:0000259|SMART:SM00112" FT DOMAIN 298..390 FT /note="CA" FT /evidence="ECO:0000259|SMART:SM00112" FT DOMAIN 413..494 FT /note="CA" FT /evidence="ECO:0000259|SMART:SM00112" FT DOMAIN 517..604 FT /note="CA" FT /evidence="ECO:0000259|SMART:SM00112" FT REGION 27..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..46 FT /note="Basic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 800 AA; 88933 MW; 25B84ABE5598810B CRC64; MWEGLRLQVF FLCLGAALWS AAAAATHRGS GPRERGHRRH LSLHRHRERG KEGQVLHRSK RGWVWNQFFV IEEYTGPDPV LVGRLHSDVD SGDGNIKYIL SGEGAGTIFV IDDKTGNIHA TKTLDREEQA QYTLTAQAVA RDTNKPLEPP SEFIVKVQDI NDNPPEFLHG PYYARVAEMS NVGTSVIKVT ATDADDPTYG NSARLVYSIL QGQPYFSVEP QTGIIRTALP NMDREARQEY DVVIQAKDMG GHMGGLSGTT QVKITLTDVN DNPPKFAQGV YAMAVSEDKV PGEEVGRLKA RDPDLAENGL VDYRILEGDG MNYFEITKDS ETQEAVIKLK KPVDFETKRS YTLKVEATNT HVDPRFIAWG PYKDTTIVKI SVEDADEPPT FMAPSYNFEV EENAPAGTLV GRVHAKDTDM MNNPIRYMIP HYTDLEEFFT INPEDGIIKT TRPLDREAQA WHNISVSATE IGGHHQDAKV RVNIKVKDVN DNAPEFATQN EVLVCENVNP GKLIETVSAT DKDEMAHRQH FHFSLAPEVA NNHSFSLKDN RDSTASIFVI RKGFSRMTQD IYHLPIEIND NGVPPMSSTN TLIIRVCSCD SKDTILSCNV EPFILTAGLS TGALIAILAC IVILLAIVVL FVALRRQKKE PLIVFEEEDI RENIITYDDE GGGEEDTEAF DIATLQNPDG ANGFLPRKDM KPELQYGMRP GLRPIGNSVD VDDFIKTRIS DADNDPTAPP YDSIQIYGYE GRGSIAGSLS SLESVTTDSD LDYDYLQSWG PRFKKLADLY GTKDSVDDNS //