ID   CDON_MOUSE              Reviewed;        1250 AA.
AC   Q32MD9; E9QKV9; O88971;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Cell adhesion molecule-related/down-regulated by oncogenes;
DE   Flags: Precursor;
GN   Name=Cdon; Synonyms=Cdo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=9786951; DOI=10.1083/jcb.143.2.403;
RA   Kang J.-S., Mulieri P.J., Miller C., Sassoon D.A., Krauss R.S.;
RT   "CDO, a robo-related cell surface protein that mediates myogenic
RT   differentiation.";
RL   J. Cell Biol. 143:403-413(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   IDENTIFICATION IN A COMPLEX WITH NEO1 AND CADHERINS, AND FUNCTION.
RX   PubMed=15520228; DOI=10.1083/jcb.200405039;
RA   Kang J.-S., Yi M.J., Zhang W., Feinleib J.L., Cole F., Krauss R.S.;
RT   "Netrins and neogenin promote myotube formation.";
RL   J. Cell Biol. 167:493-504(2004).
CC   -!- FUNCTION: Component of a cell-surface receptor complex that mediates
CC       cell-cell interactions between muscle precursor cells. Promotes
CC       differentiation of myogenic cells. Required for response to NTN3 and
CC       activation of NFATC3. {ECO:0000269|PubMed:15520228,
CC       ECO:0000269|PubMed:9786951}.
CC   -!- SUBUNIT: Part of a complex that contains BOC, CDON, NEO1, cadherins and
CC       CTNNB1. Interacts with NTN3. Interacts with DHH, IHH and SHH (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q32MD9; P00520: Abl1; NbExp=2; IntAct=EBI-7017034, EBI-914519;
CC       Q32MD9; Q01721: Gas1; NbExp=3; IntAct=EBI-7017034, EBI-15729104;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in somites and the dorsal lips of
CC       the neural tube during embryogenesis. Detected at very low levels in
CC       adult tissues. {ECO:0000269|PubMed:9786951}.
CC   -!- INDUCTION: Transiently up-regulated during myoblast differentiation.
CC       {ECO:0000269|PubMed:9786951}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
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DR   EMBL; AF090866; AAC43031.1; -; mRNA.
DR   EMBL; AC118232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC109176; AAI09177.1; -; mRNA.
DR   CCDS; CCDS22964.1; -.
DR   RefSeq; NP_067314.2; NM_021339.2.
DR   RefSeq; XP_006510570.1; XM_006510507.3.
DR   RefSeq; XP_006510571.1; XM_006510508.3.
DR   RefSeq; XP_006510572.1; XM_006510509.3.
DR   RefSeq; XP_006510573.1; XM_006510510.3.
DR   RefSeq; XP_006510574.1; XM_006510511.3.
DR   RefSeq; XP_011240883.1; XM_011242581.2.
DR   AlphaFoldDB; Q32MD9; -.
DR   SMR; Q32MD9; -.
DR   BioGRID; 208333; 5.
DR   DIP; DIP-57227N; -.
DR   IntAct; Q32MD9; 7.
DR   MINT; Q32MD9; -.
DR   STRING; 10090.ENSMUSP00000113977; -.
DR   GlyCosmos; Q32MD9; 8 sites, No reported glycans.
DR   GlyGen; Q32MD9; 8 sites.
DR   iPTMnet; Q32MD9; -.
DR   PhosphoSitePlus; Q32MD9; -.
DR   PaxDb; 10090-ENSMUSP00000113977; -.
DR   PeptideAtlas; Q32MD9; -.
DR   ProteomicsDB; 281443; -.
DR   Pumba; Q32MD9; -.
DR   Antibodypedia; 2227; 223 antibodies from 30 providers.
DR   DNASU; 57810; -.
DR   Ensembl; ENSMUST00000042842.6; ENSMUSP00000045547.6; ENSMUSG00000038119.16.
DR   Ensembl; ENSMUST00000119129.10; ENSMUSP00000113977.2; ENSMUSG00000038119.16.
DR   GeneID; 57810; -.
DR   KEGG; mmu:57810; -.
DR   UCSC; uc009ote.2; mouse.
DR   AGR; MGI:1926387; -.
DR   CTD; 50937; -.
DR   MGI; MGI:1926387; Cdon.
DR   VEuPathDB; HostDB:ENSMUSG00000038119; -.
DR   eggNOG; ENOG502QT4P; Eukaryota.
DR   GeneTree; ENSGT00940000157114; -.
DR   HOGENOM; CLU_008503_0_0_1; -.
DR   InParanoid; Q32MD9; -.
DR   OMA; NGCAHLH; -.
DR   OrthoDB; 3138076at2759; -.
DR   PhylomeDB; Q32MD9; -.
DR   TreeFam; TF332268; -.
DR   Reactome; R-MMU-525793; Myogenesis.
DR   Reactome; R-MMU-5632681; Ligand-receptor interactions.
DR   Reactome; R-MMU-5635838; Activation of SMO.
DR   BioGRID-ORCS; 57810; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Cdo1; mouse.
DR   PRO; PR:Q32MD9; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q32MD9; Protein.
DR   Bgee; ENSMUSG00000038119; Expressed in vestibular membrane of cochlear duct and 241 other cell types or tissues.
DR   ExpressionAtlas; Q32MD9; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR   GO; GO:0001708; P:cell fate specification; IGI:MGI.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0010172; P:embryonic body morphogenesis; IMP:MGI.
DR   GO; GO:0048598; P:embryonic morphogenesis; IGI:MGI.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR   GO; GO:0007520; P:myoblast fusion; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; TAS:UniProtKB.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
DR   GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IMP:MGI.
DR   GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0016202; P:regulation of striated muscle tissue development; ISO:MGI.
DR   GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR   GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd00096; Ig; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 8.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   PANTHER; PTHR44170:SF30; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 3.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   Genevisible; Q32MD9; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1250
FT                   /note="Cell adhesion molecule-related/down-regulated by
FT                   oncogenes"
FT                   /id="PRO_0000234055"
FT   TOPO_DOM        25..962
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        963..983
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        984..1250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..113
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          119..203
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          224..302
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          309..395
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          404..515
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          572..673
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          719..814
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          822..922
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          524..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          929..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1178..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1223..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        869
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        140..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        242..289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        332..379
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        425..499
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        368
FT                   /note="R -> G (in Ref. 1; AAC43031 and 3; AAI09177)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        381
FT                   /note="A -> P (in Ref. 1; AAC43031)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        456
FT                   /note="P -> S (in Ref. 3; AAI09177)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        542
FT                   /note="Q -> R (in Ref. 1; AAC43031 and 3; AAI09177)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="R -> K (in Ref. 1; AAC43031 and 3; AAI09177)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        689
FT                   /note="V -> L (in Ref. 1; AAC43031)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1250 AA;  135422 MW;  11ECD241176C2BFC CRC64;
     MHPDLGPLWT LLYVLVILCS SVSSDLAPYF ISEPLSAVQK LGRPVVLHCS AKPVTARISW
     LHNGKRLDRN TEQIKIHRGT LTILSLNPSL SGCYQCVANN SVGAVVSGPA TVSAAALGDF
     DSSTMHVITA EEKNTGFIGC RVPESNPKAE VRYKIRGKWL KHSTGNYIIL PSGNLQVLNV
     SSKDKGSYKC AAYNPVTSEL KVEPTGRKLL VSRPSSNGFH ILHPALSQAL AVLPHSPVTL
     ECVVSGVPAS QVYWLKDGQD AVAGSNWRRL YSHLATASID PADSGNYSCV VGNKSGDVKH
     VTYMVNVLEH ASISKGLHDQ KVSLGATVHF TCDVHGNPAP NRTWFHNAQP IHPSSRHLTE
     GNVLKITRVV MEDSGLYQCV ADNGIGFMQS TGRLQIEQDS GWKPVIVTAP ANIEVMDGDF
     VTLSCNATGV PVPVIHWYGR HGLITSHPSQ VLRSKPRKSH LFRPGDLDLE PVYLIMSQAG
     SSSLSIQAVT LEHAGKYTCE ATNKHGSTQS EAFLTVVPFE TNTKAESVTP SEASQNDERD
     PQDGSESSLL NLFPVKVHPS GVELPAERNA SVPDAPNILS PPQTHMPDTY NLVWRAGRDG
     GMPINAYFVK YRKLDDGSGA VGSWHTVRVP GSENELHLTE LEPSSLYEVL MVARSAVGEG
     QPAMLTFRTS KEKMASSKNT QASFPPVGVP KRPVTAEASN SNFGVVLTDS SRHSGVPEAP
     DRPTISMASE TSVYVTWIPR ANGGSPITAF KVEYKRMRTS DWLVAAEDIP PSKLSVEVRS
     LEPGSIYKFR VIAINHYGES FRSSASRPYQ VAGFPNRFSN RPITGPHIAY TEAVSDTQIM
     LKWTYVPSSN NNTPIQGFYI YYRPTDSDND SDYKRDVVEG SKQWHTIGHL QPETSYDIKM
     QCFNEGGESE FSNVMICETK VKRVPGASDY PVKELSTPPS SSGNAGNVGP ATSPARSSDM
     LYLIVGCVLG VMVLILMVFI ALCLWKSRQQ STIQKYDPPG YLYQGSEING QMVEYTTLSG
     AARINGSVHG GFLSNGCSHL HHKGPSGVNG TLSGNINGGL YSAHTNSLTR ACVEFEHPHH
     LVNSGGVYTA VPQMDPLECI NCRNCRNNNR CFTKTNSPLP VVPVVASYPQ GGLEMKPLNA
     MKVPVCPAST VPDHGQLPDD CVKDSVAPIP TQHTCCQDNI SDINSDSTED TAEFSRGDSS
     GHSEAEDKVF SWNPLILSPV LEDCGEKTAR SPPGPPLDGL SVVLQQAQET
//