CDON_MOUSE
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 03-AUG-2022, entry version 131.
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; 3.
DR DIP; DIP-57227N; -.
DR IntAct; Q32MD9; 7.
DR MINT; Q32MD9; -.
DR STRING; 10090.ENSMUSP00000113977; -.
DR GlyGen; Q32MD9; 8 sites.
DR iPTMnet; Q32MD9; -.
DR PhosphoSitePlus; Q32MD9; -.
DR PaxDb; Q32MD9; -.
DR PeptideAtlas; Q32MD9; -.
DR PRIDE; Q32MD9; -.
DR ProteomicsDB; 281443; -.
DR Antibodypedia; 2227; 204 antibodies from 30 providers.
DR DNASU; 57810; -.
DR Ensembl; ENSMUST00000042842; ENSMUSP00000045547; ENSMUSG00000038119.
DR Ensembl; ENSMUST00000119129; ENSMUSP00000113977; ENSMUSG00000038119.
DR GeneID; 57810; -.
DR KEGG; mmu:57810; -.
DR UCSC; uc009ote.2; mouse.
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; 102649at2759; -.
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 73 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 238 other tissues.
DR ExpressionAtlas; Q32MD9; baseline and differential.
DR Genevisible; Q32MD9; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of 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: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:2000179; P:positive regulation of neural precursor cell 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:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0043393; P:regulation of protein binding; IDA: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 Gene3D; 2.60.40.10; -; 8.
DR InterPro; IPR032983; CDO.
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:SF1; PTHR44170:SF1; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
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
