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Q32MD9 (CDON_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell adhesion molecule-related/down-regulated by oncogenes
Gene names
Name:Cdon
Synonyms:Cdo
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1250 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells. Required for response to NTN3 and activation of NFATC3. Ref.1 Ref.4

Subunit structure

Part of a complex that contains BOC, CDON, NEO1, cadherins and CTNNB1. Interacts with NTN3. Interacts with DHH, IHH and SHH By similarity. Ref.4

Subcellular location

Cell membrane; Single-pass membrane protein By similarity.

Tissue specificity

Highly expressed in somites and the dorsal lips of the neural tube during embryogenesis. Detected at very low levels in adult tissues. Ref.1

Induction

Transiently up-regulated during myoblast differentiation. Ref.1

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Contains 3 fibronectin type-III domains.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from mutant phenotype PubMed 19754878. Source: MGI

cell fate specification

Inferred from genetic interaction PubMed 16647304. Source: MGI

cerebral cortex development

Inferred from mutant phenotype PubMed 16648472. Source: MGI

embryonic body morphogenesis

Inferred from mutant phenotype PubMed 16647303. Source: MGI

embryonic morphogenesis

Inferred from genetic interaction PubMed 17504941. Source: MGI

embryonic retina morphogenesis in camera-type eye

Inferred from mutant phenotype PubMed 19754878. Source: MGI

lens development in camera-type eye

Inferred from mutant phenotype PubMed 19754878. Source: MGI

myoblast fusion

Inferred from mutant phenotype Ref.4. Source: MGI

positive regulation of MAPK cascade

Inferred from mutant phenotype PubMed 19244314. Source: MGI

positive regulation of myoblast differentiation

Traceable author statement PubMed 11782431. Source: UniProtKB

positive regulation of neural precursor cell proliferation

Inferred from mutant phenotype PubMed 16648472. Source: MGI

positive regulation of neuron differentiation

Inferred from direct assay PubMed 16648472. Source: MGI

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 15572127. Source: MGI

positive regulation of skeletal muscle tissue development

Inferred from mutant phenotype PubMed 15572127. Source: MGI

positive regulation of small GTPase mediated signal transduction

Inferred from mutant phenotype PubMed 19244314. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 15572127PubMed 16648472. Source: MGI

regulation of neuron differentiation

Inferred from mutant phenotype PubMed 16648472. Source: MGI

regulation of protein heterodimerization activity

Inferred from direct assay PubMed 15572127PubMed 16648472. Source: MGI

regulation of striated muscle tissue development

Inferred from sequence orthology PubMed 11782431. Source: MGI

satellite cell differentiation

Inferred from mutant phenotype PubMed 15572127. Source: MGI

single organismal cell-cell adhesion

Traceable author statement Ref.4. Source: UniProtKB

smoothened signaling pathway

Inferred from genetic interaction PubMed 16647304. Source: MGI

striated muscle cell differentiation

Inferred from genetic interaction PubMed 20160094. Source: MGI

   Cellular_componentcell surface

Traceable author statement Ref.4. Source: UniProtKB

integral component of plasma membrane

Inferred from sequence orthology PubMed 11782431. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11782431. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Abl1P005202EBI-7017034,EBI-914519

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 12501226Cell adhesion molecule-related/down-regulated by oncogenes
PRO_0000234055

Regions

Topological domain25 – 962938Extracellular Potential
Transmembrane963 – 98321Helical; Potential
Topological domain984 – 1250267Cytoplasmic Potential
Domain28 – 11386Ig-like C2-type 1
Domain119 – 20385Ig-like C2-type 2
Domain224 – 30279Ig-like C2-type 3
Domain309 – 39587Ig-like C2-type 4
Domain404 – 515112Ig-like C2-type 5
Domain572 – 673102Fibronectin type-III 1
Domain719 – 81496Fibronectin type-III 2
Domain822 – 922101Fibronectin type-III 3

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Glycosylation8691N-linked (GlcNAc...) Potential
Disulfide bond49 ↔ 96 By similarity
Disulfide bond140 ↔ 190 By similarity
Disulfide bond242 ↔ 289 By similarity
Disulfide bond332 ↔ 379 By similarity
Disulfide bond425 ↔ 499 By similarity

Experimental info

Sequence conflict3681R → G in AAC43031. Ref.1
Sequence conflict3681R → G in AAI09177. Ref.3
Sequence conflict3811A → P in AAC43031. Ref.1
Sequence conflict4561P → S in AAI09177. Ref.3
Sequence conflict5421Q → R in AAC43031. Ref.1
Sequence conflict5421Q → R in AAI09177. Ref.3
Sequence conflict5681R → K in AAC43031. Ref.1
Sequence conflict5681R → K in AAI09177. Ref.3
Sequence conflict6891V → L in AAC43031. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q32MD9 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 11ECD241176C2BFC

FASTA1,250135,422
        10         20         30         40         50         60 
MHPDLGPLWT LLYVLVILCS SVSSDLAPYF ISEPLSAVQK LGRPVVLHCS AKPVTARISW 

        70         80         90        100        110        120 
LHNGKRLDRN TEQIKIHRGT LTILSLNPSL SGCYQCVANN SVGAVVSGPA TVSAAALGDF 

       130        140        150        160        170        180 
DSSTMHVITA EEKNTGFIGC RVPESNPKAE VRYKIRGKWL KHSTGNYIIL PSGNLQVLNV 

       190        200        210        220        230        240 
SSKDKGSYKC AAYNPVTSEL KVEPTGRKLL VSRPSSNGFH ILHPALSQAL AVLPHSPVTL 

       250        260        270        280        290        300 
ECVVSGVPAS QVYWLKDGQD AVAGSNWRRL YSHLATASID PADSGNYSCV VGNKSGDVKH 

       310        320        330        340        350        360 
VTYMVNVLEH ASISKGLHDQ KVSLGATVHF TCDVHGNPAP NRTWFHNAQP IHPSSRHLTE 

       370        380        390        400        410        420 
GNVLKITRVV MEDSGLYQCV ADNGIGFMQS TGRLQIEQDS GWKPVIVTAP ANIEVMDGDF 

       430        440        450        460        470        480 
VTLSCNATGV PVPVIHWYGR HGLITSHPSQ VLRSKPRKSH LFRPGDLDLE PVYLIMSQAG 

       490        500        510        520        530        540 
SSSLSIQAVT LEHAGKYTCE ATNKHGSTQS EAFLTVVPFE TNTKAESVTP SEASQNDERD 

       550        560        570        580        590        600 
PQDGSESSLL NLFPVKVHPS GVELPAERNA SVPDAPNILS PPQTHMPDTY NLVWRAGRDG 

       610        620        630        640        650        660 
GMPINAYFVK YRKLDDGSGA VGSWHTVRVP GSENELHLTE LEPSSLYEVL MVARSAVGEG 

       670        680        690        700        710        720 
QPAMLTFRTS KEKMASSKNT QASFPPVGVP KRPVTAEASN SNFGVVLTDS SRHSGVPEAP 

       730        740        750        760        770        780 
DRPTISMASE TSVYVTWIPR ANGGSPITAF KVEYKRMRTS DWLVAAEDIP PSKLSVEVRS 

       790        800        810        820        830        840 
LEPGSIYKFR VIAINHYGES FRSSASRPYQ VAGFPNRFSN RPITGPHIAY TEAVSDTQIM 

       850        860        870        880        890        900 
LKWTYVPSSN NNTPIQGFYI YYRPTDSDND SDYKRDVVEG SKQWHTIGHL QPETSYDIKM 

       910        920        930        940        950        960 
QCFNEGGESE FSNVMICETK VKRVPGASDY PVKELSTPPS SSGNAGNVGP ATSPARSSDM 

       970        980        990       1000       1010       1020 
LYLIVGCVLG VMVLILMVFI ALCLWKSRQQ STIQKYDPPG YLYQGSEING QMVEYTTLSG 

      1030       1040       1050       1060       1070       1080 
AARINGSVHG GFLSNGCSHL HHKGPSGVNG TLSGNINGGL YSAHTNSLTR ACVEFEHPHH 

      1090       1100       1110       1120       1130       1140 
LVNSGGVYTA VPQMDPLECI NCRNCRNNNR CFTKTNSPLP VVPVVASYPQ GGLEMKPLNA 

      1150       1160       1170       1180       1190       1200 
MKVPVCPAST VPDHGQLPDD CVKDSVAPIP TQHTCCQDNI SDINSDSTED TAEFSRGDSS 

      1210       1220       1230       1240       1250 
GHSEAEDKVF SWNPLILSPV LEDCGEKTAR SPPGPPLDGL SVVLQQAQET 

« Hide

References

« Hide 'large scale' references
[1]"CDO, a robo-related cell surface protein that mediates myogenic differentiation."
Kang J.-S., Mulieri P.J., Miller C., Sassoon D.A., Krauss R.S.
J. Cell Biol. 143:403-413(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY.
Tissue: Embryo.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Netrins and neogenin promote myotube formation."
Kang J.-S., Yi M.J., Zhang W., Feinleib J.L., Cole F., Krauss R.S.
J. Cell Biol. 167:493-504(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH NEO1 AND CADHERINS, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF090866 mRNA. Translation: AAC43031.1.
AC118232 Genomic DNA. No translation available.
AC159894 Genomic DNA. No translation available.
BC109176 mRNA. Translation: AAI09177.1.
CCDSCCDS22964.1.
RefSeqNP_067314.2. NM_021339.2.
XP_006510570.1. XM_006510507.1.
XP_006510571.1. XM_006510508.1.
XP_006510572.1. XM_006510509.1.
XP_006510573.1. XM_006510510.1.
XP_006510574.1. XM_006510511.1.
UniGeneMm.80509.

3D structure databases

ProteinModelPortalQ32MD9.
SMRQ32MD9. Positions 26-920.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208333. 3 interactions.
DIPDIP-57227N.
IntActQ32MD9. 1 interaction.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ32MD9.

Proteomic databases

PRIDEQ32MD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042842; ENSMUSP00000045547; ENSMUSG00000038119.
ENSMUST00000119129; ENSMUSP00000113977; ENSMUSG00000038119.
GeneID57810.
KEGGmmu:57810.
UCSCuc009ote.2. mouse.

Organism-specific databases

CTD50937.
MGIMGI:1926387. Cdon.

Phylogenomic databases

eggNOGNOG150729.
GeneTreeENSGT00750000117685.
HOGENOMHOG000060072.
HOVERGENHBG081073.
InParanoidQ32MD9.
OMAVSDTQIM.
OrthoDBEOG7MD4PB.
TreeFamTF332268.

Gene expression databases

ArrayExpressQ32MD9.
BgeeQ32MD9.
GenevestigatorQ32MD9.

Family and domain databases

Gene3D2.60.40.10. 9 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF00041. fn3. 3 hits.
PF07679. I-set. 3 hits.
[Graphical view]
SMARTSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio313990.
PROQ32MD9.
SOURCESearch...

Entry information

Entry nameCDON_MOUSE
AccessionPrimary (citable) accession number: Q32MD9
Secondary accession number(s): E9QKV9, O88971
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot