Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q4KMG0 (CDON_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1287 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 By similarity.

Subunit structure

Part of a complex that contains BOC, CDON, NEO1, cadherins and CTNNB1. Interacts with NTN3 By similarity. Interacts with PTCH1 By similarity. Interacts with GAS1 By similarity. Interacts with DHH, IHH and SHH. Ref.4 Ref.5

Subcellular location

Cell membrane; Single-pass membrane protein By similarity.

Post-translational modification

N-glycosylated By similarity.

Involvement in disease

Holoprosencephaly 11 (HPE11) [MIM:614226]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Sequence similarities

Contains 3 fibronectin type-III domains.

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

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Holoprosencephaly
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Traceable author statement Ref.1. Source: UniProtKB

cell fate specification

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

embryonic body morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic retina morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

muscle cell differentiation

Traceable author statement. Source: Reactome

myoblast fusion

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

positive regulation of neural precursor cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

positive regulation of small GTPase mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of protein heterodimerization activity

Inferred from electronic annotation. Source: Ensembl

satellite cell differentiation

Inferred from electronic annotation. Source: Ensembl

smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABL1P005192EBI-7016840,EBI-375543

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q4KMG0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q4KMG0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1212-1234: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 12871262Cell adhesion molecule-related/down-regulated by oncogenes
PRO_0000234054

Regions

Topological domain26 – 963938Extracellular Potential
Transmembrane964 – 98421Helical; Potential
Topological domain985 – 1287303Cytoplasmic Potential
Domain29 – 11486Ig-like C2-type 1
Domain120 – 20485Ig-like C2-type 2
Domain225 – 30379Ig-like C2-type 3
Domain310 – 39687Ig-like C2-type 4
Domain405 – 516112Ig-like C2-type 5
Domain579 – 67799Fibronectin type-III 1
Domain723 – 82199Fibronectin type-III 2
Domain826 – 926101Fibronectin type-III 3

Amino acid modifications

Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential
Glycosylation5701N-linked (GlcNAc...) Potential
Glycosylation8731N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 97 By similarity
Disulfide bond141 ↔ 191 By similarity
Disulfide bond243 ↔ 290 By similarity
Disulfide bond333 ↔ 380 By similarity
Disulfide bond426 ↔ 500 By similarity

Natural variations

Alternative sequence1212 – 123423Missing in isoform 2.
VSP_018201
Natural variant661K → R.
Corresponds to variant rs7122277 [ dbSNP | Ensembl ].
VAR_056038
Natural variant1621E → K.
Corresponds to variant rs3740909 [ dbSNP | Ensembl ].
VAR_056039
Natural variant3511P → A.
Corresponds to variant rs35665264 [ dbSNP | Ensembl ].
VAR_056040
Natural variant6841T → S in HPE11. Ref.6
Corresponds to variant rs145983470 [ dbSNP | Ensembl ].
VAR_066497
Natural variant6861A → V.
Corresponds to variant rs12274923 [ dbSNP | Ensembl ].
VAR_056041
Natural variant6891P → A in HPE11. Ref.6
VAR_066498
Natural variant6911V → M in HPE11. Ref.6
VAR_066499
Natural variant7801V → E in HPE11. Ref.6
VAR_066500
Natural variant7901T → A in HPE11. Ref.6
VAR_066501
Natural variant9401S → R in HPE11. Ref.6
VAR_066502

Experimental info

Sequence conflict751V → I in AAC34901. Ref.1
Sequence conflict751V → I in AAH98583. Ref.3
Sequence conflict2651G → E in AAH98583. Ref.3
Sequence conflict3001K → E in AAC34901. Ref.1
Sequence conflict6691L → I in AAC34901. Ref.1
Sequence conflict12441I → N in AAH98583. Ref.3

Secondary structure

................... 1287
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: B7870C66F5224BBE

FASTA1,287139,147
        10         20         30         40         50         60 
MHPDLGPLCT LLYVTLTILC SSVSSDLAPY FTSEPLSAVQ KLGGPVVLHC SAQPVTTRIS 

        70         80         90        100        110        120 
WLHNGKTLDG NLEHVKIHQG TLTILSLNSS LLGYYQCLAN NSIGAIVSGP ATVSVAVLGD 

       130        140        150        160        170        180 
FGSSTKHVIT AEEKSAGFIG CRVPESNPKA EVRYKIRGKW LEHSTENYLI LPSGNLQILN 

       190        200        210        220        230        240 
VSLEDKGSYK CAAYNPVTHQ LKVEPIGRKL LVSRPSSDDV HILHPTHSQA LAVLSRSPVT 

       250        260        270        280        290        300 
LECVVSGVPA PQVYWLKDGQ DIAPGSNWRR LYSHLATDSV DPADSGNYSC MAGNKSGDVK 

       310        320        330        340        350        360 
YVTYMVNVLE HASISKGLQD QIVSLGATVH FTCDVHGNPA PNCTWFHNAQ PIHPSARHLT 

       370        380        390        400        410        420 
AGNGLKISGV TVEDVGMYQC VADNGIGFMH STGRLEIEND GGFKPVIITA PVSAKVADGD 

       430        440        450        460        470        480 
FVTLSCNASG LPVPVIRWYD SHGLITSHPS QVLRSKSRKS QLSRPEGLNL EPVYFVLSQA 

       490        500        510        520        530        540 
GASSLHIQAV TQEHAGKYIC EAANEHGTTQ AEASLMVVPF ETNTKAETVT LPDAAQNDDR 

       550        560        570        580        590        600 
SKRDGSETGL LSSFPVKVHP SAVESAPEKN ASGISVPDAP IILSPPQTHT PDTYNLVWRA 

       610        620        630        640        650        660 
GKDGGLPINA YFVKYRKLDD GVGMLGSWHT VRVPGSENEL HLAELEPSSL YEVLMVARSA 

       670        680        690        700        710        720 
AGEGQPAMLT FRTSKEKTAS SKNTQASSPP VGIPKYPVVS EAANNNFGVV LTDSSRHSGV 

       730        740        750        760        770        780 
PEAPDRPTIS TASETSVYVT WIPRANGGSP ITAFKVEYKR MRTSNWLVAA EDIPPSKLSV 

       790        800        810        820        830        840 
EVRSLEPGST YKFRVIAINH YGESFRSSAS RPYQVVGFPN RFSSRPITGP HIAYTEAVSD 

       850        860        870        880        890        900 
TQIMLKWTYI PSSNNNTPIQ GFYIYYRPTD SDNDSDYKRD VVEGSKQWHM IGHLQPETSY 

       910        920        930        940        950        960 
DIKMQCFNEG GESEFSNVMI CETKVKRVPG ASEYPVKDLS TPPNSLGSGG NVGPATSPAR 

       970        980        990       1000       1010       1020 
SSDMLYLIVG CVLGVMVLIL MVFIAMCLWK NRQQNTIQKY DPPGYLYQGS DMNGQMVDYT 

      1030       1040       1050       1060       1070       1080 
TLSGASQING NVHGGFLTNG GLSSGYSHLH HKVPNAVNGI VNGSLNGGLY SGHSNSLTRT 

      1090       1100       1110       1120       1130       1140 
HVDFEHPHHL VNGGGMYTAV PQIDPLECVN CRNCRNNNRC FTKTNSTFSS SPPPVVPVVA 

      1150       1160       1170       1180       1190       1200 
PYPQDGLEMK PLSHVKVPVC LTSAVPDCGQ LPEESVKDNV EPVPTQRTCC QDIVNDVSSD 

      1210       1220       1230       1240       1250       1260 
GSEDPAEFSR GQEGMINLRI PDHLQLAKSC VWEGDSCAHS ETEINIVSWN ALILPPVPEG 

      1270       1280 
CAEKTMWSPP GIPLDSPTEV LQQPRET 

« Hide

Isoform 2 [UniParc].

Checksum: 79AB36E0B52C61D7
Show »

FASTA1,264136,527

References

« Hide 'large scale' references
[1]"CDO: an oncogene-, serum-, and anchorage-regulated member of the Ig/fibronectin type III repeat family."
Kang J.-S., Gao M., Feinleib J.L., Cotter P.D., Guadagno S.N., Krauss R.S.
J. Cell Biol. 138:203-213(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fetal brain and Fetal lung.
[2]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1).
Tissue: Placenta.
[4]"The mode of Hedgehog binding to Ihog homologues is not conserved across different phyla."
McLellan J.S., Zheng X., Hauk G., Ghirlando R., Beachy P.A., Leahy D.J.
Nature 455:979-983(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 826-924 IN COMPLEX WITH SHH, INTERACTION WITH SHH.
[5]"All mammalian Hedgehog proteins interact with cell adhesion molecule, down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved manner."
Kavran J.M., Ward M.D., Oladosu O.O., Mulepati S., Leahy D.J.
J. Biol. Chem. 285:24584-24590(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 826-924 IN COMPLEXES WITH IHH AND DHH, INTERACTION WITH IHH AND DHH.
[6]"Mutations in CDON, encoding a hedgehog receptor, result in holoprosencephaly and defective interactions with other hedgehog receptors."
Bae G.U., Domene S., Roessler E., Schachter K., Kang J.S., Muenke M., Krauss R.S.
Am. J. Hum. Genet. 89:231-240(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HPE11 SER-684; ALA-689; MET-691; GLU-780; ALA-790 AND ARG-940.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004841 mRNA. Translation: AAC34901.2.
AP000821 Genomic DNA. No translation available.
AP000842 Genomic DNA. No translation available.
BC098583 mRNA. Translation: AAH98583.1.
PIRT03097.
RefSeqNP_001230526.1. NM_001243597.1.
NP_058648.4. NM_016952.4.
UniGeneHs.38034.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3D1MX-ray1.70C/D826-924[»]
3N1FX-ray1.60C/D826-924[»]
3N1QX-ray2.89C/D/F826-924[»]
ProteinModelPortalQ4KMG0.
SMRQ4KMG0. Positions 27-924.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119165. 4 interactions.
DIPDIP-57226N.
IntActQ4KMG0. 1 interaction.
MINTMINT-2795255.
STRING9606.ENSP00000263577.

PTM databases

PhosphoSiteQ4KMG0.

Polymorphism databases

DMDM308153422.

Proteomic databases

PaxDbQ4KMG0.
PRIDEQ4KMG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263577; ENSP00000263577; ENSG00000064309. [Q4KMG0-2]
ENST00000392693; ENSP00000376458; ENSG00000064309. [Q4KMG0-1]
GeneID50937.
KEGGhsa:50937.
UCSCuc001qdc.4. human. [Q4KMG0-2]
uc009zbw.3. human. [Q4KMG0-1]

Organism-specific databases

CTD50937.
GeneCardsGC11M125866.
H-InvDBHIX0035847.
HGNCHGNC:17104. CDON.
HPACAB012422.
HPA017377.
MIM608707. gene.
614226. phenotype.
neXtProtNX_Q4KMG0.
Orphanet93925. Alobar holoprosencephaly.
93924. Lobar holoprosencephaly.
280200. Microform holoprosencephaly.
93926. Midline interhemispheric variant of holoprosencephaly.
220386. Semilobar holoprosencephaly.
280195. Septopreoptic holoprosencephaly.
PharmGKBPA26328.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG150729.
HOGENOMHOG000060072.
HOVERGENHBG081073.
InParanoidQ4KMG0.
OMAVSDTQIM.
OrthoDBEOG7MD4PB.
PhylomeDBQ4KMG0.
TreeFamTF332268.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ4KMG0.
BgeeQ4KMG0.
CleanExHS_CDON.
GenevestigatorQ4KMG0.

Family and domain databases

Gene3D2.60.40.10. 8 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

EvolutionaryTraceQ4KMG0.
GeneWikiCDON.
GenomeRNAi50937.
NextBio53379.
PROQ4KMG0.
SOURCESearch...

Entry information

Entry nameCDON_HUMAN
AccessionPrimary (citable) accession number: Q4KMG0
Secondary accession number(s): O14631
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM