ID CDON_RAT Reviewed; 1256 AA. AC O35158; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 2. DT 27-MAR-2024, entry version 142. DE RecName: Full=Cell adhesion molecule-related/down-regulated by oncogenes; DE Flags: Precursor; GN Name=Cdon; Synonyms=Cdo; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION, SUBCELLULAR RP LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY. RC TISSUE=Embryonic fibroblast; RX PubMed=9214393; DOI=10.1083/jcb.138.1.203; RA Kang J.-S., Gao M., Feinleib J.L., Cotter P.D., Guadagno S.N., Krauss R.S.; RT "CDO: an oncogene-, serum-, and anchorage-regulated member of the RT Ig/fibronectin type III repeat family."; RL J. Cell Biol. 138:203-213(1997). RN [2] RP INTERACTION WITH PTCH1, BOC AND GAS1, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF PRO-686; VAL-777; ILE-787 AND SER-937. RX PubMed=21802063; DOI=10.1016/j.ajhg.2011.07.001; RA Bae G.U., Domene S., Roessler E., Schachter K., Kang J.S., Muenke M., RA Krauss R.S.; RT "Mutations in CDON, encoding a hedgehog receptor, result in RT holoprosencephaly and defective interactions with other hedgehog RT receptors."; RL Am. J. Hum. Genet. 89:231-240(2011). 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 (By similarity). {ECO:0000250}. 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). Interacts with PTCH1. Interacts with GAS1. {ECO:0000250, CC ECO:0000269|PubMed:21802063}. CC -!- INTERACTION: CC O35158; P00519: ABL1; Xeno; NbExp=4; IntAct=EBI-7016767, EBI-375543; CC O35158; Q9BWV1: BOC; Xeno; NbExp=2; IntAct=EBI-7016767, EBI-718555; CC O35158; Q01721: Gas1; Xeno; NbExp=4; IntAct=EBI-7016767, EBI-15729104; CC O35158; Q13635: PTCH1; Xeno; NbExp=2; IntAct=EBI-7016767, EBI-8775406; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21802063, CC ECO:0000269|PubMed:9214393}; Single-pass membrane protein CC {ECO:0000269|PubMed:21802063, ECO:0000269|PubMed:9214393}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O35158-1; Sequence=Displayed; CC Name=2; CC IsoId=O35158-2; Sequence=VSP_018202; CC -!- TISSUE SPECIFICITY: Detected at low levels in stomach, spleen, brain, CC large intestine and lung. {ECO:0000269|PubMed:9214393}. CC -!- INDUCTION: Down-regulated in actively dividing cells. Not detectable in CC suspension cultures. Accumulates only in cells that are attached to a CC solid substrate (in vitro). {ECO:0000269|PubMed:9214393}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9214393}. 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; AF004840; AAC34735.1; -; mRNA. DR PIR; T03096; T03096. DR RefSeq; NP_059054.1; NM_017358.1. DR AlphaFoldDB; O35158; -. DR SMR; O35158; -. DR BioGRID; 248437; 2. DR IntAct; O35158; 4. DR MINT; O35158; -. DR STRING; 10116.ENSRNOP00000016247; -. DR GlyCosmos; O35158; 9 sites, No reported glycans. DR GlyGen; O35158; 9 sites. DR PhosphoSitePlus; O35158; -. DR PaxDb; 10116-ENSRNOP00000016247; -. DR GeneID; 50938; -. DR KEGG; rno:50938; -. DR UCSC; RGD:708433; rat. [O35158-1] DR AGR; RGD:708433; -. DR CTD; 50937; -. DR RGD; 708433; Cdon. DR eggNOG; ENOG502QT4P; Eukaryota. DR InParanoid; O35158; -. DR OrthoDB; 3138076at2759; -. DR PhylomeDB; O35158; -. DR Reactome; R-RNO-525793; Myogenesis. DR Reactome; R-RNO-5632681; Ligand-receptor interactions. DR Reactome; R-RNO-5635838; Activation of SMO. DR PRO; PR:O35158; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD. DR GO; GO:0007155; P:cell adhesion; IMP:RGD. DR GO; GO:0001708; P:cell fate specification; ISO:RGD. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD. DR GO; GO:0010172; P:embryonic body morphogenesis; ISO:RGD. DR GO; GO:0048598; P:embryonic morphogenesis; ISO:RGD. DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; ISO:RGD. DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD. DR GO; GO:0007520; P:myoblast fusion; ISO:RGD. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0061351; P:neural precursor cell proliferation; ISO:RGD. DR GO; GO:0007405; P:neuroblast proliferation; ISO:RGD. DR GO; GO:0030182; P:neuron differentiation; ISO:RGD. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:RGD. DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD. DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISO:RGD. DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0045664; P:regulation of neuron differentiation; ISO:RGD. DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; ISO:RGD. DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD. DR GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI. DR GO; GO:0051146; P:striated muscle cell differentiation; ISO:RGD. 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; 4. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS50835; IG_LIKE; 4. PE 1: Evidence at protein level; KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..1256 FT /note="Cell adhesion molecule-related/down-regulated by FT oncogenes" FT /id="PRO_0000234056" FT TOPO_DOM 25..963 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 964..984 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 985..1256 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..305 FT /note="Ig-like C2-type 3" FT DOMAIN 310..396 FT /note="Ig-like C2-type 4" FT DOMAIN 405..516 FT /note="Ig-like C2-type 5" FT DOMAIN 573..674 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 720..815 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 823..923 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 522..550 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 671..696 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 929..952 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1174..1212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1231..1256 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 671..685 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 935..952 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1176..1194 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1195..1211 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 294 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 342 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 427 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 570 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 870 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 333..380 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 426..500 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 400..516 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9214393" FT /id="VSP_018202" FT MUTAGEN 686 FT /note="P->A: Fails to support induction of the Sonic FT hedgehog/SSH receptors PTCH1 and GLI1. The mutant protein FT retains very little residual activity even during FT overexpression and interacts with SHH, but does not FT interact with PTCH1, BOC, or GAS1." FT /evidence="ECO:0000269|PubMed:21802063" FT MUTAGEN 777 FT /note="V->E: Fails to support induction of the Sonic FT hedgehog/SSH receptors PTCH1 and GLI1. The mutant protein FT retains some residual activity during overexpression. The FT mutant protein interacts with SHH, but does not interact FT with PTCH1. The mutation protein has a shorted half-life FT compared to wild-type and may have an altered conformation FT resulting in destabilization." FT /evidence="ECO:0000269|PubMed:21802063" FT MUTAGEN 787 FT /note="I->A: Fails to support induction of the Sonic FT hedgehog/SSH receptors PTCH1 and GLI1. The mutant protein FT retains some residual activity during overexpression. The FT mutant protein interacts with SHH, but does not interact FT with GAS1." FT /evidence="ECO:0000269|PubMed:21802063" FT MUTAGEN 937 FT /note="S->R: Fails to support induction of the Sonic FT hedgehog/SSH receptors PTCH1 and GLI1. The mutant protein FT retains some residual activity during overexpression. The FT mutant protein interacts with SHH, but does not interact FT with PTCH1 or GAS1. The mutation protein has a shorted FT half-life compared to wild-type and may have an altered FT conformation resulting in destabilization." FT /evidence="ECO:0000269|PubMed:21802063" SQ SEQUENCE 1256 AA; 136204 MW; 775805754F0C2EA4 CRC64; MHPDLGPLWK LLYVLVILCS SVSSDLATYF ISEPLSAVQK LGRPVVLHCS AKPVTARISW LHNGKRLDRN TEQIKIHRGT LTILSLNPSL SGCYQCVANN SVGAVVSGPA TVSADALADF DSSTMHVITA EKKNTGFIGC RVPESNPKAE VRYKIRGKWL MYSTGNYIIL PSGNLQILNV SSKDKGSYKC AAYNPVTSEL KVEPAGRKLL VSRPSSDGFH ILHPALSQAL AVLPHSPVTL ECVVSGVPAS QVYWLKDGQD CLSGSNWRRL YSHLATASID PADSGNYSCV VGNNSSGDVK HVTYTVNVLE HASISKGLHD QKVSLGATVR FTCEVHGNPA PNRTWFHNAQ PIRPSSRHLT EGSVLKITGV IMEDSGLYQC MADNGIGFMQ STGRLQIEQD SGQRPVIVTA PANVEVTDGD FVTLSCNATG EPVPVIHWYG RHGLITSHPS QVLRSKSRKS HLFRPGDLDP EPVYLIMSQA GSSSLSIQAV TREHAGKYTC EAVNKHGSTQ SEAFLTVVPF ETNTKAEPVT PSEASQNDER DPRDGSESGL LNLFPVKVHS GGVELPAEKN ASVPDAPNIL SPPQTHMPDT YTLVWRTGRD GGMPINAYFV KYRKLDDGSG AVGSWHTVRV PGSESELHLT ELEPSSLYEV LMVARSAVGE GQPAMLTFRT SKEKMASSKN TQASFPPVGI PKRPVTSEAS NSNFGVVLTD SSRHSGVPEA PDRPTISMAS ETSVYVTWIP RANGGSPITA FKVEYKRMKS SDWLVAAEDI PPSKLSVEVR SLEPGSIYKF RVIVINHYGE SFRSSASRPY QVAGFPNRFS NRPITGPHIA YTEAVSDTQI MLKWTYIPSS NNNTPIQGFY IYYRPTDSDN DSDYKRDVVE GSKQWHTIGH LQPETSYDIK MQCFNEGGES EFSNVMICET KVKRVPGASE YPMKELSTPP SSSGNGGNVG PATSPARSSD MLYLIVGCVL GVMVLILLVF IALCLWKSRQ QSAIQKYDPP GYLYQGSEIN GQMVEYTTLS GTARINGSVH GGFLSKGSLS NGCSHLHHKG PNGVNGILNG TINGGLYSAH TSSLTRTCVE FEHPHHLVNG GAVYTAVPQM DPLECINCRN CRNNNRCFTK TNSPLPVVPV VASYPQDGLE MKPLGVMKFP VCPVSTVPDG GQIPEECLKD SVAPAPTQRT CRQDNTSDIN SDSTEDTAEF NRGDSSGHSE AEDKVFSWSP LILSPVLEDC SEKTAWSPPG PPLDGLSVVL QQAQET //