CDON_RAT
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 25-MAY-2022, entry version 133.
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}.
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DR EMBL; AF004840; AAC34735.1; -; mRNA.
DR PIR; T03096; T03096.
DR RefSeq; NP_059054.1; NM_017358.1. [O35158-1]
DR AlphaFoldDB; O35158; -.
DR SMR; O35158; -.
DR BioGRID; 248437; 2.
DR IntAct; O35158; 4.
DR MINT; O35158; -.
DR STRING; 10116.ENSRNOP00000016247; -.
DR GlyGen; O35158; 9 sites.
DR PaxDb; O35158; -.
DR GeneID; 50938; -.
DR KEGG; rno:50938; -.
DR UCSC; RGD:708433; rat. [O35158-1]
DR CTD; 50937; -.
DR RGD; 708433; Cdon.
DR eggNOG; ENOG502QT4P; Eukaryota.
DR InParanoid; O35158; -.
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:0005887; C:integral component of plasma membrane; IEA:InterPro.
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:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IEA:InterPro.
DR GO; GO:2000179; P:positive regulation of neural precursor cell 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:0043393; P:regulation of protein binding; ISO:RGD.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; 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 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; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 2.
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
