ID   CDON_XENLA              Reviewed;        1249 AA.
AC   Q90Z04;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cell adhesion molecule-related/down-regulated by oncogenes;
DE   Flags: Precursor;
GN   Name=cdon; Synonyms=cdo;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11782431; DOI=10.1093/emboj/21.1.114;
RA   Kang J.-S., Mulieri P.J., Hu Y., Taliana L., Krauss R.S.;
RT   "BOC, an Ig superfamily member, associates with CDO to positively regulate
RT   myogenic differentiation.";
RL   EMBO J. 21:114-124(2002).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
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DR   EMBL; AF388035; AAK71997.1; -; mRNA.
DR   RefSeq; NP_001079158.1; NM_001085689.1.
DR   AlphaFoldDB; Q90Z04; -.
DR   SMR; Q90Z04; -.
DR   PRIDE; Q90Z04; -.
DR   GeneID; 373711; -.
DR   KEGG; xla:373711; -.
DR   CTD; 373711; -.
DR   Xenbase; XB-GENE-922842; cdon.L.
DR   OrthoDB; 102649at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 373711; Expressed in internal ear and 15 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0048598; P:embryonic morphogenesis; IEA:InterPro.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; IEA:InterPro.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IEA:InterPro.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:InterPro.
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; 2.
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   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1249
FT                   /note="Cell adhesion molecule-related/down-regulated by
FT                   oncogenes"
FT                   /id="PRO_0000234057"
FT   TOPO_DOM        26..957
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        958..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        979..1249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..113
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          120..212
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          217..307
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          314..400
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          406..517
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          577..675
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          721..815
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          826..923
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          528..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..690
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          1158..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1172..1187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1188..1202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
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        50..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        142..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        244..292
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        335..382
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        427..501
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   1249 AA;  137077 MW;  B9BA58D8E87BC764 CRC64;
     MHSDPGPWHP LLCFLVLALS TSANSDVTPR FTSKPLSTVQ KPGGPVTLLC SAEPPWAHIS
     WLFNGEQFER ISSQGVDIQS GHLVIPSLGP AHVGQYQCIA STSVGAILSK SVSVSVAYLN
     DFETTTGHSV TAEEGSSAFI GCKIPESNPK AHVRYKVRGK WLKESSDKYL ILPSGNLHIL
     NVSVEDRGTY RCAAYNPVTH DLKLSTSTLK LSVNRSPRVD SRILHPVTSQ AVLVQIHDPL
     TLECVVGGGP SHPPVYWYKG GQEAAAYGRR KLLHTHLVIE QVQRSDAGNY SCVLGNGSGI
     SQRVYYTVIV LEPPSVSQKT EDQSLTAGSN VRFSCESRGN PTPNITWFHN AVQIHASTRH
     QISGNKIRIT SLFAQDSGIY QCFVNNEAGS AQVSQRATVH LKWSKPVIVS PPTSIRVANG
     DLVTLTCNAT GIPTPTIRWY DSHGPISSHP SQVLRSKSRK ALLSKIGTPG QDPVHYTMSQ
     AGSSSLYIRA ITVQHAGTYK CEATNEFGSA HADAYLTVVP YEMSTKPEDI TPLDLTQSDE
     GDYDSETRVP DHSQINEHKP EPRVTEKPYS GASLPEAPII LSPPQTTKPD MYNLMWRSGK
     DGGLPINAYF VRYRKLDDDG NMVGNWNSIR VPASENEFPL TELEPSSLYE VLMVARNAAG
     EGQPAMLTFR TSKERTSSSK NTQAPFPPIG VPKQTIIHGV SNTNNGLVPV DPSRHSGVPE
     APDRPTISTA SETSVYVTWI PRANGGSPIT SFKVEYKRTG GHWNAAAENI PPSKLSVEVS
     NLEPGGLYKF RVIAINNYGE SRRSTVSRPY QVAGYSIRLP NPLIVGPRID QTEAVTDTQI
     LLKWTYIPEN NNNTPIQGFY IYYRPTDSDN DSDYKRDMVE GTKLRHLISH LQPETSYDIK
     MQCFNERGAS DYSNVMMCET KARRSPGASE YPVLDLSTPS VPDRSSSPSH SPTRNGDFLY
     VIVGCVLGGM VLILLAFIAM CLLKNRQQTL MQKFEPPGYL YQGADLNGQI IEYTTLPGTS
     RINGSVHTGF MGNGNINNGC PHLHHKVHNR ASEVGNGELY PGCNSSLKET YVDYDRLPHH
     LSNGRVMYTA LPQADPTECI NCRNCCNNNR CFTKPNGSYC GNGVAVMPVG FSPQQEEGET
     KPLNHVMVPM CLTSPDQNCS EEIEEDQNEK ETQLSANSVC PEEATQTGTE QHEGEDCTKT
     EDDSSILTWT PLILPAISKD CDEKHVWTST DITLDKSNVD HPQLQTQEA