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Database: UniProt
Entry: A0A1U7RCI4_MESAU
LinkDB: A0A1U7RCI4_MESAU
Original site: A0A1U7RCI4_MESAU 
ID   A0A1U7RCI4_MESAU        Unreviewed;      1254 AA.
AC   A0A1U7RCI4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cell adhesion molecule-related/down-regulated by oncogenes isoform X1 {ECO:0000313|RefSeq:XP_005085899.1};
GN   Name=Cdon {ECO:0000313|RefSeq:XP_005085899.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005085899.1};
RN   [1] {ECO:0000313|RefSeq:XP_005085899.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_005085899.1; XM_005085842.3.
DR   AlphaFoldDB; A0A1U7RCI4; -.
DR   STRING; 10036.ENSMAUP00000021804; -.
DR   GeneID; 101841139; -.
DR   KEGG; maua:101841139; -.
DR   CTD; 50937; -.
DR   eggNOG; ENOG502QT4P; Eukaryota.
DR   OrthoDB; 3138076at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR   GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR   GO; GO:0010172; P:embryonic body morphogenesis; IEA:Ensembl.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR   GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR   GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IEA:Ensembl.
DR   GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IEA:Ensembl.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
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; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1254
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010544373"
FT   TRANSMEM        960..985
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..113
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          138..203
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          224..302
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          309..395
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          404..515
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          572..673
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          719..814
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          822..922
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          524..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          928..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1166..1212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1194..1210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1254 AA;  136302 MW;  DBDDBECFF75FFB26 CRC64;
     MHPDLGPLWT LLYVLGILCS SVSSDLVPYF ISEPLSAVQK LGRPVDLHCS AKPVTARISW
     LHNGKRLDSN MEQIKIHQGT LTILSLNPSL SGYYQCVANN SIGAIVSGPA TVSTAALGDF
     DSSTMHVITA EEKNTGFIGC RVPESNPKAE VRYKIRGKWL KYSTGNYIIL PSGNLQILNV
     SSKDKGSYKC AAYNPVTNEL KVEPTGRKLL VSRPSSDGFH ILHPALSQAL AVLPHSPVTL
     ECVVSGVPAS QVYWLKDGQD AVSGSNWRRV HSHLATASID SADSGNYSCV VGNRSGDVKH
     VTYMVNVLER ASISKGLQDQ KVSLGATVHF TCDVHGNPAP NRTWFHNAQP IHPSSRHLTE
     GNGLKITGVT MEDSGLYQCV ADNGIGLMQS TGRLQIEQDS GLKPVIVTAP ENVEVMDGDF
     VTLSCNATGV PVPTIHWYGH RGLITSHPSQ VLRSKSRKSH LLRHRDLDLE PVYFIMSRAG
     SSSLSIRAAT QEHAGKYTCE ATNKHGATQS EAFLTVVPFE TNTKAESVTP SEATQNDERD
     PRDGLESSLL SLFPVKVHSS GVELPTQKNA SVPDAPHILS PPQTHMPDTY NLVWRAGRDG
     GLPINAYFVK YRKLDDGTGT VGSWHTVRVP GSENELHLTE LEPSSLYEVL MVARSTVGEG
     QPAMLTFRTS KEKMASSKNT QASFPPVGIP KRPVISEASN SNFGVVLTDS SRHSGVPEAP
     DRPTISTASE TSVYVTWIPR ANGGSPITAF KVEYKRMRSS DWLVAAEDIP PSKLSVEVRS
     LEPGSTYKFR VIAINHYGES FRSSASRPYQ VAGFPNRFSN RPITGPHIAY TEAVSDTQIM
     LKWTYIPSSN NNTPIQGFYI YYRPTDSDND SDYKRDVVEG SKQWHTIGHL QPETSYDIKM
     QCFNEGGESE FSNVMICETK VKRVPGASEY PVKDLSTPPG SSGNGGNVGP ATSPARSSDM
     LYLIVGCVLG VMVLILMVFI ALCLWKSRQQ NAIQKYDPPG YLYQGSEMNG QMVEYTTLSG
     TTRINGSVHG GFLSKGSLGN GCSHLHHKVP NGVNGVLNGS INGGLYSAHT NSLTRTCVEF
     EHPRHLMNGG GMYTAVPQID PLECINCRNC RNNNRCFTKT NSPLPVVPVL ASYPQDGLEM
     KPLSALKVPV CPASTLPDCG QLPEESLKDS VAPTPTQHTC CQDNISDINS DSTEDTAEFS
     RGDRNGHSEA EDNVLSWNPH ILSPVLEDCP EKTAWSPGLP LDGLSVVLQQ AQET
//
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