ID E1BHG3_BOVIN Unreviewed; 1247 AA.
AC E1BHG3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Cell adhesion associated, onco regulated {ECO:0000313|Ensembl:ENSBTAP00000012270.5};
GN Name=CDON {ECO:0000313|Ensembl:ENSBTAP00000012270.5,
GN ECO:0000313|VGNC:VGNC:27151};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000012270.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000012270.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000012270.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000012270.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000012270.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_005226878.1; XM_005226821.3.
DR RefSeq; XP_010819244.1; XM_010820942.2.
DR STRING; 9913.ENSBTAP00000066135; -.
DR PaxDb; 9913-ENSBTAP00000012270; -.
DR Ensembl; ENSBTAT00000012270.6; ENSBTAP00000012270.5; ENSBTAG00000009315.6.
DR Ensembl; ENSBTAT00000078436.1; ENSBTAP00000062865.1; ENSBTAG00000009315.6.
DR Ensembl; ENSBTAT00000080826.1; ENSBTAP00000066135.1; ENSBTAG00000009315.6.
DR GeneID; 536011; -.
DR CTD; 50937; -.
DR VEuPathDB; HostDB:ENSBTAG00000009315; -.
DR VGNC; VGNC:27151; CDON.
DR eggNOG; ENOG502QT4P; Eukaryota.
DR GeneTree; ENSGT00940000157114; -.
DR HOGENOM; CLU_008503_0_0_1; -.
DR OMA; NGCAHLH; -.
DR OrthoDB; 3138076at2759; -.
DR TreeFam; TF332268; -.
DR Reactome; R-BTA-525793; Myogenesis.
DR Reactome; R-BTA-5632681; Ligand-receptor interactions.
DR Reactome; R-BTA-5635838; Activation of SMO.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000009315; Expressed in omental fat pad and 101 other cell types or tissues.
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:0098609; P:cell-cell adhesion; IBA:GO_Central.
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:0007399; P:nervous system development; IBA:GO_Central.
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 InterPro; IPR013106; Ig_V-set.
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; 2.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 2.
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:UP000009136};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1247
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041157013"
FT TRANSMEM 957..982
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..114
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 139..204
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 225..303
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 310..396
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 405..513
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 573..671
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 716..811
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 819..919
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 455..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1247 AA; 134752 MW; 52E5D05CC3371071 CRC64;
MHPDSRPLQT LLYVTLLMLC ASVSPDLAPY FVSEPLSAVQ KLGGPVVLHC SAKPVTARIS
WLHNGKRLDR NVEQIKVHQG TLTILSLNPS LSGHYQCVAN NSIGAILSGP ATVSTAVLGD
FGASGKHVIT AEEKSTGFIA CRVPDSNPKA EVRYKIRGKW LKQSTENYLI LPSGNLQILN
VSLEDKGSYK CAAFNPVTHE LKVEPIGQKL LVSRPSSGDF HILHPTFSQA LAVLSRSPVT
LECVVSGVPA SHVRWLKGGQ DAVVGSTWRR LYTHLATDSI DPADSGNYSC VVGNKAGDAK
HVTYMVNVLE HASISKGLQD QTVSLGATVQ FTCEVHGNPA PNRTWFHNAQ PIRPSPRHLT
VGNGLKISGV TMEDSGLYQC VADNGIGFTQ STGRLEIEKG SGLKPIITRS PASAEVAVGD
SVTLSCNATG LPVPAIHWYD KRGLITSHLS QALRSKSRKP HLLRPGSSDP EPVTSRAGSG
SLYIQAVRRE HAGKYTCEAT NVHGTTRSEA ILVVVPFETD TKAEIVTSSD PTQNDKSDDS
ETGLLSSFPV KEHSSAKESS SEKNASGPSV PDAPIILSPP QTHTPDTYSL VWRAGKDGGL
PINAYFVKYR KLEDGVGVVG SWHTVRVPGS ENELHLTELE PSSLYEVLMV ARSAAGEGQP
AMLTFRTSKE KTASSKNTQA SSPPVGIPKR PVVSEAADNF GVVLTDASRH SGVPEAPDRP
TISTASETSV YVTWIPRANG GSPITAFKVE YKRMRTSDWL VAAEDIPPSK LSVEVRSLEP
GSTYKFRVIA INHYGESFRS SASRPYQVAG FPNRFSNRPI TGPHIAYTEA VSDTQIMLKW
TYIPSSNNNT PIQGFYIYYR PTDSDNDSDY KRDIVEGSKQ WHMIGHLQPE TSYDIKMQCF
NEGGESEFSN VMICETKVKR VPGASEYPIK DLSTPPNSSG SGGNVGPAAS PTRSSDMLYL
IVGCVLGVMV LILMAFIAMC LWKNRQQSTI QKYDPPGYLY QGSDVNGQMV EYTTLPGTNR
INGSVHGSFS NGCSHLHHKV PNGVSGSLNG GLYPGHVSSL TRTRVDFEHP RRLVNGGGLY
TAVPPADPME CINCRNCRNN NRCFTKTSST FSSSPLPVVP VIAPYPQDGL EMKPFGHMKM
PVCLASTVPD CVQPPEEGIK EDETPTPAQP ICCQDSRDGA SSDCVEDTAE FHRGDSCVPS
EAENNILSWN PLVLPPVSKD CTEKTLWCPP GTPVDSPPGV LQQPQET
//
