DCC_HUMAN
ID DCC_HUMAN Reviewed; 1447 AA.
AC P43146;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Netrin receptor DCC;
DE AltName: Full=Colorectal cancer suppressor;
DE AltName: Full=Immunoglobulin superfamily DCC subclass member 1;
DE AltName: Full=Tumor suppressor protein DCC;
DE Flags: Precursor;
GN Name=DCC; Synonyms=IGDCC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT LEU-23.
RX PubMed=7926722; DOI=10.1101/gad.8.10.1174;
RA Hedrick L., Cho K.R., Fearon E.R., Wu T.-C., Kinzler K.W., Vogelstein B.;
RT "The DCC gene product in cellular differentiation and colorectal
RT tumorigenesis.";
RL Genes Dev. 8:1174-1183(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-750, AND VARIANT LEU-23.
RX PubMed=2294591; DOI=10.1126/science.2294591;
RA Fearon E.R., Cho K.R., Nigro J.M., Kern S.E., Simons J.W., Ruppert J.M.,
RA Hamilton S.R., Preisinger A.C., Thomas G., Kinzler K.W., Vogelstein B.;
RT "Identification of a chromosome 18q gene that is altered in colorectal
RT cancers.";
RL Science 247:49-56(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-472.
RX PubMed=1991322; DOI=10.1016/0092-8674(91)90244-s;
RA Nigro J.M., Cho K.R., Fearon E.R., Kern S.E., Ruppert J.M., Oliner J.D.,
RA Kinzler K.W., Vogelstein B.;
RT "Scrambled exons.";
RL Cell 64:607-613(1991).
RN [5]
RP GENE STRUCTURE, AND VARIANT HIS-1375.
RX PubMed=8188295; DOI=10.1006/geno.1994.1102;
RA Cho K.R., Oliner J.D., Simons J.W., Hedrick L., Fearon E.R.,
RA Preisinger A.C., Hedge P., Silverman G.A., Vogelstein B.;
RT "The DCC gene: structural analysis and mutations in colorectal
RT carcinomas.";
RL Genomics 19:525-531(1994).
RN [6]
RP FUNCTION.
RX PubMed=8861902; DOI=10.1016/s0092-8674(00)81336-7;
RA Keino-Masu K., Masu M., Hinck L., Leonardo E.D., Chan S.S.-Y.,
RA Culotti J.G., Tessier-Lavigne M.;
RT "Deleted in colorectal cancer (DCC) encodes a netrin receptor.";
RL Cell 87:175-185(1996).
RN [7]
RP INTERACTION WITH SIAH1 AND SIAH2, UBIQUITINATION, AND PROTEASOMAL
RP DEGRADATION.
RX PubMed=9334332; DOI=10.1101/gad.11.20.2701;
RA Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R.;
RT "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-
RT proteasome pathway.";
RL Genes Dev. 11:2701-2714(1997).
RN [8]
RP INVOLVEMENT IN MRMV1.
RX PubMed=20431009; DOI=10.1126/science.1186463;
RA Srour M., Riviere J.B., Pham J.M., Dube M.P., Girard S., Morin S.,
RA Dion P.A., Asselin G., Rochefort D., Hince P., Diab S.,
RA Sharafaddinzadeh N., Chouinard S., Theoret H., Charron F., Rouleau G.A.;
RT "Mutations in DCC cause congenital mirror movements.";
RL Science 328:592-592(2010).
RN [9]
RP INVOLVEMENT IN MRMV1, AND VARIANTS MRMV1 275-ARG--PHE-1447 DEL; PRO-597;
RP LEU-743; MET-754; GLY-793; GLU-805; THR-893; VAL-1217 AND THR-1250.
RX PubMed=28250454; DOI=10.1038/ng.3794;
RA Marsh A.P., Heron D., Edwards T.J., Quartier A., Galea C., Nava C.,
RA Rastetter A., Moutard M.L., Anderson V., Bitoun P., Bunt J., Faudet A.,
RA Garel C., Gillies G., Gobius I., Guegan J., Heide S., Keren B., Lesne F.,
RA Lukic V., Mandelstam S.A., McGillivray G., McIlroy A., Meneret A.,
RA Mignot C., Morcom L.R., Odent S., Paolino A., Pope K., Riant F.,
RA Robinson G.A., Spencer-Smith M., Srour M., Stephenson S.E., Tankard R.,
RA Trouillard O., Welniarz Q., Wood A., Brice A., Rouleau G., Attie-Bitach T.,
RA Delatycki M.B., Mandel J.L., Amor D.J., Roze E., Piton A., Bahlo M.,
RA Billette de Villemeur T., Sherr E.H., Leventer R.J., Richards L.J.,
RA Lockhart P.J., Depienne C.;
RT "Mutations in DCC cause isolated agenesis of the corpus callosum with
RT incomplete penetrance.";
RL Nat. Genet. 49:511-514(2017).
RN [10]
RP STRUCTURE BY NMR OF 419-1047.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the fibronectin type III domains of human netrin
RT receptor DCC.";
RL Submitted (MAR-2008) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1390-1447 IN COMPLEX WITH MYO10,
RP INTERACTION WITH MYO10, AND MUTAGENESIS OF LEU-1432; 1435-LEU-MET-1436 AND
RP LEU-1439.
RX PubMed=21642953; DOI=10.1038/emboj.2011.177;
RA Hirano Y., Hatano T., Takahashi A., Toriyama M., Inagaki N., Hakoshima T.;
RT "Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain.";
RL EMBO J. 30:2734-2747(2011).
RN [12]
RP VARIANTS THR-168 AND GLY-201, AND ROLE IN METASTATIC TUMOR DISSEMINATION.
RX PubMed=8187090;
RA Miyake S., Nagai K., Yoshino K., Oto M., Endo M., Yuasa Y.;
RT "Point mutations and allelic deletion of tumor suppressor gene DCC in human
RT esophageal squamous cell carcinomas and their relation to metastasis.";
RL Cancer Res. 54:3007-3010(1994).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] SER-1039.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [14]
RP VARIANT HGPPS2 LYS-691, AND INVOLVEMENT IN HGPPS2.
RX PubMed=28250456; DOI=10.1038/ng.3804;
RA Jamuar S.S., Schmitz-Abe K., D'Gama A.M., Drottar M., Chan W.M., Peeva M.,
RA Servattalab S., Lam A.N., Delgado M.R., Clegg N.J., Zayed Z.A., Dogar M.A.,
RA Alorainy I.A., Jamea A.A., Abu-Amero K., Griebel M., Ward W., Lein E.S.,
RA Markianos K., Barkovich A.J., Robson C.D., Grant P.E., Bosley T.M.,
RA Engle E.C., Walsh C.A., Yu T.W.;
RT "Biallelic mutations in human DCC cause developmental split-brain
RT syndrome.";
RL Nat. Genet. 49:606-612(2017).
CC -!- FUNCTION: Receptor for netrin required for axon guidance. Mediates axon
CC attraction of neuronal growth cones in the developing nervous system
CC upon ligand binding. Its association with UNC5 proteins may trigger
CC signaling for axon repulsion. It also acts as a dependence receptor
CC required for apoptosis induction when not associated with netrin
CC ligand. Implicated as a tumor suppressor gene.
CC {ECO:0000269|PubMed:8187090, ECO:0000269|PubMed:8861902}.
CC -!- SUBUNIT: Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and
CC probably UNC5D (By similarity). Interacts with DSCAM (By similarity).
CC Interacts with PTK2/FAK1 and MAPK1 (By similarity). Interacts with NTN1
CC (By similarity). Interacts with MYO10 (PubMed:21642953). Interacts with
CC CBLN4; this interaction can be competed by NTN1 (By similarity).
CC Interacts with SIAH1 and SIAH2 (PubMed:9334332).
CC {ECO:0000250|UniProtKB:P70211, ECO:0000250|UniProtKB:Q63155,
CC ECO:0000269|PubMed:21642953, ECO:0000269|PubMed:9334332}.
CC -!- INTERACTION:
CC P43146; P55211: CASP9; NbExp=2; IntAct=EBI-1222919, EBI-516799;
CC P43146; P56270: MAZ; NbExp=4; IntAct=EBI-1222919, EBI-1809742;
CC P43146; Q9HD67: MYO10; NbExp=7; IntAct=EBI-1222919, EBI-307061;
CC P43146; O95631: NTN1; NbExp=4; IntAct=EBI-1222919, EBI-2678626;
CC P43146; P46779: RPL28; NbExp=3; IntAct=EBI-1222919, EBI-366357;
CC P43146; P46777: RPL5; NbExp=7; IntAct=EBI-1222919, EBI-358018;
CC P43146; P62266: RPS23; NbExp=2; IntAct=EBI-1222919, EBI-353072;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Found in axons of the central and peripheral
CC nervous system and in differentiated cell types of the intestine. Not
CC expressed in colorectal tumor cells that lost their capacity to
CC differentiate into mucus producing cells. {ECO:0000269|PubMed:7926722}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000269|PubMed:9334332}.
CC -!- DISEASE: Mirror movements 1 (MRMV1) [MIM:157600]: A disorder
CC characterized by contralateral involuntary movements that mirror
CC voluntary ones. While mirror movements are occasionally found in young
CC children, persistence beyond the age of 10 is abnormal. Mirror
CC movements occur more commonly in the upper extremities. Some MRMV1
CC patients have agenesis of the corpus callosum.
CC {ECO:0000269|PubMed:20431009, ECO:0000269|PubMed:28250454}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Gaze palsy, familial horizontal, with progressive scoliosis,
CC 2, with impaired intellectual development (HGPPS2) [MIM:617542]: An
CC autosomal recessive neurologic disorder characterized by global
CC developmental delay, delayed walking, intellectual disability,
CC horizontal gaze palsy, and childhood-onset progressive scoliosis.
CC {ECO:0000269|PubMed:28250456}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Inactivation of DCC due to allelic deletion and/or point
CC mutations is related to lymphatic and hematogenous metastatic tumor
CC dissemination.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52175.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA52177.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA52179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA52180.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DCCID331ch18q21.html";
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DR EMBL; X76132; CAA53735.1; -; mRNA.
DR EMBL; AC011155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC021486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M32292; AAA35751.1; -; mRNA.
DR EMBL; M32286; AAA52174.1; -; Genomic_DNA.
DR EMBL; M32288; AAA52175.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M32290; AAA52176.1; -; Genomic_DNA.
DR EMBL; M63696; AAA52177.1; ALT_INIT; Genomic_DNA.
DR EMBL; M63700; AAA52178.1; -; Genomic_DNA.
DR EMBL; M63702; AAA52179.1; ALT_INIT; Genomic_DNA.
DR EMBL; M63718; AAA52180.1; ALT_INIT; Genomic_DNA.
DR EMBL; M63698; AAA52181.1; -; Genomic_DNA.
DR CCDS; CCDS11952.1; -.
DR PIR; A54100; A54100.
DR RefSeq; NP_005206.2; NM_005215.3.
DR PDB; 2ED7; NMR; -; A=419-524.
DR PDB; 2ED8; NMR; -; A=528-620.
DR PDB; 2ED9; NMR; -; A=602-718.
DR PDB; 2EDB; NMR; -; A=716-818.
DR PDB; 2EDD; NMR; -; A=833-942.
DR PDB; 2EDE; NMR; -; A=944-1044.
DR PDB; 3AU4; X-ray; 1.90 A; B=1390-1447.
DR PDB; 4URT; X-ray; 3.10 A; B=844-1043.
DR PDB; 5X83; X-ray; 3.00 A; A/C=721-815, B/D=844-1043.
DR PDBsum; 2ED7; -.
DR PDBsum; 2ED8; -.
DR PDBsum; 2ED9; -.
DR PDBsum; 2EDB; -.
DR PDBsum; 2EDD; -.
DR PDBsum; 2EDE; -.
DR PDBsum; 3AU4; -.
DR PDBsum; 4URT; -.
DR PDBsum; 5X83; -.
DR AlphaFoldDB; P43146; -.
DR BMRB; P43146; -.
DR SMR; P43146; -.
DR BioGRID; 107998; 65.
DR DIP; DIP-38423N; -.
DR ELM; P43146; -.
DR IntAct; P43146; 47.
DR MINT; P43146; -.
DR STRING; 9606.ENSP00000389140; -.
DR GlyGen; P43146; 7 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P43146; -.
DR PhosphoSitePlus; P43146; -.
DR SwissPalm; P43146; -.
DR BioMuta; DCC; -.
DR DMDM; 296434474; -.
DR jPOST; P43146; -.
DR MassIVE; P43146; -.
DR MaxQB; P43146; -.
DR PaxDb; P43146; -.
DR PeptideAtlas; P43146; -.
DR PRIDE; P43146; -.
DR ProteomicsDB; 55591; -.
DR Antibodypedia; 3710; 304 antibodies from 39 providers.
DR DNASU; 1630; -.
DR Ensembl; ENST00000442544.7; ENSP00000389140.2; ENSG00000187323.12.
DR GeneID; 1630; -.
DR KEGG; hsa:1630; -.
DR MANE-Select; ENST00000442544.7; ENSP00000389140.2; NM_005215.4; NP_005206.2.
DR UCSC; uc002lfe.3; human.
DR CTD; 1630; -.
DR DisGeNET; 1630; -.
DR GeneCards; DCC; -.
DR GeneReviews; DCC; -.
DR HGNC; HGNC:2701; DCC.
DR HPA; ENSG00000187323; Group enriched (brain, testis).
DR MalaCards; DCC; -.
DR MIM; 120470; gene.
DR MIM; 157600; phenotype.
DR MIM; 617542; phenotype.
DR neXtProt; NX_P43146; -.
DR OpenTargets; ENSG00000187323; -.
DR Orphanet; 238722; Familial congenital mirror movements.
DR Orphanet; 2744; Horizontal gaze palsy with progressive scoliosis.
DR Orphanet; 478; Kallmann syndrome.
DR PharmGKB; PA27170; -.
DR VEuPathDB; HostDB:ENSG00000187323; -.
DR eggNOG; KOG4221; Eukaryota.
DR GeneTree; ENSGT00940000158867; -.
DR InParanoid; P43146; -.
DR OMA; KVYTSMM; -.
DR OrthoDB; 217780at2759; -.
DR PhylomeDB; P43146; -.
DR TreeFam; TF321506; -.
DR PathwayCommons; P43146; -.
DR Reactome; R-HSA-373752; Netrin-1 signaling.
DR Reactome; R-HSA-376172; DSCAM interactions.
DR Reactome; R-HSA-418885; DCC mediated attractive signaling.
DR Reactome; R-HSA-418886; Netrin mediated repulsion signals.
DR Reactome; R-HSA-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
DR Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR SignaLink; P43146; -.
DR SIGNOR; P43146; -.
DR BioGRID-ORCS; 1630; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; DCC; human.
DR EvolutionaryTrace; P43146; -.
DR GeneWiki; Deleted_in_Colorectal_Cancer; -.
DR GenomeRNAi; 1630; -.
DR Pharos; P43146; Tbio.
DR PRO; PR:P43146; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P43146; protein.
DR Bgee; ENSG00000187323; Expressed in cortical plate and 106 other tissues.
DR ExpressionAtlas; P43146; baseline and differential.
DR Genevisible; P43146; HS.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0005042; F:netrin receptor activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; TAS:ProtInc.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IEA:Ensembl.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; TAS:BHF-UCL.
DR GO; GO:2000171; P:negative regulation of dendrite development; TAS:BHF-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; TAS:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IBA:GO_Central.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:1901214; P:regulation of neuron death; IMP:UniProtKB.
DR GO; GO:0021965; P:spinal cord ventral commissure morphogenesis; IEA:Ensembl.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR033012; DCC.
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; IPR010560; Neogenin_C.
DR PANTHER; PTHR44170:SF8; PTHR44170:SF8; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF06583; Neogenin_C; 1.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Developmental protein; Disease variant;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Intellectual disability; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Tumor suppressor; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1447
FT /note="Netrin receptor DCC"
FT /id="PRO_0000014744"
FT TOPO_DOM 26..1097
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1098..1122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1123..1447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..135
FT /note="Ig-like C2-type 1"
FT DOMAIN 139..229
FT /note="Ig-like C2-type 2"
FT DOMAIN 234..326
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..416
FT /note="Ig-like C2-type 4"
FT DOMAIN 431..524
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 530..620
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 625..718
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 728..821
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 846..942
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 947..1044
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1126..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1439
FT /note="Interaction with MYO10"
FT /evidence="ECO:0000269|PubMed:21642953"
FT COMPBIAS 1175..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1178
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q63155"
FT MOD_RES 1187
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q63155"
FT MOD_RES 1267
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q63155"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 161..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 261..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 23
FT /note="F -> L (in dbSNP:rs9951523)"
FT /evidence="ECO:0000269|PubMed:2294591,
FT ECO:0000269|PubMed:7926722"
FT /id="VAR_060257"
FT VARIANT 168
FT /note="M -> T (in a esophageal carcinoma;
FT dbSNP:rs121912967)"
FT /evidence="ECO:0000269|PubMed:8187090"
FT /id="VAR_003909"
FT VARIANT 201
FT /note="R -> G (in dbSNP:rs2229080)"
FT /evidence="ECO:0000269|PubMed:8187090"
FT /id="VAR_003910"
FT VARIANT 275..1447
FT /note="Missing (in MRMV1)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079145"
FT VARIANT 597
FT /note="R -> P (in MRMV1; unknown pathological significance;
FT dbSNP:rs1057519056)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079146"
FT VARIANT 679
FT /note="L -> R (in dbSNP:rs2271042)"
FT /id="VAR_060258"
FT VARIANT 691
FT /note="Q -> K (in HGPPS2; unknown pathological
FT significance; dbSNP:rs1555652216)"
FT /evidence="ECO:0000269|PubMed:28250456"
FT /id="VAR_079287"
FT VARIANT 743
FT /note="M -> L (in MRMV1; unknown pathological significance;
FT dbSNP:rs199651452)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079147"
FT VARIANT 754
FT /note="V -> M (in MRMV1; unknown pathological significance;
FT dbSNP:rs775565634)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079148"
FT VARIANT 759
FT /note="I -> M (in dbSNP:rs2278339)"
FT /id="VAR_056043"
FT VARIANT 793
FT /note="V -> G (in MRMV1; dbSNP:rs1057519054)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079149"
FT VARIANT 805
FT /note="G -> E (in MRMV1; dbSNP:rs1057519055)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079150"
FT VARIANT 893
FT /note="A -> T (in MRMV1; unknown pathological significance;
FT dbSNP:rs1057519057)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079151"
FT VARIANT 1017
FT /note="M -> V (in dbSNP:rs984274)"
FT /id="VAR_024495"
FT VARIANT 1039
FT /note="F -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035511"
FT VARIANT 1191
FT /note="H -> L (in dbSNP:rs2270950)"
FT /id="VAR_060259"
FT VARIANT 1217
FT /note="M -> V (in MRMV1; unknown pathological significance;
FT dbSNP:rs1057519058)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079152"
FT VARIANT 1250
FT /note="A -> T (in MRMV1; unknown pathological significance;
FT dbSNP:rs748112308)"
FT /evidence="ECO:0000269|PubMed:28250454"
FT /id="VAR_079153"
FT VARIANT 1375
FT /note="P -> H (in a colorectal carcinoma;
FT dbSNP:rs387906555)"
FT /evidence="ECO:0000269|PubMed:8188295"
FT /id="VAR_003911"
FT MUTAGEN 1432
FT /note="L->S: Abolishes interaction with MYO10."
FT /evidence="ECO:0000269|PubMed:21642953"
FT MUTAGEN 1435..1436
FT /note="LM->SS: Abolishes interaction with MYO10."
FT /evidence="ECO:0000269|PubMed:21642953"
FT MUTAGEN 1439
FT /note="L->S: Abolishes interaction with MYO10."
FT /evidence="ECO:0000269|PubMed:21642953"
FT CONFLICT 951
FT /note="L -> F (in Ref. 1; CAA53735)"
FT /evidence="ECO:0000305"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 459..470
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:2ED7"
FT STRAND 532..537
FT /evidence="ECO:0007829|PDB:2ED8"
FT STRAND 543..549
FT /evidence="ECO:0007829|PDB:2ED8"
FT STRAND 560..567
FT /evidence="ECO:0007829|PDB:2ED8"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:2ED8"
FT STRAND 573..578
FT /evidence="ECO:0007829|PDB:2ED8"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:2ED8"
FT STRAND 593..601
FT /evidence="ECO:0007829|PDB:2ED8"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:2ED8"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:2ED8"
FT STRAND 631..635
FT /evidence="ECO:0007829|PDB:2ED9"
FT STRAND 638..642
FT /evidence="ECO:0007829|PDB:2ED9"
FT TURN 648..650
FT /evidence="ECO:0007829|PDB:2ED9"
FT STRAND 657..668
FT /evidence="ECO:0007829|PDB:2ED9"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:2ED9"
FT STRAND 679..684
FT /evidence="ECO:0007829|PDB:2ED9"
FT STRAND 691..694
FT /evidence="ECO:0007829|PDB:2ED9"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:2ED9"
FT STRAND 711..714
FT /evidence="ECO:0007829|PDB:2ED9"
FT STRAND 716..719
FT /evidence="ECO:0007829|PDB:2EDB"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 741..746
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 757..765
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 769..775
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 791..800
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 808..813
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 848..854
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 860..865
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:2EDD"
FT STRAND 880..891
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 896..907
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 915..924
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 927..929
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 935..938
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 949..955
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 963..968
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 977..986
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:5X83"
FT HELIX 992..994
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 995..1001
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 1006..1009
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 1017..1026
FT /evidence="ECO:0007829|PDB:5X83"
FT STRAND 1037..1040
FT /evidence="ECO:0007829|PDB:5X83"
FT HELIX 1415..1421
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1425..1443
FT /evidence="ECO:0007829|PDB:3AU4"
SQ SEQUENCE 1447 AA; 158457 MW; BC17EA0E93DE8768 CRC64;
MENSLRCVWV PKLAFVLFGA SLFSAHLQVT GFQIKAFTAL RFLSEPSDAV TMRGGNVLLD
CSAESDRGVP VIKWKKDGIH LALGMDERKQ QLSNGSLLIQ NILHSRHHKP DEGLYQCEAS
LGDSGSIISR TAKVAVAGPL RFLSQTESVT AFMGDTVLLK CEVIGEPMPT IHWQKNQQDL
TPIPGDSRVV VLPSGALQIS RLQPGDIGIY RCSARNPASS RTGNEAEVRI LSDPGLHRQL
YFLQRPSNVV AIEGKDAVLE CCVSGYPPPS FTWLRGEEVI QLRSKKYSLL GGSNLLISNV
TDDDSGMYTC VVTYKNENIS ASAELTVLVP PWFLNHPSNL YAYESMDIEF ECTVSGKPVP
TVNWMKNGDV VIPSDYFQIV GGSNLRILGV VKSDEGFYQC VAENEAGNAQ TSAQLIVPKP
AIPSSSVLPS APRDVVPVLV SSRFVRLSWR PPAEAKGNIQ TFTVFFSREG DNRERALNTT
QPGSLQLTVG NLKPEAMYTF RVVAYNEWGP GESSQPIKVA TQPELQVPGP VENLQAVSTS
PTSILITWEP PAYANGPVQG YRLFCTEVST GKEQNIEVDG LSYKLEGLKK FTEYSLRFLA
YNRYGPGVST DDITVVTLSD VPSAPPQNVS LEVVNSRSIK VSWLPPPSGT QNGFITGYKI
RHRKTTRRGE METLEPNNLW YLFTGLEKGS QYSFQVSAMT VNGTGPPSNW YTAETPENDL
DESQVPDQPS SLHVRPQTNC IIMSWTPPLN PNIVVRGYII GYGVGSPYAE TVRVDSKQRY
YSIERLESSS HYVISLKAFN NAGEGVPLYE SATTRSITDP TDPVDYYPLL DDFPTSVPDL
STPMLPPVGV QAVALTHDAV RVSWADNSVP KNQKTSEVRL YTVRWRTSFS ASAKYKSEDT
TSLSYTATGL KPNTMYEFSV MVTKNRRSST WSMTAHATTY EAAPTSAPKD LTVITREGKP
RAVIVSWQPP LEANGKITAY ILFYTLDKNI PIDDWIMETI SGDRLTHQIM DLNLDTMYYF
RIQARNSKGV GPLSDPILFR TLKVEHPDKM ANDQGRHGDG GYWPVDTNLI DRSTLNEPPI
GQMHPPHGSV TPQKNSNLLV IIVVTVGVIT VLVVVIVAVI CTRRSSAQQR KKRATHSAGK
RKGSQKDLRP PDLWIHHEEM EMKNIEKPSG TDPAGRDSPI QSCQDLTPVS HSQSETQLGS
KSTSHSGQDT EEAGSSMSTL ERSLAARRAP RAKLMIPMDA QSNNPAVVSA IPVPTLESAQ
YPGILPSPTC GYPHPQFTLR PVPFPTLSVD RGFGAGRSQS VSEGPTTQQP PMLPPSQPEH
SSSEEAPSRT IPTACVRPTH PLRSFANPLL PPPMSAIEPK VPYTPLLSQP GPTLPKTHVK
TASLGLAGKA RSPLLPVSVP TAPEVSEESH KPTEDSANVY EQDDLSEQMA SLEGLMKQLN
AITGSAF
