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   27-MAR-2024, entry version 216.
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="https://atlasgeneticsoncology.org/gene/331/DCC";
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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   GlyCosmos; P43146; 6 sites, No reported glycans.
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; 9606-ENSP00000389140; -.
DR   PeptideAtlas; P43146; -.
DR   ProteomicsDB; 55591; -.
DR   Antibodypedia; 3710; 345 antibodies from 39 providers.
DR   DNASU; 1630; -.
DR   Ensembl; ENST00000442544.7; ENSP00000389140.2; ENSG00000187323.13.
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   AGR; HGNC:2701; -.
DR   CTD; 1630; -.
DR   DisGeNET; 1630; -.
DR   GeneCards; DCC; -.
DR   GeneReviews; DCC; -.
DR   HGNC; HGNC:2701; DCC.
DR   HPA; ENSG00000187323; Tissue enhanced (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; KPEAVYT; -.
DR   OrthoDB; 5398621at2759; -.
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 1146 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 108 other cell types or tissues.
DR   ExpressionAtlas; P43146; baseline and differential.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
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:0021965; P:spinal cord ventral commissure morphogenesis; IEA:Ensembl.
DR   CDD; cd00063; FN3; 6.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05722; IgI_1_Neogenin_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
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; NETRIN RECEPTOR DCC; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF00041; fn3; 6.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF06583; Neogenin_C; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00060; FN3; 6.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; Fibronectin type III; 4.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50853; FN3; 6.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   Genevisible; P43146; HS.
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; uncertain 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; uncertain significance;
FT                   dbSNP:rs1555652216)"
FT                   /evidence="ECO:0000269|PubMed:28250456"
FT                   /id="VAR_079287"
FT   VARIANT         743
FT                   /note="M -> L (in MRMV1; uncertain significance;
FT                   dbSNP:rs199651452)"
FT                   /evidence="ECO:0000269|PubMed:28250454"
FT                   /id="VAR_079147"
FT   VARIANT         754
FT                   /note="V -> M (in MRMV1; uncertain 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; uncertain 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; uncertain significance;
FT                   dbSNP:rs1057519058)"
FT                   /evidence="ECO:0000269|PubMed:28250454"
FT                   /id="VAR_079152"
FT   VARIANT         1250
FT                   /note="A -> T (in MRMV1; uncertain 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
//