DCDC2_HUMAN
ID DCDC2_HUMAN Reviewed; 476 AA.
AC Q9UHG0; Q5VTR8; Q5VTR9; Q86W35; Q9UFD1; Q9UHG1; Q9ULR6;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Doublecortin domain-containing protein 2;
DE AltName: Full=Protein RU2S;
GN Name=DCDC2; Synonyms=KIAA1154, RU2;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP GLY-221.
RX PubMed=10601354; DOI=10.1084/jem.190.12.1793;
RA Van den Eynde B.J., Gaugler B., Probst-Kepper M., Michaux L., Devuyst O.,
RA Lorge F., Weynants P., Boon T.;
RT "A new antigen recognized by cytolytic T lymphocytes on a human kidney
RT tumor results from reverse strand transcription.";
RL J. Exp. Med. 190:1793-1800(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-221.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-221.
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INVOLVEMENT IN DYX2, AND TISSUE SPECIFICITY.
RX PubMed=16278297; DOI=10.1073/pnas.0508591102;
RA Meng H., Smith S.D., Hager K., Held M., Liu J., Olson R.K.,
RA Pennington B.F., DeFries J.C., Gelernter J., O'Reilly-Pol T., Somlo S.,
RA Skudlarski P., Shaywitz S.E., Shaywitz B.A., Marchione K., Wang Y.,
RA Paramasivam M., LoTurco J.J., Page G.P., Gruen J.R.;
RT "DCDC2 is associated with reading disability and modulates neuronal
RT development in the brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17053-17058(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DVL1; DVL2 AND DVL3, AND
RP INVOLVEMENT IN NPHP19.
RX PubMed=25557784; DOI=10.1016/j.ajhg.2014.12.002;
RA Schueler M., Braun D.A., Chandrasekar G., Gee H.Y., Klasson T.D.,
RA Halbritter J., Bieder A., Porath J.D., Airik R., Zhou W., LoTurco J.J.,
RA Che A., Otto E.A., Boeckenhauer D., Sebire N.J., Honzik T., Harris P.C.,
RA Koon S.J., Gunay-Aygun M., Saunier S., Zerres K., Bruechle N.O.,
RA Drenth J.P., Pelletier L., Tapia-Paez I., Lifton R.P., Giles R.H., Kere J.,
RA Hildebrandt F.;
RT "DCDC2 mutations cause a renal-hepatic ciliopathy by disrupting Wnt
RT signaling.";
RL Am. J. Hum. Genet. 96:81-92(2015).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN DFNB66, VARIANT DFNB66
RP PRO-424, AND CHARACTERIZATION OF VARIANT DFNB66 PRO-424.
RX PubMed=25601850; DOI=10.1093/hmg/ddv009;
RA Grati M., Chakchouk I., Ma Q., Bensaid M., Desmidt A., Turki N., Yan D.,
RA Baanannou A., Mittal R., Driss N., Blanton S., Farooq A., Lu Z., Liu X.Z.,
RA Masmoudi S.;
RT "A missense mutation in DCDC2 causes human recessive deafness DFNB66,
RT likely by interfering with sensory hair cell and supporting cell cilia
RT length regulation.";
RL Hum. Mol. Genet. 24:2482-2491(2015).
RN [10]
RP INVOLVEMENT IN NSC, VARIANT NSC ASN-17, CHARACTERIZATION OF VARIANT NSC
RP ASN-17, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27319779; DOI=10.1002/humu.23031;
RA Girard M., Bizet A.A., Lachaux A., Gonzales E., Filhol E.,
RA Collardeau-Frachon S., Jeanpierre C., Henry C., Fabre M., Viremouneix L.,
RA Galmiche L., Debray D., Bole-Feysot C., Nitschke P., Pariente D.,
RA Guettier C., Lyonnet S., Heidet L., Bertholet A., Jacquemin E.,
RA Henrion-Caude A., Saunier S.;
RT "DCDC2 mutations cause neonatal sclerosing cholangitis.";
RL Hum. Mutat. 37:1025-1029(2016).
RN [11]
RP INVOLVEMENT IN NSC, AND VARIANTS NSC 217-LYS--ALA-476 DEL AND
RP 297-LEU--ALA-476 DEL.
RX PubMed=27469900; DOI=10.1016/j.jhep.2016.07.017;
RG University of Washington Center for Mendelian Genomics;
RA Grammatikopoulos T., Sambrotta M., Strautnieks S., Foskett P.,
RA Knisely A.S., Wagner B., Deheragoda M., Starling C., Mieli-Vergani G.,
RA Smith J., Bull L., Thompson R.J.;
RT "Mutations in DCDC2 (doublecortin domain containing protein 2) in neonatal
RT sclerosing cholangitis.";
RL J. Hepatol. 65:1179-1187(2016).
RN [12]
RP STRUCTURE BY NMR OF 132-226.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-062, a DCX domain from human.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Protein that plays a role in the inhibition of canonical Wnt
CC signaling pathway (PubMed:25557784). May be involved in neuronal
CC migration during development of the cerebral neocortex (By similarity).
CC Involved in the control of ciliogenesis and ciliary length
CC (PubMed:25601850, PubMed:27319779). {ECO:0000250|UniProtKB:D3ZR10,
CC ECO:0000269|PubMed:25557784, ECO:0000269|PubMed:25601850,
CC ECO:0000269|PubMed:27319779}.
CC -!- SUBUNIT: Interacts with DVL1, DVL2 and DVL3.
CC {ECO:0000269|PubMed:25557784}.
CC -!- INTERACTION:
CC Q9UHG0; Q9BYG0: B3GNT5; NbExp=3; IntAct=EBI-10303987, EBI-3923833;
CC Q9UHG0; Q9P296: C5AR2; NbExp=3; IntAct=EBI-10303987, EBI-2874691;
CC Q9UHG0; Q9BU64: CENPO; NbExp=3; IntAct=EBI-10303987, EBI-745954;
CC Q9UHG0; P61024: CKS1B; NbExp=3; IntAct=EBI-10303987, EBI-456371;
CC Q9UHG0; Q9P000: COMMD9; NbExp=3; IntAct=EBI-10303987, EBI-1550510;
CC Q9UHG0; Q9UIA0: CYTH4; NbExp=3; IntAct=EBI-10303987, EBI-11521003;
CC Q9UHG0; Q8TCX1-2: DYNC2LI1; NbExp=3; IntAct=EBI-10303987, EBI-8568452;
CC Q9UHG0; Q8IZS6: DYNLT2; NbExp=3; IntAct=EBI-10303987, EBI-22730131;
CC Q9UHG0; Q9NWS6: FAM118A; NbExp=3; IntAct=EBI-10303987, EBI-8638992;
CC Q9UHG0; Q9NVN8: GNL3L; NbExp=3; IntAct=EBI-10303987, EBI-746682;
CC Q9UHG0; Q86X24: HORMAD1; NbExp=3; IntAct=EBI-10303987, EBI-12165207;
CC Q9UHG0; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-10303987, EBI-3958099;
CC Q9UHG0; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-10303987, EBI-1043191;
CC Q9UHG0; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-10303987, EBI-11742507;
CC Q9UHG0; Q9BQP7: MGME1; NbExp=3; IntAct=EBI-10303987, EBI-739561;
CC Q9UHG0; Q8IY33: MICALL2; NbExp=3; IntAct=EBI-10303987, EBI-2555563;
CC Q9UHG0; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-10303987, EBI-995714;
CC Q9UHG0; Q9HB07: MYG1; NbExp=3; IntAct=EBI-10303987, EBI-709754;
CC Q9UHG0; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-10303987, EBI-740897;
CC Q9UHG0; P48645: NMU; NbExp=3; IntAct=EBI-10303987, EBI-10210351;
CC Q9UHG0; P01178: OXT; NbExp=3; IntAct=EBI-10303987, EBI-1762651;
CC Q9UHG0; Q969H6: POP5; NbExp=3; IntAct=EBI-10303987, EBI-366525;
CC Q9UHG0; Q14761: PTPRCAP; NbExp=3; IntAct=EBI-10303987, EBI-722217;
CC Q9UHG0; Q96QD8: SLC38A2; NbExp=3; IntAct=EBI-10303987, EBI-723083;
CC Q9UHG0; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-10303987, EBI-74615;
CC Q9UHG0; Q7Z4G4: TRMT11; NbExp=3; IntAct=EBI-10303987, EBI-2515608;
CC Q9UHG0; O94892: ZNF432; NbExp=3; IntAct=EBI-10303987, EBI-12121104;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:25601850, ECO:0000269|PubMed:27319779}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25557784,
CC ECO:0000269|PubMed:27319779}. Cell projection, kinocilium
CC {ECO:0000250|UniProtKB:D3ZR10}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:D3ZR10}. Note=Localizes to the ciliary axoneme
CC and to mitotic spindle fibers in a cell-cycle-dependent manner.
CC {ECO:0000269|PubMed:25557784}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHG0-2; Sequence=VSP_014670, VSP_014671;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. In brain, highly expressed
CC in the entorhinal cortex, inferior temporal cortex, medial temporal
CC cortex, hypothalamus, amygdala and hippocampus (PubMed:10601354,
CC PubMed:16278297). Expressed in liver by cholangiocytes, the epithelial
CC cells of the bile ducts (at protein level) (PubMed:27319779).
CC {ECO:0000269|PubMed:10601354, ECO:0000269|PubMed:16278297,
CC ECO:0000269|PubMed:27319779}.
CC -!- DISEASE: Dyslexia 2 (DYX2) [MIM:600202]: A relatively common, complex
CC cognitive disorder characterized by an impairment of reading
CC performance despite adequate motivational, educational and intellectual
CC opportunities. It is a multifactorial trait, with evidence for familial
CC clustering and heritability. {ECO:0000269|PubMed:16278297}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- DISEASE: Nephronophthisis 19 (NPHP19) [MIM:616217]: A form of
CC nephronophthisis, an autosomal recessive disorder characterized by
CC chronic tubulointerstitial nephritis resulting in end-stage renal
CC disease. NPHP19 patients also manifest hepatosplenomegaly, hepatic
CC fibrosis, destruction of the bile ducts, focal bile ductal
CC proliferation, ductal plate malformation, and cholestasis.
CC {ECO:0000269|PubMed:25557784}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal recessive, 66 (DFNB66) [MIM:610212]: A
CC form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner ear,
CC the nerve pathways to the brain, or the area of the brain that receives
CC sound information. {ECO:0000269|PubMed:25601850}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Sclerosing cholangitis, neonatal (NSC) [MIM:617394]: An
CC autosomal recessive form of liver disease with onset in infancy.
CC Affected infants have jaundice, cholestasis, acholic stools, and
CC progressive liver dysfunction resulting in fibrosis and cirrhosis.
CC Cholangiography shows patent biliary ducts, but there are bile duct
CC irregularities. {ECO:0000269|PubMed:27319779,
CC ECO:0000269|PubMed:27469900}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB61371.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF181720; AAF23610.1; -; Genomic_DNA.
DR EMBL; AF181721; AAF23612.1; -; mRNA.
DR EMBL; AB032980; BAA86468.2; -; mRNA.
DR EMBL; AL133043; CAB61371.1; ALT_INIT; mRNA.
DR EMBL; AL359389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO393410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050704; AAH50704.1; -; mRNA.
DR CCDS; CCDS4550.1; -. [Q9UHG0-1]
DR PIR; T42643; T42643.
DR RefSeq; NP_001182539.1; NM_001195610.1. [Q9UHG0-1]
DR RefSeq; NP_057440.2; NM_016356.4. [Q9UHG0-1]
DR PDB; 2DNF; NMR; -; A=132-226.
DR PDBsum; 2DNF; -.
DR AlphaFoldDB; Q9UHG0; -.
DR SMR; Q9UHG0; -.
DR BioGRID; 119558; 27.
DR CORUM; Q9UHG0; -.
DR IntAct; Q9UHG0; 28.
DR STRING; 9606.ENSP00000367715; -.
DR iPTMnet; Q9UHG0; -.
DR PhosphoSitePlus; Q9UHG0; -.
DR BioMuta; DCDC2; -.
DR DMDM; 147744557; -.
DR jPOST; Q9UHG0; -.
DR MassIVE; Q9UHG0; -.
DR MaxQB; Q9UHG0; -.
DR PaxDb; Q9UHG0; -.
DR PeptideAtlas; Q9UHG0; -.
DR PRIDE; Q9UHG0; -.
DR ProteomicsDB; 84347; -. [Q9UHG0-1]
DR ProteomicsDB; 84348; -. [Q9UHG0-2]
DR Antibodypedia; 25259; 254 antibodies from 28 providers.
DR DNASU; 51473; -.
DR Ensembl; ENST00000378450.6; ENSP00000367711.3; ENSG00000146038.12. [Q9UHG0-2]
DR Ensembl; ENST00000378454.8; ENSP00000367715.3; ENSG00000146038.12. [Q9UHG0-1]
DR GeneID; 51473; -.
DR KEGG; hsa:51473; -.
DR MANE-Select; ENST00000378454.8; ENSP00000367715.3; NM_016356.5; NP_057440.2.
DR UCSC; uc003ndx.4; human. [Q9UHG0-1]
DR CTD; 51473; -.
DR DisGeNET; 51473; -.
DR GeneCards; DCDC2; -.
DR GeneReviews; DCDC2; -.
DR HGNC; HGNC:18141; DCDC2.
DR HPA; ENSG00000146038; Tissue enhanced (kidney, pancreas).
DR MalaCards; DCDC2; -.
DR MIM; 600202; phenotype.
DR MIM; 605755; gene.
DR MIM; 610212; phenotype.
DR MIM; 616217; phenotype.
DR MIM; 617394; phenotype.
DR neXtProt; NX_Q9UHG0; -.
DR OpenTargets; ENSG00000146038; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR Orphanet; 480556; Isolated neonatal sclerosing cholangitis.
DR Orphanet; 84081; Senior-Boichis syndrome.
DR PharmGKB; PA134978716; -.
DR VEuPathDB; HostDB:ENSG00000146038; -.
DR eggNOG; KOG3757; Eukaryota.
DR GeneTree; ENSGT00940000159377; -.
DR HOGENOM; CLU_105460_0_0_1; -.
DR InParanoid; Q9UHG0; -.
DR OMA; SYGQKAS; -.
DR OrthoDB; 894392at2759; -.
DR PhylomeDB; Q9UHG0; -.
DR TreeFam; TF338406; -.
DR PathwayCommons; Q9UHG0; -.
DR SignaLink; Q9UHG0; -.
DR SIGNOR; Q9UHG0; -.
DR BioGRID-ORCS; 51473; 7 hits in 1064 CRISPR screens.
DR ChiTaRS; DCDC2; human.
DR EvolutionaryTrace; Q9UHG0; -.
DR GeneWiki; DCDC2; -.
DR GenomeRNAi; 51473; -.
DR Pharos; Q9UHG0; Tbio.
DR PRO; PR:Q9UHG0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UHG0; protein.
DR Bgee; ENSG00000146038; Expressed in secondary oocyte and 116 other tissues.
DR ExpressionAtlas; Q9UHG0; baseline and differential.
DR Genevisible; Q9UHG0; HS.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0060091; C:kinocilium; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:GO_Central.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR033036; DCDC2.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR PANTHER; PTHR23004:SF5; PTHR23004:SF5; 1.
DR Pfam; PF03607; DCX; 2.
DR SMART; SM00537; DCX; 2.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Deafness;
KW Disease variant; Nephronophthisis; Neurogenesis; Non-syndromic deafness;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..476
FT /note="Doublecortin domain-containing protein 2"
FT /id="PRO_0000079804"
FT DOMAIN 17..100
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 139..221
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT REGION 234..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZR10"
FT VAR_SEQ 1..247
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014670"
FT VAR_SEQ 248..307
FT /note="RKSKGSGNDRHSKSTVGSSDNSSPQPLKRKGKKEDVNSEKLTKLKQNVKLKN
FT SQETIPNS -> MKMWNNWGWCGGRRRGCTKILSTKKGIQMSIKNKHLIVIPAFSHTMS
FT QLDFDFHCVFVSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014671"
FT VARIANT 17
FT /note="K -> N (in NSC; loss of localization to the cilium
FT axoneme; dbSNP:rs1042640142)"
FT /evidence="ECO:0000269|PubMed:27319779"
FT /id="VAR_077245"
FT VARIANT 152
FT /note="P -> A (in dbSNP:rs33914824)"
FT /id="VAR_050946"
FT VARIANT 217..476
FT /note="Missing (in NSC)"
FT /evidence="ECO:0000269|PubMed:27469900"
FT /id="VAR_078767"
FT VARIANT 221
FT /note="S -> G (in dbSNP:rs2274305)"
FT /evidence="ECO:0000269|PubMed:10574461,
FT ECO:0000269|PubMed:10601354, ECO:0000269|PubMed:15489334"
FT /id="VAR_022890"
FT VARIANT 297..476
FT /note="Missing (in NSC)"
FT /evidence="ECO:0000269|PubMed:27469900"
FT /id="VAR_078768"
FT VARIANT 424
FT /note="Q -> P (in DFNB66; results in ciliary abnormalities
FT including increased ciliary length; dbSNP:rs794729665)"
FT /evidence="ECO:0000269|PubMed:25601850"
FT /id="VAR_074667"
FT VARIANT 456
FT /note="K -> N (in dbSNP:rs9460973)"
FT /id="VAR_050947"
FT CONFLICT 71
FT /note="G -> D (in Ref. 6; AAH50704)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="N -> K (in Ref. 4; CAB61371)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="Q -> R (in Ref. 4; CAB61371)"
FT /evidence="ECO:0000305"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2DNF"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2DNF"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2DNF"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2DNF"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:2DNF"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:2DNF"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2DNF"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:2DNF"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2DNF"
SQ SEQUENCE 476 AA; 52834 MW; 50DD06EA2FB9BD53 CRC64;
MSGSSARSSH LSQPVVKSVL VYRNGDPFYA GRRVVIHEKK VSSFEVFLKE VTGGVQAPFG
AVRNIYTPRT GHRIRKLDQI QSGGNYVAGG QEAFKKLNYL DIGEIKKRPM EVVNTEVKPV
IHSRINVSAR FRKPLQEPCT IFLIANGDLI NPASRLLIPR KTLNQWDHVL QMVTEKITLR
SGAVHRLYTL EGKLVESGAE LENGQFYVAV GRDKFKKLPY SELLFDKSTM RRPFGQKASS
LPPIVGSRKS KGSGNDRHSK STVGSSDNSS PQPLKRKGKK EDVNSEKLTK LKQNVKLKNS
QETIPNSDEG IFKAGAERSE TRGAAEVQED EDTQVEVPVD QRPAEIVDEE EDGEKANKDA
EQKEDFSGMN GDLEEEGGRE ATDAPEQVEE ILDHSEQQAR PARVNGGTDE ENGEELQQVN
NELQLVLDKE RKSQGAGSGQ DEADVDPQRP PRPEVKITSP EENENNQQNK DYAAVA
