DCDC2_RAT
ID DCDC2_RAT Reviewed; 475 AA.
AC D3ZR10;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Doublecortin domain-containing protein 2;
GN Name=Dcdc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Protein that plays a role in the inhibition of canonical Wnt
CC signaling pathway (By similarity). May be involved in neuronal
CC migration during development of the cerebral neocortex
CC (PubMed:16278297). Involved in the control of ciliogenesis and ciliary
CC length (By similarity). {ECO:0000250|UniProtKB:Q9UHG0,
CC ECO:0000269|PubMed:16278297}.
CC -!- SUBUNIT: Interacts with DVL1, DVL2 and DVL3.
CC {ECO:0000250|UniProtKB:Q9UHG0}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9UHG0}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q9UHG0}. Cell projection, kinocilium
CC {ECO:0000269|PubMed:25601850}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:25601850}. Note=Localizes to the ciliary axoneme
CC and to mitotic spindle fibers in a cell-cycle-dependent manner.
CC {ECO:0000250|UniProtKB:Q9UHG0}.
CC -!- TISSUE SPECIFICITY: Expressed in hair cells of the inner ear.
CC {ECO:0000269|PubMed:25601850}.
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DR EMBL; CH474064; EDL86488.1; -; Genomic_DNA.
DR RefSeq; NP_001099580.2; NM_001106110.2.
DR AlphaFoldDB; D3ZR10; -.
DR SMR; D3ZR10; -.
DR CORUM; D3ZR10; -.
DR STRING; 10116.ENSRNOP00000060289; -.
DR iPTMnet; D3ZR10; -.
DR PhosphoSitePlus; D3ZR10; -.
DR PaxDb; D3ZR10; -.
DR PRIDE; D3ZR10; -.
DR Ensembl; ENSRNOT00000068021; ENSRNOP00000060289; ENSRNOG00000017511.
DR GeneID; 291130; -.
DR KEGG; rno:291130; -.
DR CTD; 51473; -.
DR RGD; 1310227; Dcdc2.
DR eggNOG; KOG3757; Eukaryota.
DR GeneTree; ENSGT00940000159377; -.
DR HOGENOM; CLU_035041_3_0_1; -.
DR InParanoid; D3ZR10; -.
DR OMA; SYGQKAS; -.
DR OrthoDB; 894392at2759; -.
DR PhylomeDB; D3ZR10; -.
DR TreeFam; TF338406; -.
DR PRO; PR:D3ZR10; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000017511; Expressed in testis and 12 other tissues.
DR Genevisible; D3ZR10; RN.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0060091; C:kinocilium; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0019894; F:kinesin binding; IPI:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0019228; P:neuronal action potential; ISO:RGD.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:RGD.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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 Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Neurogenesis; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..475
FT /note="Doublecortin domain-containing protein 2"
FT /id="PRO_0000403481"
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..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 475 AA; 52033 MW; A29B7868D7F264D8 CRC64;
MNGPSPRSSH LSQPVVKSVL VYRNGDPFFA GRRVVIHEKK VSSFDIFLKE VTGGVQAPFG
AVRNIYTPRT GHRIRKLDQI ESGGNYVAGG QEAFKKLNYL DIGEIKKRPM EAVNTEVKPV
IHSKINVSAR FRKALHEPCT IFLIANGDLI SPASRLLIPR KALNQWDHVL QMVTEKITLR
SGAVHRLYTL EGKLVESGAE LENGQFYVAV GRDKFKRLPY SELLFDKSAM RRPYGQKASS
LPPMVGSRKS KGSGNYRQSK STIGSSDNSS PQPLKRKGKK DSNSEKPTKV KQSVKSKNSH
QAIPDNDEGI FKAGAERSET RGAAEVQEDE DTQVEVPVDQ RPAEIVDEEE DGEKTSKDAN
QKDDFSAMNG EAEDRAGSKV ADAPEEEEGI PDQGEKKASP SRVNGGTDEE NGEELDQVTE
ELQPTVDEKG KAEGDNSAQD EAGLDAQRPP RPEVTVTSPQ ENEGNESNKA SSAVA
