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Neuronal migration protein doublecortin (Doublin) (Lissencephalin-X) (Lis-X)

 DCX_MOUSE               Reviewed;         366 AA.
O88809; Q6E5A4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
20-JUN-2018, entry version 151.
RecName: Full=Neuronal migration protein doublecortin;
AltName: Full=Doublin;
AltName: Full=Lissencephalin-X;
Short=Lis-X;
Name=Dcx; Synonyms=Dcn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Hippocampus;
PubMed=9837748; DOI=10.1006/bbrc.1998.9698;
Matsuo N., Kawamoto S., Matsubara K., Okubo K.;
"Cloning and developmental expression of the murine homolog of
doublecortin.";
Biochem. Biophys. Res. Commun. 252:571-576(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=9668176; DOI=10.1093/hmg/7.8.1327;
Sossey-Alaoui K., Hartung A.J., Guerrini R., Manchester D.K.,
Posar A., Puche-Mira A., Andermann E., Dobyns W.B., Srivastava A.K.;
"Human doublecortin (DCX) and the homologous gene in mouse encode a
putative Ca2+-dependent signaling protein which is mutated in human X-
linked neuronal migration defects.";
Hum. Mol. Genet. 7:1327-1332(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-28; SER-287;
THR-289; SER-297; THR-326; SER-332 AND SER-339, AND MUTAGENESIS OF
SER-28; SER-287; THR-289; SER-297; THR-326; SER-332; THR-336 AND
SER-339.
STRAIN=Swiss Webster; TISSUE=Embryo;
PubMed=15099191; DOI=10.1042/BJ20040324;
Graham M.E., Ruma-Haynes P., Capes-Davis A.G., Dunn J.M., Tan T.C.,
Valova V.A., Robinson P.J., Jeffrey P.L.;
"Multisite phosphorylation of doublecortin by cyclin-dependent kinase
5.";
Biochem. J. 381:471-481(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-339, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
PHOSPHORYLATION AT SER-265 AND SER-297.
PubMed=22807455; DOI=10.1002/pmic.201200003;
Goswami T., Li X., Smith A.M., Luderowski E.M., Vincent J.J., Rush J.,
Ballif B.A.;
"Comparative phosphoproteomic analysis of neonatal and adult murine
brain.";
Proteomics 12:2185-2189(2012).
[8]
UBIQUITINATION.
PubMed=25088421; DOI=10.1016/j.celrep.2014.06.056;
Yoshihara S., Takahashi H., Nishimura N., Kinoshita M., Asahina R.,
Kitsuki M., Tatsumi K., Furukawa-Hibi Y., Hirai H., Nagai T.,
Yamada K., Tsuboi A.;
"Npas4 regulates Mdm2 and thus Dcx in experience-dependent dendritic
spine development of newborn olfactory bulb interneurons.";
Cell Rep. 8:843-857(2014).
-!- FUNCTION: Microtubule-associated protein required for initial
steps of neuronal dispersion and cortex lamination during cerebral
cortex development. May act by competing with the putative
neuronal protein kinase DCLK1 in binding to a target protein. May
in that way participate in a signaling pathway that is crucial for
neuronal interaction before and during migration, possibly as part
of a calcium ion-dependent signal transduction pathway. May
participate along with PAFAH1B1/LIS-1 in a distinct overlapping
signaling pathway that promotes neuronal migration.
{ECO:0000250|UniProtKB:Q9ESI7}.
-!- SUBUNIT: Interacts with tubulin. Interacts with USP9X.
{ECO:0000250|UniProtKB:O43602}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection
{ECO:0000250|UniProtKB:Q9ESI7}. Note=Localizes at neurite tips.
{ECO:0000250|UniProtKB:Q9ESI7}.
-!- TISSUE SPECIFICITY: In neonatal tissues, highly expressed in
brain, but not expressed in heart, liver, kidney and spleen. In
adult tissues, faintly expressed in brain but not expressed in
muscle, heart, lung, liver, spleen, intestine, kidney, testis and
placenta.
-!- DEVELOPMENTAL STAGE: Already expressed by embryonic day 11 (E11),
maximally around birth, expression decreasing gradually during the
second postnatal week, with no expression in adult stages.
-!- PTM: Phosphorylation by MARK1, MARK2 and PKA regulates its ability
to bind microtubules (By similarity). Phosphorylation at Ser-265
and Ser-297 seems to occur only in neonatal brain, the levels
falling precipitously by postnatal day 21 (PubMed:15099191,
PubMed:22807455). {ECO:0000250|UniProtKB:Q9ESI7,
ECO:0000269|PubMed:15099191, ECO:0000269|PubMed:22807455}.
-!- PTM: Ubiquitinated by MDM2, leading to its degradation by the
proteasome (PubMed:25088421). Ubiquitinated by MDM2 and subsequent
degradation leads to reduce the dendritic spine density of
olfactory bulb granule cells (PubMed:25088421).
{ECO:0000269|PubMed:25088421}.
-----------------------------------------------------------------------
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EMBL; AB011678; BAA33387.1; -; mRNA.
EMBL; AF045547; AAC31799.1; -; mRNA.
EMBL; AY560329; AAT58219.1; -; mRNA.
EMBL; BX530055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS53209.1; -.
PIR; JE0368; JE0368.
RefSeq; NP_001103692.1; NM_001110222.1.
RefSeq; NP_001103693.1; NM_001110223.1.
RefSeq; NP_001103694.1; NM_001110224.1.
RefSeq; NP_034155.2; NM_010025.2.
UniGene; Mm.12871; -.
ProteinModelPortal; O88809; -.
SMR; O88809; -.
BioGrid; 199073; 10.
IntAct; O88809; 5.
STRING; 10090.ENSMUSP00000033642; -.
iPTMnet; O88809; -.
PhosphoSitePlus; O88809; -.
PaxDb; O88809; -.
PeptideAtlas; O88809; -.
PRIDE; O88809; -.
Ensembl; ENSMUST00000033642; ENSMUSP00000033642; ENSMUSG00000031285.
Ensembl; ENSMUST00000087313; ENSMUSP00000084570; ENSMUSG00000031285.
GeneID; 13193; -.
KEGG; mmu:13193; -.
UCSC; uc033jun.1; mouse.
CTD; 1641; -.
MGI; MGI:1277171; Dcx.
eggNOG; KOG3757; Eukaryota.
eggNOG; ENOG410ZE6Q; LUCA.
GeneTree; ENSGT00840000129744; -.
HOVERGEN; HBG003790; -.
InParanoid; O88809; -.
KO; K16579; -.
OMA; CRVMKGS; -.
OrthoDB; EOG091G02RF; -.
PhylomeDB; O88809; -.
TreeFam; TF318770; -.
ChiTaRS; Dcx; mouse.
PRO; PR:O88809; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031285; -.
CleanEx; MM_DCN; -.
CleanEx; MM_DCX; -.
ExpressionAtlas; O88809; baseline and differential.
Genevisible; O88809; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0048675; P:axon extension; IGI:MGI.
GO; GO:0007420; P:brain development; IGI:MGI.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IGI:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
GO; GO:0021766; P:hippocampus development; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
GO; GO:0001764; P:neuron migration; IGI:MGI.
GO; GO:0048672; P:positive regulation of collateral sprouting; ISO:MGI.
GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
GO; GO:0021860; P:pyramidal neuron development; IGI:MGI.
CDD; cd01617; DCX; 2.
Gene3D; 3.10.20.230; -; 2.
InterPro; IPR017302; Doublecortin_chordata.
InterPro; IPR003533; Doublecortin_dom.
InterPro; IPR036572; Doublecortin_dom_sf.
Pfam; PF03607; DCX; 2.
PIRSF; PIRSF037870; Doublin; 1.
SMART; SM00537; DCX; 2.
SUPFAM; SSF89837; SSF89837; 2.
PROSITE; PS50309; DC; 2.
1: Evidence at protein level;
Cell projection; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; Microtubule; Neurogenesis; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 366 Neuronal migration protein doublecortin.
/FTId=PRO_0000079834.
DOMAIN 53 139 Doublecortin 1. {ECO:0000255|PROSITE-
ProRule:PRU00072}.
DOMAIN 180 263 Doublecortin 2. {ECO:0000255|PROSITE-
ProRule:PRU00072}.
COMPBIAS 287 342 Pro/Ser-rich.
MOD_RES 28 28 Phosphoserine; by CDK5.
{ECO:0000269|PubMed:15099191}.
MOD_RES 47 47 Phosphoserine; by MARK1 and PKA.
{ECO:0000250|UniProtKB:Q9ESI7}.
MOD_RES 70 70 Phosphotyrosine; by ABL. {ECO:0000255}.
MOD_RES 74 74 Phosphoserine; by PKC. {ECO:0000255}.
MOD_RES 90 90 Phosphoserine; by CK2. {ECO:0000255}.
MOD_RES 110 110 Phosphoserine; by PKC. {ECO:0000255}.
MOD_RES 115 115 Phosphoserine; by CK2, MARK1 and PKA.
{ECO:0000250|UniProtKB:Q9ESI7}.
MOD_RES 265 265 Phosphoserine; by CK2.
{ECO:0000269|PubMed:22807455}.
MOD_RES 287 287 Phosphoserine; by CDK5.
{ECO:0000269|PubMed:15099191}.
MOD_RES 289 289 Phosphothreonine; by CDK5.
{ECO:0000269|PubMed:15099191}.
MOD_RES 294 294 Phosphoserine; by PKC. {ECO:0000255}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000269|PubMed:15099191,
ECO:0000269|PubMed:22807455}.
MOD_RES 297 297 Phosphoserine; by CDK5.
{ECO:0000269|PubMed:15099191,
ECO:0000269|PubMed:22807455}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:15345747}.
MOD_RES 326 326 Phosphothreonine; by CDK5.
{ECO:0000269|PubMed:15099191}.
MOD_RES 326 326 Phosphothreonine; by PKC and MAPK.
{ECO:0000255}.
MOD_RES 332 332 Phosphoserine; by CDK5.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15099191}.
MOD_RES 332 332 Phosphoserine; by MAPK. {ECO:0000255}.
MOD_RES 336 336 Phosphothreonine; by MAPK. {ECO:0000255}.
MOD_RES 339 339 Phosphoserine; by CDK5.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15099191}.
MOD_RES 339 339 Phosphoserine; by MAPK. {ECO:0000255}.
MOD_RES 342 342 Phosphoserine; by PKC. {ECO:0000255}.
MOD_RES 355 355 Phosphoserine; by CK2. {ECO:0000255}.
MOD_RES 361 361 Phosphoserine; by CK2. {ECO:0000255}.
MUTAGEN 28 28 S->A: Reduces overall phosphorylation by
25%. {ECO:0000269|PubMed:15099191}.
MUTAGEN 287 287 S->A: No effect on overall
phosphorylation.
{ECO:0000269|PubMed:15099191}.
MUTAGEN 289 289 T->A: No effect on overall
phosphorylation.
{ECO:0000269|PubMed:15099191}.
MUTAGEN 297 297 S->A: No effect on overall
phosphorylation.
{ECO:0000269|PubMed:15099191}.
MUTAGEN 326 326 T->A: No effect on overall
phosphorylation.
{ECO:0000269|PubMed:15099191}.
MUTAGEN 332 332 S->A: No effect on overall
phosphorylation. Reduces overall
phosphorylation by 36%; when associated
with A-339.
{ECO:0000269|PubMed:15099191}.
MUTAGEN 336 336 T->A: No effect on overall
phosphorylation.
{ECO:0000269|PubMed:15099191}.
MUTAGEN 339 339 S->A: No effect on overall
phosphorylation. Reduces overall
phosphorylation by 36%; when associated
with A-332.
{ECO:0000269|PubMed:15099191}.
CONFLICT 345 345 K -> R (in Ref. 2; AAC31799).
{ECO:0000305}.
CONFLICT 348 348 Missing (in Ref. 2; AAC31799).
{ECO:0000305}.
SEQUENCE 366 AA; 40613 MW; 323D0774C222F295 CRC64;
MELDFGHFDE RDKASRNMRG SRMNGLPSPT HSAHCSFYRT RTLQALSNEK KAKKVRFYRN
GDRYFKGIVY AVSSDRFRSF DALLADLTRS LSDNINLPQG VRYIYTIDGS RKIGSMDELE
EGESYVCSSD NFFKKVEYTK NVNPNWSVNV KTSANMKAPQ SLASSNSAQA RENKDFVRPK
LVTIIRSGVK PRKAVRVLLN KKTAHSFEQV LTDITEAIKL ETGVVKKLYT LDGKQVTCLH
DFFGDDDVFI ACGPEKFRYA QDDFSLDENE CRVMKGNPSA AAGPKASPTP QKTSAKSPGP
MRRSKSPADS GNDQDANGTS SSQLSTPKSK QSPISTPTSP GSLRKHKVDL YLPLSLDDSD
SLGDSM


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