DCX_RAT
ID DCX_RAT Reviewed; 365 AA.
AC Q9ESI7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Neuronal migration protein doublecortin;
GN Name=Dcx;
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 [MRNA].
RC STRAIN=Sprague-Dawley;
RA Park S., Kim H., Kang Y., Chang Y.;
RT "Characterization of gene related with neuronal migration.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-47 AND SER-115, AND
RP MUTAGENESIS OF SER-47 AND SER-115.
RX PubMed=14741102; DOI=10.1016/s0896-6273(03)00843-2;
RA Schaar B.T., Kinoshita K., McConnell S.K.;
RT "Doublecortin microtubule affinity is regulated by a balance of kinase and
RT phosphatase activity at the leading edge of migrating neurons.";
RL Neuron 41:203-213(2004).
RN [3]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Microtubule-associated protein required for initial steps of
CC neuronal dispersion and cortex lamination during cerebral cortex
CC development. May act by competing with the putative neuronal protein
CC kinase DCLK1 in binding to a target protein. May in that way
CC participate in a signaling pathway that is crucial for neuronal
CC interaction before and during migration, possibly as part of a calcium
CC ion-dependent signal transduction pathway. May participate along with
CC PAFAH1B1/LIS-1 in a distinct overlapping signaling pathway that
CC promotes neuronal migration. {ECO:0000269|PubMed:14741102}.
CC -!- SUBUNIT: Interacts with tubulin. Interacts with USP9X.
CC {ECO:0000250|UniProtKB:O43602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection, neuron
CC projection {ECO:0000269|PubMed:14741102}. Note=Localizes at neurite
CC tips (PubMed:14741102).
CC -!- PTM: Phosphorylation by MARK1, MARK2 and PKA regulates its ability to
CC bind microtubules (PubMed:14741102). Phosphorylation at Ser-265 and
CC Ser-297 seems to occur only in neonatal brain, the levels falling
CC precipitously by postnatal day 21 (By similarity).
CC {ECO:0000250|UniProtKB:O88809, ECO:0000269|PubMed:14741102}.
CC -!- PTM: Ubiquitinated by MDM2, leading to its degradation by the
CC proteasome. Ubiquitinated by MDM2 and subsequent degradation leads to
CC reduce the dendritic spine density of olfactory bulb granule cells.
CC {ECO:0000250|UniProtKB:O88809}.
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DR EMBL; AF155959; AAG18479.2; -; mRNA.
DR AlphaFoldDB; Q9ESI7; -.
DR BMRB; Q9ESI7; -.
DR SMR; Q9ESI7; -.
DR IntAct; Q9ESI7; 1.
DR MINT; Q9ESI7; -.
DR STRING; 10116.ENSRNOP00000065381; -.
DR iPTMnet; Q9ESI7; -.
DR PhosphoSitePlus; Q9ESI7; -.
DR PaxDb; Q9ESI7; -.
DR PRIDE; Q9ESI7; -.
DR RGD; 620670; Dcx.
DR eggNOG; KOG3757; Eukaryota.
DR InParanoid; Q9ESI7; -.
DR PRO; PR:Q9ESI7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0035082; P:axoneme assembly; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0021819; P:layer formation in cerebral cortex; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; IMP:RGD.
DR GO; GO:0042461; P:photoreceptor cell development; IBA:GO_Central.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; IMP:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:0021860; P:pyramidal neuron development; ISO:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR017302; Doublecortin_chordata.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR040163; RP1/RP1L1/DCX.
DR PANTHER; PTHR23005; PTHR23005; 1.
DR Pfam; PF03607; DCX; 2.
DR PIRSF; PIRSF037870; Doublin; 1.
DR SMART; SM00537; DCX; 2.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Developmental protein; Differentiation;
KW Microtubule; Neurogenesis; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..365
FT /note="Neuronal migration protein doublecortin"
FT /id="PRO_0000079835"
FT DOMAIN 53..139
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 180..263
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT REGION 275..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 47
FT /note="Phosphoserine; by MARK1 and PKA"
FT /evidence="ECO:0000269|PubMed:14741102"
FT MOD_RES 70
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000255"
FT MOD_RES 74
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 90
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 110
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 115
FT /note="Phosphoserine; by CK2, MARK1 and PKA"
FT /evidence="ECO:0000269|PubMed:14741102"
FT MOD_RES 265
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 287
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 289
FT /note="Phosphothreonine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 294
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 297
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 306
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:O43602, ECO:0000255"
FT MOD_RES 306
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250"
FT MOD_RES 326
FT /note="Phosphothreonine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 326
FT /note="Phosphothreonine; by PKC and MAPK"
FT /evidence="ECO:0000255"
FT MOD_RES 332
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 332
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000255"
FT MOD_RES 336
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000255"
FT MOD_RES 339
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 339
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000255"
FT MOD_RES 342
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 354
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 360
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MUTAGEN 47
FT /note="S->A: Impairs phosphorylation by MARK1 and PKA; when
FT associated with A-115."
FT /evidence="ECO:0000269|PubMed:14741102"
FT MUTAGEN 115
FT /note="S->A: Impairs phosphorylation by MARK1 and PKA; when
FT associated with A-47."
FT /evidence="ECO:0000269|PubMed:14741102"
SQ SEQUENCE 365 AA; 40560 MW; 6FCF92406ECC57D0 CRC64;
MELDFGHFDE RDKASRNMRG SRMNGLPSPT HSAHCSFYRT RTLQALSNEK KAKKVRFYRN
GDRYFKGIVY AVSSDRFRSF DALLADLTRS LSDNINLLQG VRYIYTIDGS RKIGSMDELE
EGESYVCSSD NFFKKVEYTK NVNPNWSVNV KTSANMKAPQ SLASSNSAQA RENKDFVRPK
LVTIIRSGVK PRKAVRVLLN KKTAHSFEQV LTDITEAIKL ETGVVKKLYT LDGKQVTCLH
DFFGDDDVFI ACGPEKFRYA QDDFSLDENE CRVMKGNPSA TAGPKASPTP QKTSAKSPGP
MRRSKSPADS GNDQDANGTS SSQLSTPKSK QSPISTPTSP GSLRKHKDLY LPLSLDDSDS
LGDSM
