NDEL1_RAT
ID NDEL1_RAT Reviewed; 345 AA.
AC Q78PB6; Q6IRI4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Nuclear distribution protein nudE-like 1;
DE Short=Protein Nudel;
GN Name=Ndel1; Synonyms=Nude2, Nudel;
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] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Umezu M., Kitagawa M., Aoki J., Arai H.;
RT "Functional analysis of NUDE that interacts with LIS1, the lissencephaly
RT gene product.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
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 [3]
RP INTERACTION WITH PAFAH1B1 AND DYNEIN, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=11163260; DOI=10.1016/s0896-6273(00)00147-1;
RA Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
RA Morabito M., Tsai L.-H.;
RT "NUDEL is a novel cdk5 substrate that associates with LIS1 and cytoplasmic
RT dynein.";
RL Neuron 28:697-711(2000).
RN [4]
RP PUTATIVE FUNCTION AS AN OLIGOPEPTIDASE.
RX PubMed=15728732; DOI=10.1073/pnas.0500330102;
RA Hayashi M.A.F., Portaro F.C.V., Bastos M.F., Guerreiro J.R., Oliveira V.,
RA Gorrao S.S., Tambourgi D.V., Sant'Anna O.A., Whiting P.J., Camargo L.M.,
RA Konno K., Brandon N.J., de Camargo A.C.M.;
RT "Inhibition of NUDEL (nuclear distribution element-like)-oligopeptidase
RT activity by disrupted-in-schizophrenia 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3828-3833(2005).
RN [5]
RP FUNCTION, INTERACTION WITH DISC1, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17035248; DOI=10.1093/hmg/ddl407;
RA Kamiya A., Tomoda T., Chang J., Takaki M., Zhan C., Morita M., Cascio M.B.,
RA Elashvili S., Koizumi H., Takanezawa Y., Dickerson F., Yolken R., Arai H.,
RA Sawa A.;
RT "DISC1-NDEL1/NUDEL protein interaction, an essential component for neurite
RT outgrowth, is modulated by genetic variations of DISC1.";
RL Hum. Mol. Genet. 15:3313-3323(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, 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).
CC -!- FUNCTION: Required for organization of the cellular microtubule array
CC and microtubule anchoring at the centrosome. May regulate microtubule
CC organization at least in part by targeting the microtubule severing
CC protein KATNA1 to the centrosome. Also positively regulates the
CC activity of the minus-end directed microtubule motor protein dynein.
CC May enhance dynein-mediated microtubule sliding by targeting dynein to
CC the microtubule plus ends. Required for several dynein- and
CC microtubule-dependent processes such as the maintenance of Golgi
CC integrity, the centripetal motion of secretory vesicles and the
CC coupling of the nucleus and centrosome. Also required during brain
CC development for the migration of newly formed neurons from the
CC ventricular/subventricular zone toward the cortical plate. Required for
CC mitosis in some cell types but appears to be dispensible for mitosis in
CC cortical neuronal progenitors, which instead requires NDE1. Facilitates
CC the polymerization of neurofilaments from the individual subunits NEFH
CC and NEFL. Positively regulates lysosome peripheral distribution and
CC ruffled border formation in osteoclasts (By similarity). Plays a role,
CC together with DISC1, in the regulation of neurite outgrowth.
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1,
CC ECO:0000269|PubMed:17035248}.
CC -!- SUBUNIT: Self-associates. Interacts with dynactin, tubulin gamma,
CC KATNA1, KATNB1, microtubules, PCM1, PCNT, and YWHAE. Interacts directly
CC with NEFL and indirectly with NEFH. Interacts (via C-terminus) with
CC CENPF. Interacts with DISC1, dynein and PAFAH1B1. Interacts with
CC ZNF365. Interacts with PLEKHM1 (via N- and C-terminus). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ERR1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Chromosome, centromere,
CC kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the
CC mitotic spindle and to the microtubules of the manchette in elongated
CC spermatids (By similarity). Localizes to the interphase centrosome.
CC Localizes to the cell body of the motor neurons and colocalizes with
CC assembled neurofilaments within axonal processes. Colocalizes with
CC DISC1 in the perinuclear region, including the centrosome.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q78PB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q78PB6-2; Sequence=VSP_019312, VSP_019313;
CC -!- INDUCTION: Up-regulated during neurite outgrowth upon differentiation
CC with NGF. {ECO:0000269|PubMed:17035248}.
CC -!- PTM: Phosphorylated in mitosis. Can be phosphorylated by CDK1, CDK5 and
CC MAPK1. Phosphorylation by CDK5 promotes interaction with KATNA1 and
CC YWHAE (By similarity). {ECO:0000250}.
CC -!- PTM: Palmitoylation at Cys-273 reduces affinity for dynein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to function as an oligopeptidase
CC (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate
CC peptide levels relevant to brain function.
CC {ECO:0000305|PubMed:15728732}.
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DR EMBL; AY008298; AAG21830.1; -; mRNA.
DR EMBL; BC070909; AAH70909.1; -; mRNA.
DR RefSeq; NP_579854.1; NM_133320.1. [Q78PB6-1]
DR RefSeq; XP_006246640.1; XM_006246578.3. [Q78PB6-2]
DR PDB; 2V71; X-ray; 2.24 A; A/B=8-193.
DR PDBsum; 2V71; -.
DR AlphaFoldDB; Q78PB6; -.
DR SMR; Q78PB6; -.
DR IntAct; Q78PB6; 1.
DR MINT; Q78PB6; -.
DR STRING; 10116.ENSRNOP00000005574; -.
DR iPTMnet; Q78PB6; -.
DR PhosphoSitePlus; Q78PB6; -.
DR jPOST; Q78PB6; -.
DR PaxDb; Q78PB6; -.
DR PRIDE; Q78PB6; -.
DR Ensembl; ENSRNOT00000005574; ENSRNOP00000005574; ENSRNOG00000004139. [Q78PB6-2]
DR GeneID; 170845; -.
DR KEGG; rno:170845; -.
DR UCSC; RGD:621235; rat. [Q78PB6-1]
DR CTD; 81565; -.
DR RGD; 621235; Ndel1.
DR VEuPathDB; HostDB:ENSRNOG00000004139; -.
DR eggNOG; KOG1853; Eukaryota.
DR GeneTree; ENSGT00390000000111; -.
DR HOGENOM; CLU_057872_0_0_1; -.
DR InParanoid; Q78PB6; -.
DR OMA; EVEALKX; -.
DR OrthoDB; 1082224at2759; -.
DR PhylomeDB; Q78PB6; -.
DR TreeFam; TF325693; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR EvolutionaryTrace; Q78PB6; -.
DR PRO; PR:Q78PB6; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004139; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q78PB6; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043203; C:axon hillock; ISO:RGD.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0090724; C:central region of growth cone; IDA:RGD.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005871; C:kinesin complex; IDA:RGD.
DR GO; GO:0000776; C:kinetochore; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0060053; C:neurofilament cytoskeleton; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; IMP:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0070012; F:oligopeptidase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; ISO:RGD.
DR GO; GO:0051642; P:centrosome localization; ISO:RGD.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
DR GO; GO:0007059; P:chromosome segregation; ISO:RGD.
DR GO; GO:0051303; P:establishment of chromosome localization; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0001833; P:inner cell mass cell proliferation; ISO:RGD.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007100; P:mitotic centrosome separation; ISO:RGD.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR GO; GO:1990138; P:neuron projection extension; ISO:RGD.
DR GO; GO:0051081; P:nuclear membrane disassembly; IDA:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:UniProtKB.
DR GO; GO:0140650; P:radial glia-guided pyramidal neuron migration; IEA:Ensembl.
DR GO; GO:0033157; P:regulation of intracellular protein transport; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; ISO:RGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISO:RGD.
DR InterPro; IPR033493; NDEL1.
DR InterPro; IPR033494; NUDE.
DR InterPro; IPR006964; NUDE_dom.
DR PANTHER; PTHR10921; PTHR10921; 1.
DR PANTHER; PTHR10921:SF0; PTHR10921:SF0; 1.
DR Pfam; PF04880; NUDE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Centromere; Chromosome; Coiled coil;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW Kinetochore; Lipoprotein; Microtubule; Neurogenesis; Palmitate;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..345
FT /note="Nuclear distribution protein nudE-like 1"
FT /id="PRO_0000240215"
FT REGION 56..166
FT /note="Self-association"
FT /evidence="ECO:0000250"
FT REGION 64..189
FT /note="Interaction with KATNB1"
FT /evidence="ECO:0000250"
FT REGION 114..133
FT /note="Required for interaction with PAFAH1B1"
FT /evidence="ECO:0000250"
FT REGION 175..345
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000250"
FT REGION 189..256
FT /note="Interaction with YWHAE"
FT /evidence="ECO:0000250"
FT REGION 191..345
FT /note="Interaction with NEFL"
FT /evidence="ECO:0000250"
FT REGION 195..256
FT /note="Interaction with KATNA1"
FT /evidence="ECO:0000250"
FT REGION 217..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..278
FT /note="Interaction with DISC1"
FT /evidence="ECO:0000250"
FT REGION 256..291
FT /note="Required for localization to the centrosome and
FT interaction with dynein, dynactin, tubulin gamma, PCM1 and
FT PCNT"
FT /evidence="ECO:0000250"
FT REGION 314..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..190
FT /evidence="ECO:0000255"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 219
FT /note="Phosphothreonine; by CDK1 and MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 242
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 245
FT /note="Phosphothreonine; by CDK1 and MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 273
FT /note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7"
FT /evidence="ECO:0000250"
FT VAR_SEQ 316..328
FT /note="AVNGFDPAPPPPG -> QEKVIFPTLFMGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019312"
FT VAR_SEQ 329..345
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019313"
FT CONFLICT 42
FT /note="E -> Q (in Ref. 2; AAH70909)"
FT /evidence="ECO:0000305"
FT HELIX 12..164
FT /evidence="ECO:0007829|PDB:2V71"
SQ SEQUENCE 345 AA; 38366 MW; CB3059DFD998E9EC CRC64;
MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ
RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ
ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE
LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENSFP SPKAIPNGFG
TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYVPGS VNCGVMNSNG
PECPRSGRAT FFHKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV
