GENTAUR Molecular Products.

 NDEL1_RAT               Reviewed;         345 AA.
 Q78PB6; Q6IRI4;
 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
 05-JUL-2004, sequence version 1.
 18-JUL-2018, entry version 114.
 RecName: Full=Nuclear distribution protein nudE-like 1;
          Short=Protein Nudel;
 Name=Ndel1; Synonyms=Nude2, Nudel;
 Rattus norvegicus (Rat).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Rattus.
 NCBI_TaxID=10116;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
 STRAIN=Sprague-Dawley; TISSUE=Liver;
 Umezu M., Kitagawa M., Aoki J., Arai H.;
 "Functional analysis of NUDE that interacts with LIS1, the
 lissencephaly gene product.";
 Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
 TISSUE=Heart;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [3]
 INTERACTION WITH PAFAH1B1 AND DYNEIN, AND SUBCELLULAR LOCATION.
 TISSUE=Brain;
 PubMed=11163260; DOI=10.1016/S0896-6273(00)00147-1;
 Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
 Morabito M., Tsai L.-H.;
 "NUDEL is a novel cdk5 substrate that associates with LIS1 and
 cytoplasmic dynein.";
 Neuron 28:697-711(2000).
 [4]
 PUTATIVE FUNCTION AS AN OLIGOPEPTIDASE.
 PubMed=15728732; DOI=10.1073/pnas.0500330102;
 Hayashi M.A.F., Portaro F.C.V., Bastos M.F., Guerreiro J.R.,
 Oliveira V., Gorrao S.S., Tambourgi D.V., Sant'Anna O.A.,
 Whiting P.J., Camargo L.M., Konno K., Brandon N.J., de Camargo A.C.M.;
 "Inhibition of NUDEL (nuclear distribution element-like)-
 oligopeptidase activity by disrupted-in-schizophrenia 1.";
 Proc. Natl. Acad. Sci. U.S.A. 102:3828-3833(2005).
 [5]
 FUNCTION, INTERACTION WITH DISC1, INDUCTION, AND SUBCELLULAR LOCATION.
 PubMed=17035248; DOI=10.1093/hmg/ddl407;
 Kamiya A., Tomoda T., Chang J., Takaki M., Zhan C., Morita M.,
 Cascio M.B., Elashvili S., Koizumi H., Takanezawa Y., Dickerson F.,
 Yolken R., Arai H., Sawa A.;
 "DISC1-NDEL1/NUDEL protein interaction, an essential component for
 neurite outgrowth, is modulated by genetic variations of DISC1.";
 Hum. Mol. Genet. 15:3313-3323(2006).
 [6]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=22673903; DOI=10.1038/ncomms1871;
 Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
 Lundby C., Olsen J.V.;
 "Quantitative maps of protein phosphorylation sites across 14
 different rat organs and tissues.";
 Nat. Commun. 3:876-876(2012).
 -!- FUNCTION: Required for organization of the cellular microtubule
     array and microtubule anchoring at the centrosome. May regulate
     microtubule organization at least in part by targeting the
     microtubule severing protein KATNA1 to the centrosome. Also
     positively regulates the activity of the minus-end directed
     microtubule motor protein dynein. May enhance dynein-mediated
     microtubule sliding by targeting dynein to the microtubule plus
     ends. Required for several dynein- and microtubule-dependent
     processes such as the maintenance of Golgi integrity, the
     centripetal motion of secretory vesicles and the coupling of the
     nucleus and centrosome. Also required during brain development for
     the migration of newly formed neurons from the
     ventricular/subventricular zone toward the cortical plate.
     Required for mitosis in some cell types but appears to be
     dispensible for mitosis in cortical neuronal progenitors, which
     instead requires NDE1. Facilitates the polymerization of
     neurofilaments from the individual subunits NEFH and NEFL.
     Positively regulates lysosome peripheral distribution and ruffled
     border formation in osteoclasts (By similarity). Plays a role,
     together with DISC1, in the regulation of neurite outgrowth.
     {ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1,
     ECO:0000269|PubMed:17035248}.
 -!- SUBUNIT: Self-associates. Interacts with dynactin, tubulin gamma,
     KATNA1, KATNB1, microtubules, PCM1, PCNT, and YWHAE. Interacts
     directly with NEFL and indirectly with NEFH. Interacts (via C-
     terminus) with CENPF. Interacts with DISC1, dynein and PAFAH1B1.
     Interacts with ZNF365. Interacts with PLEKHM1 (via N- and C-
     terminus). {ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1}.
 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
     cytoskeleton, microtubule organizing center, centrosome.
     Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton,
     spindle. Note=Localizes to the mitotic spindle and to the
     microtubules of the manchette in elongated spermatids (By
     similarity). Localizes to the interphase centrosome. Localizes to
     the cell body of the motor neurons and colocalizes with assembled
     neurofilaments within axonal processes. Colocalizes with DISC1 in
     the perinuclear region, including the centrosome. {ECO:0000250}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=1;
       IsoId=Q78PB6-1; Sequence=Displayed;
     Name=2;
       IsoId=Q78PB6-2; Sequence=VSP_019312, VSP_019313;
       Note=No experimental confirmation available.;
 -!- INDUCTION: Up-regulated during neurite outgrowth upon
     differentiation with NGF. {ECO:0000269|PubMed:17035248}.
 -!- PTM: Phosphorylated in mitosis. Can be phosphorylated by CDK1,
     CDK5 and MAPK1. Phosphorylation by CDK5 promotes interaction with
     KATNA1 and YWHAE (By similarity). {ECO:0000250}.
 -!- PTM: Palmitoylation at Cys-273 reduces affinity for dynein.
     {ECO:0000250}.
 -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
 -!- CAUTION: Was originally thought to function as an oligopeptidase
     (NUDEL-oligopeptidase or endooligopeptidase A) which could
     regulate peptide levels relevant to brain function.
     {ECO:0000305|PubMed:15728732}.
 -----------------------------------------------------------------------
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 EMBL; AY008298; AAG21830.1; -; mRNA.
 EMBL; BC070909; AAH70909.1; -; mRNA.
 RefSeq; NP_579854.1; NM_133320.1. [Q78PB6-1]
 RefSeq; XP_006246640.1; XM_006246578.3. [Q78PB6-2]
 UniGene; Rn.2947; -.
 PDB; 2V71; X-ray; 2.24 A; A/B=8-193.
 PDBsum; 2V71; -.
 ProteinModelPortal; Q78PB6; -.
 SMR; Q78PB6; -.
 STRING; 10116.ENSRNOP00000005574; -.
 iPTMnet; Q78PB6; -.
 PhosphoSitePlus; Q78PB6; -.
 PaxDb; Q78PB6; -.
 PRIDE; Q78PB6; -.
 Ensembl; ENSRNOT00000005574; ENSRNOP00000005574; ENSRNOG00000004139. [Q78PB6-1]
 Ensembl; ENSRNOT00000065505; ENSRNOP00000062145; ENSRNOG00000004139. [Q78PB6-2]
 GeneID; 170845; -.
 KEGG; rno:170845; -.
 UCSC; RGD:621235; rat. [Q78PB6-1]
 CTD; 81565; -.
 RGD; 621235; Ndel1.
 eggNOG; KOG1853; Eukaryota.
 eggNOG; ENOG410XPMP; LUCA.
 GeneTree; ENSGT00390000000111; -.
 HOGENOM; HOG000280681; -.
 HOVERGEN; HBG082010; -.
 InParanoid; Q78PB6; -.
 KO; K16739; -.
 OMA; RTTVSMY; -.
 OrthoDB; EOG091G0GBV; -.
 PhylomeDB; Q78PB6; -.
 TreeFam; TF325693; -.
 Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
 Reactome; R-RNO-2467813; Separation of Sister Chromatids.
 Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
 Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
 Reactome; R-RNO-68877; Mitotic Prometaphase.
 EvolutionaryTrace; Q78PB6; -.
 PRO; PR:Q78PB6; -.
 Proteomes; UP000002494; Chromosome 10.
 Bgee; ENSRNOG00000004139; -.
 Genevisible; Q78PB6; RN.
 GO; GO:0030424; C:axon; IDA:RGD.
 GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
 GO; GO:0043203; C:axon hillock; IEA:Ensembl.
 GO; GO:0044297; C:cell body; IDA:RGD.
 GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
 GO; GO:0090724; C:central region of growth cone; IDA:RGD.
 GO; GO:0005813; C:centrosome; IDA:UniProtKB.
 GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO; GO:0005737; C:cytoplasm; IDA:RGD.
 GO; GO:0005829; C:cytosol; IDA:RGD.
 GO; GO:0005871; C:kinesin complex; IDA:RGD.
 GO; GO:0000776; C:kinetochore; IBA:GO_Central.
 GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO; GO:0060053; C:neurofilament cytoskeleton; IEA:Ensembl.
 GO; GO:0005635; C:nuclear envelope; IMP:MGI.
 GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
 GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
 GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
 GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
 GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
 GO; GO:0070012; F:oligopeptidase activity; IDA:RGD.
 GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
 GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
 GO; GO:0016477; P:cell migration; IBA:GO_Central.
 GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:Ensembl.
 GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
 GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl.
 GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
 GO; GO:0051303; P:establishment of chromosome localization; IBA:GO_Central.
 GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
 GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
 GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
 GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
 GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
 GO; GO:0007100; P:mitotic centrosome separation; IBA:GO_Central.
 GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
 GO; GO:0001764; P:neuron migration; IEA:Ensembl.
 GO; GO:0031175; P:neuron projection development; IMP:RGD.
 GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
 GO; GO:0051081; P:nuclear envelope disassembly; IDA:MGI.
 GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
 GO; GO:0048680; P:positive regulation of axon regeneration; IMP:RGD.
 GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:UniProtKB.
 GO; GO:0033157; P:regulation of intracellular protein transport; IEA:Ensembl.
 GO; GO:2000574; P:regulation of microtubule motor activity; IEA:InterPro.
 GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
 GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
 GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
 InterPro; IPR033493; NDEL1.
 InterPro; IPR033494; NUDE.
 InterPro; IPR006964; NUDE_dom.
 PANTHER; PTHR10921; PTHR10921; 1.
 PANTHER; PTHR10921:SF0; PTHR10921:SF0; 1.
 Pfam; PF04880; NUDE_C; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Centromere; Chromosome;
 Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
 Developmental protein; Differentiation; Kinetochore; Lipoprotein;
 Microtubule; Neurogenesis; Palmitate; Phosphoprotein;
 Reference proteome; Transport.
 CHAIN         1    345       Nuclear distribution protein nudE-like 1.
                              /FTId=PRO_0000240215.
 REGION       56    166       Self-association. {ECO:0000250}.
 REGION       64    189       Interaction with KATNB1. {ECO:0000250}.
 REGION      114    133       Required for interaction with PAFAH1B1.
                              {ECO:0000250}.
 REGION      175    345       Interaction with CENPF. {ECO:0000250}.
 REGION      189    256       Interaction with YWHAE. {ECO:0000250}.
 REGION      191    345       Interaction with NEFL. {ECO:0000250}.
 REGION      195    256       Interaction with KATNA1. {ECO:0000250}.
 REGION      227    278       Interaction with DISC1. {ECO:0000250}.
 REGION      256    291       Required for localization to the
                              centrosome and interaction with dynein,
                              dynactin, tubulin gamma, PCM1 and PCNT.
                              {ECO:0000250}.
 COILED       28    190       {ECO:0000255}.
 MOD_RES     215    215       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9GZM8}.
 MOD_RES     219    219       Phosphothreonine; by CDK1 and MAPK1.
                              {ECO:0000250|UniProtKB:Q9GZM8}.
 MOD_RES     231    231       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9GZM8}.
 MOD_RES     242    242       Phosphoserine; by CDK1.
                              {ECO:0000250|UniProtKB:Q9GZM8}.
 MOD_RES     245    245       Phosphothreonine; by CDK1 and MAPK1.
                              {ECO:0000250|UniProtKB:Q9GZM8}.
 MOD_RES     344    344       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 LIPID       273    273       S-palmitoyl cysteine; by ZDHHC2, ZDHHC3
                              and ZDHHC7. {ECO:0000250}.
 VAR_SEQ     316    328       AVNGFDPAPPPPG -> QEKVIFPTLFMGQ (in
                              isoform 2).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_019312.
 VAR_SEQ     329    345       Missing (in isoform 2).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_019313.
 CONFLICT     42     42       E -> Q (in Ref. 2; AAH70909).
                              {ECO:0000305}.
 HELIX        12    164       {ECO:0000244|PDB:2V71}.
 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

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