NDE1_RAT
ID NDE1_RAT Reviewed; 344 AA.
AC Q9ES39; Q642F3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Nuclear distribution protein nudE homolog 1;
DE Short=NudE;
DE Short=rNudE;
GN Name=Nde1; Synonyms=Nude, Nude1;
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], INTERACTION WITH PAFAH1B1, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10940388; DOI=10.1016/s0014-5793(00)01856-1;
RA Kitagawa M., Umezu M., Aoki J., Koizumi H., Arai H., Inoue K.;
RT "Direct association of LIS1, the lissencephaly gene product, with a
RT mammalian homologue of a fungal nuclear distribution protein, rNUDE.";
RL FEBS Lett. 479:57-62(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-314.
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).
CC -!- FUNCTION: Required for centrosome duplication and formation and
CC function of the mitotic spindle. Essential for the development of the
CC cerebral cortex. May regulate the production of neurons by controlling
CC the orientation of the mitotic spindle during division of cortical
CC neuronal progenitors of the proliferative ventricular zone of the
CC brain. Orientation of the division plane perpendicular to the layers of
CC the cortex gives rise to two proliferative neuronal progenitors whereas
CC parallel orientation of the division plane yields one proliferative
CC neuronal progenitor and a post-mitotic neuron. A premature shift
CC towards a neuronal fate within the progenitor population may result in
CC an overall reduction in the final number of neurons and an increase in
CC the number of neurons in the deeper layers of the cortex (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Self-associates. May interact with CENPF, CNTRL, LIS1,
CC dynactin, dynein, tubulin gamma, PCM1, PCNT, SLMAP and TCP1 (By
CC similarity). Interacts with PAFAH1B1. Interacts with ZNF365 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9ES39; P43033: PAFAH1B1; Xeno; NbExp=2; IntAct=EBI-1007897, EBI-1007886;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Cleavage furrow {ECO:0000250}.
CC Note=Localizes to the interphase and S phase centrosome. During
CC mitosis, partially associated with the mitotic spindle. Concentrates at
CC the plus ends of microtubules coincident with kinetochores in metaphase
CC and anaphase in a CENPF-dependent manner. Also localizes to the
CC cleavage furrow during cytokinesis (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC skeletal muscle, spleen and testis. {ECO:0000269|PubMed:10940388}.
CC -!- PTM: Phosphorylated in mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH81759.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF240463; AAG10105.1; -; mRNA.
DR EMBL; BC081759; AAH81759.1; ALT_SEQ; mRNA.
DR RefSeq; NP_445799.1; NM_053347.1.
DR RefSeq; XP_006245911.1; XM_006245849.3.
DR RefSeq; XP_006245912.1; XM_006245850.3.
DR RefSeq; XP_006245913.1; XM_006245851.2.
DR AlphaFoldDB; Q9ES39; -.
DR SMR; Q9ES39; -.
DR IntAct; Q9ES39; 2.
DR STRING; 10116.ENSRNOP00000000029; -.
DR PhosphoSitePlus; Q9ES39; -.
DR jPOST; Q9ES39; -.
DR PaxDb; Q9ES39; -.
DR PRIDE; Q9ES39; -.
DR GeneID; 83836; -.
DR KEGG; rno:83836; -.
DR UCSC; RGD:620038; rat.
DR CTD; 54820; -.
DR RGD; 620038; Nde1.
DR VEuPathDB; HostDB:ENSRNOG00000058007; -.
DR eggNOG; KOG1853; Eukaryota.
DR HOGENOM; CLU_057872_1_0_1; -.
DR InParanoid; Q9ES39; -.
DR OMA; CERPATL; -.
DR OrthoDB; 1082224at2759; -.
DR PhylomeDB; Q9ES39; -.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q9ES39; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000058007; Expressed in thymus and 19 other tissues.
DR Genevisible; Q9ES39; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0031616; C:spindle pole centrosome; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051303; P:establishment of chromosome localization; ISO:RGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0007020; P:microtubule nucleation; ISO:RGD.
DR GO; GO:0031023; P:microtubule organizing center organization; ISO:RGD.
DR GO; GO:0007100; P:mitotic centrosome separation; IBA:GO_Central.
DR GO; GO:0007405; P:neuroblast proliferation; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISO:RGD.
DR InterPro; IPR033494; NUDE.
DR InterPro; IPR006964; NUDE_dom.
DR PANTHER; PTHR10921; PTHR10921; 1.
DR Pfam; PF04880; NUDE_C; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Kinetochore;
KW Lipoprotein; Microtubule; Mitosis; Neurogenesis; Palmitate; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..344
FT /note="Nuclear distribution protein nudE homolog 1"
FT /id="PRO_0000240204"
FT REGION 1..93
FT /note="Self-association"
FT /evidence="ECO:0000250"
FT REGION 30..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..156
FT /note="Interaction with PAFAH1B1"
FT /evidence="ECO:0000250"
FT REGION 167..290
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000250"
FT REGION 181..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 18..188
FT /evidence="ECO:0000255"
FT COMPBIAS 30..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT LIPID 274
FT /note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7"
FT /evidence="ECO:0000250"
SQ SEQUENCE 344 AA; 38528 MW; 0A5E625751A24058 CRC64;
MEDSGKTFGS EEEETNYWRD LAMTYKQRAE NTQEELREFQ EGSREYEAEL ETQLQQAETR
NRDLLSENNR LRMELESVKE KFEMQHSEGY RQISALEDDL AHTKAIKDQL QKYIRELEQA
NDDLERAKRA TIMSLEDFEQ RLNQAIERNA FLESELDEKE NLLESVQRLK DEARDLRQEL
AVQQKQDKPR TPMPSSGETK RTDMAVQATG SAPSTPITHQ GSSSGLNTPE TFRCGLGSPS
SGTPLTPAAR ISALNIVGDL LRKVGALESK LASCKNFMYD QSPSRKSGPA LGRGTKNRDG
IDRRPGSTAV GDKGSGKRLE FAKPSSQLSS PALPSTQGVV KLLL
