NUDC_MOUSE
ID NUDC_MOUSE Reviewed; 332 AA.
AC O35685; Q3UJS7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Nuclear migration protein nudC;
DE AltName: Full=Nuclear distribution protein C homolog;
DE AltName: Full=Silica-induced gene 92 protein;
DE Short=SIG-92;
GN Name=Nudc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Macrophage;
RX PubMed=7868905;
RA Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S.;
RT "Isolation of nine gene sequences induced by silica in murine
RT macrophages.";
RL J. Immunol. 154:2384-2392(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PAFAH1B1, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Lung, and T-cell;
RX PubMed=9601647; DOI=10.1016/s0960-9822(98)70232-5;
RA Morris S.M., Albrecht U., Reiner O., Eichele G., Yu-Lee L.-Y.;
RT "The lissenchephaly gene product Lis1, a protein involved in neuronal
RT migration, interacts with a nuclear movement protein, NudC.";
RL Curr. Biol. 8:603-606(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DYNEIN, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11734602; DOI=10.1523/jneurosci.21-24-j0002.2001;
RA Aumais J.P., Tunstead J.R., McNeil R.S., Schaar B.T., McConnell S.K.,
RA Lin S.-H., Clark G.D., Yu-Lee L.-Y.;
RT "NudC associates with Lis1 and the dynein motor at the leading pole of
RT neurons.";
RL J. Neurosci. 21:RC187-RC187(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP STRUCTURE BY NMR OF 171-288.
RG RIKEN structural genomics initiative (RSGI);
RT "Nuclear move domain of nuclear distribution gene C homolog.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Plays a role in neurogenesis and neuronal migration
CC (PubMed:11734602). Necessary for correct formation of mitotic spindles
CC and chromosome separation during mitosis (By similarity). Necessary for
CC cytokinesis and cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y266, ECO:0000269|PubMed:11734602}.
CC -!- SUBUNIT: Interacts with PLK1 (By similarity). Interacts with PAFAH1B1
CC (PubMed:9601647). Part of a complex containing PLK1, NUDC, dynein and
CC dynactin (PubMed:11734602). Interacts with DCDC1 (By similarity).
CC Interacts with EML4 (via WD repeats) (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y266, ECO:0000269|PubMed:11734602,
CC ECO:0000269|PubMed:9601647}.
CC -!- INTERACTION:
CC O35685; Q61768: Kif5b; NbExp=4; IntAct=EBI-911192, EBI-776129;
CC O35685; Q61206: Pafah1b2; NbExp=2; IntAct=EBI-911192, EBI-7445518;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9Y266}. Midbody {ECO:0000250|UniProtKB:Q9Y266}.
CC Note=A small proportion is nuclear, in a punctate pattern (By
CC similarity). In a filamentous pattern adjacent to the nucleus of
CC migrating cerebellar granule cells. Colocalizes with tubulin and dynein
CC and with the microtubule organizing center. Distributed throughout the
CC cytoplasm of non-migrating cells (By similarity). Localizes to the
CC mitotic spindle in a EML4-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y266}.
CC -!- TISSUE SPECIFICITY: Detected in fetal and adult brain, in particular in
CC the ventricular zone of the embryonic forebrain and in the embryonic
CC cortical plate. Highly expressed in brain cortex from new born and
CC adult mice. Detected in the choroid plexus and in ependymal cells in
CC embryonic brain. {ECO:0000269|PubMed:11734602,
CC ECO:0000269|PubMed:9601647}.
CC -!- INDUCTION: Up-regulated in silica-treated macrophages.
CC {ECO:0000269|PubMed:7868905}.
CC -!- PTM: Reversibly phosphorylated on serine residues during the M phase of
CC the cell cycle. Phosphorylation on Ser-275 and Ser-327 is necessary for
CC correct formation of mitotic spindles and chromosome separation during
CC mitosis. Phosphorylated by PLK and other kinases (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y266}.
CC -!- SIMILARITY: Belongs to the nudC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X81443; CAA57201.1; -; mRNA.
DR EMBL; Y15522; CAA75677.1; -; mRNA.
DR EMBL; AK032673; BAC27981.1; -; mRNA.
DR EMBL; AK146323; BAE27078.1; -; mRNA.
DR EMBL; BC011253; AAH11253.1; -; mRNA.
DR CCDS; CCDS18750.1; -.
DR RefSeq; NP_035078.1; NM_010948.3.
DR PDB; 1WFI; NMR; -; A=171-288.
DR PDB; 2CR0; NMR; -; A=161-268.
DR PDBsum; 1WFI; -.
DR PDBsum; 2CR0; -.
DR AlphaFoldDB; O35685; -.
DR SMR; O35685; -.
DR BioGRID; 201876; 23.
DR IntAct; O35685; 8.
DR MINT; O35685; -.
DR STRING; 10090.ENSMUSP00000030665; -.
DR iPTMnet; O35685; -.
DR PhosphoSitePlus; O35685; -.
DR REPRODUCTION-2DPAGE; O35685; -.
DR EPD; O35685; -.
DR jPOST; O35685; -.
DR MaxQB; O35685; -.
DR PaxDb; O35685; -.
DR PeptideAtlas; O35685; -.
DR PRIDE; O35685; -.
DR ProteomicsDB; 287852; -.
DR Antibodypedia; 30707; 406 antibodies from 37 providers.
DR DNASU; 18221; -.
DR Ensembl; ENSMUST00000030665; ENSMUSP00000030665; ENSMUSG00000028851.
DR GeneID; 18221; -.
DR KEGG; mmu:18221; -.
DR UCSC; uc012dmm.1; mouse.
DR CTD; 10726; -.
DR MGI; MGI:106014; Nudc.
DR VEuPathDB; HostDB:ENSMUSG00000028851; -.
DR eggNOG; KOG2265; Eukaryota.
DR GeneTree; ENSGT00940000155361; -.
DR HOGENOM; CLU_047332_1_0_1; -.
DR InParanoid; O35685; -.
DR OMA; KPEDSIW; -.
DR OrthoDB; 1474731at2759; -.
DR PhylomeDB; O35685; -.
DR TreeFam; TF300147; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 18221; 22 hits in 70 CRISPR screens.
DR ChiTaRS; Nudc; mouse.
DR EvolutionaryTrace; O35685; -.
DR PRO; PR:O35685; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O35685; protein.
DR Bgee; ENSMUSG00000028851; Expressed in yolk sac and 118 other tissues.
DR Genevisible; O35685; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR032572; NuDC.
DR InterPro; IPR037898; NudC_fam.
DR InterPro; IPR025934; NudC_N_dom.
DR PANTHER; PTHR12356; PTHR12356; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF16273; NuDC; 1.
DR Pfam; PF14050; Nudc_N; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..332
FT /note="Nuclear migration protein nudC"
FT /id="PRO_0000057991"
FT DOMAIN 168..259
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 65..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..332
FT /note="Interaction with EML4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT COILED 60..134
FT /evidence="ECO:0000255"
FT MOTIF 68..74
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 70..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 240
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1WFI"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:1WFI"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1WFI"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1WFI"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1WFI"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2CR0"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1WFI"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1WFI"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:1WFI"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1WFI"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1WFI"
SQ SEQUENCE 332 AA; 38358 MW; 83F30F2D8E013E3A CRC64;
MGGEQEEERF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFIGGEEGM AEKLITQTFN
HHNQLAQKAR REKRARQETE RREKAERAAR LAKEAKAETP GPQIKELTDE EAERLQLEID
QKKDAEDQEA QLKNGSLDSP GKQDAEDEED EEDEKDKGKL KPNLGNGADL PNYRWTQTLA
ELDLAVPFRV SFRLKGKDVV VDIQRRHLRV GLKGQPPVVD GELYNEVKVE ESSWLIEDGK
VVTVHLEKIN KMEWWNRLVT SDPEINTKKI NPENSKLSDL DSETRSMVEK MMYDQRQKSM
GLPTSDEQKK QEILKKFMDQ HPEMDFSKAK FN
