NUDC_RAT
ID NUDC_RAT Reviewed; 332 AA.
AC Q63525;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Nuclear migration protein nudC;
DE AltName: Full=Nuclear distribution protein C homolog;
DE AltName: Full=c15;
GN Name=Nudc;
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], INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Noble;
RX PubMed=7776977; DOI=10.1210/mend.9.3.7776977;
RA Axtell S.M., Truong T.M., O'Neal K.D., Yu-Lee L.-Y.;
RT "Characterization of a prolactin-inducible gene, clone 15, in T cells.";
RL Mol. Endocrinol. 9:312-318(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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.
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).
CC -!- FUNCTION: Plays a role in neurogenesis and neuronal migration.
CC Necessary for correct formation of mitotic spindles and chromosome
CC separation during mitosis (By similarity). Necessary for cytokinesis
CC and cell proliferation (By similarity). {ECO:0000250|UniProtKB:O35685,
CC ECO:0000250|UniProtKB:Q9Y266}.
CC -!- SUBUNIT: Interacts with PAFAH1B1 (PubMed:9601647). Interacts with PLK1
CC and DCDC1. Part of a complex containing PLK1, NUDC, dynein and dynactin
CC (By similarity). Interacts with EML4 (via WD repeats) (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y266, ECO:0000269|PubMed:9601647}.
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 (By similarity). Distributed
CC throughout the cytoplasm of non-migrating cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y266}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in stomach, small intestine,
CC spleen, liver, kidney, brain, heart and lung.
CC {ECO:0000269|PubMed:7776977}.
CC -!- INDUCTION: Up-regulated by prolactin in T-cell lymphoma. Maximum level
CC of expression occurs at the G1/S phase transition of the cell cycle.
CC {ECO:0000269|PubMed:7776977}.
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}.
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DR EMBL; X82445; CAA57825.1; -; mRNA.
DR EMBL; BC065581; AAH65581.1; -; mRNA.
DR PIR; A55897; A55897.
DR RefSeq; NP_058967.1; NM_017271.2.
DR AlphaFoldDB; Q63525; -.
DR SMR; Q63525; -.
DR BioGRID; 248270; 1.
DR STRING; 10116.ENSRNOP00000009933; -.
DR iPTMnet; Q63525; -.
DR PhosphoSitePlus; Q63525; -.
DR jPOST; Q63525; -.
DR PaxDb; Q63525; -.
DR PRIDE; Q63525; -.
DR Ensembl; ENSRNOT00000079380; ENSRNOP00000073414; ENSRNOG00000051720.
DR GeneID; 29648; -.
DR KEGG; rno:29648; -.
DR UCSC; RGD:3215; rat.
DR CTD; 10726; -.
DR RGD; 3215; Nudc.
DR eggNOG; KOG2265; Eukaryota.
DR GeneTree; ENSGT00940000155361; -.
DR HOGENOM; CLU_047332_1_0_1; -.
DR InParanoid; Q63525; -.
DR OMA; KPEDSIW; -.
DR OrthoDB; 1474731at2759; -.
DR PhylomeDB; Q63525; -.
DR TreeFam; TF300147; -.
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 Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR PRO; PR:Q63525; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000051720; Expressed in ovary and 19 other tissues.
DR Genevisible; Q63525; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
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; IMP:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
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 Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..332
FT /note="Nuclear migration protein nudC"
FT /id="PRO_0000057992"
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 121..172
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..129
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"
SQ SEQUENCE 332 AA; 38412 MW; C3751531DC43662D CRC64;
MGGEQEEERF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFIGGEEGM AEKLITQTFN
HHNQLAQKAR REKRARQETE RREKAERAAR LAKEAKAETP GPQIKELTDE EAERLQLEID
QKKDAENHEV QLKNGSLDSP GKQDAEEEED EEDEKDKGKL KPNLGNGADL PNYRWTQTLS
ELDLAVPFRV SFRLKGKDVV VDIQRRHLRV GLKGQAPVID GELYNEVKVE ESSWLIEDGK
VVTVHLEKIN KMEWWNRLVT SDPEINTKKI NPENSKLSDL DSETRSMVEK MMYDQRQKSM
GLPTSDEQKK QEILKKFMDQ HPEMDFSKAK FN
