NUDC_BOVIN
ID NUDC_BOVIN Reviewed; 332 AA.
AC Q17QG2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Nuclear migration protein nudC;
DE AltName: Full=Nuclear distribution protein C homolog;
GN Name=NUDC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 PLK1, PAFAH1B1 and DCDC1. Part of a complex
CC containing PLK1, NUDC, dynein and dynactin (By similarity). Interacts
CC with EML4 (via WD repeats) (By similarity).
CC {ECO:0000250|UniProtKB:O35685, ECO:0000250|UniProtKB:Q9Y266}.
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 -!- 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; BC118381; AAI18382.1; -; mRNA.
DR RefSeq; NP_001069075.1; NM_001075607.2.
DR AlphaFoldDB; Q17QG2; -.
DR SMR; Q17QG2; -.
DR STRING; 9913.ENSBTAP00000005789; -.
DR PaxDb; Q17QG2; -.
DR PeptideAtlas; Q17QG2; -.
DR PRIDE; Q17QG2; -.
DR Ensembl; ENSBTAT00000005789; ENSBTAP00000005789; ENSBTAG00000004416.
DR GeneID; 513277; -.
DR KEGG; bta:513277; -.
DR CTD; 10726; -.
DR VEuPathDB; HostDB:ENSBTAG00000004416; -.
DR VGNC; VGNC:32321; NUDC.
DR eggNOG; KOG2265; Eukaryota.
DR GeneTree; ENSGT00940000155361; -.
DR HOGENOM; CLU_047332_1_0_1; -.
DR InParanoid; Q17QG2; -.
DR OMA; KPEDSIW; -.
DR OrthoDB; 1474731at2759; -.
DR TreeFam; TF300147; -.
DR Reactome; R-BTA-9696270; RND2 GTPase cycle.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000004416; Expressed in temporal cortex and 103 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0006457; P:protein folding; IBA:GO_Central.
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 2: Evidence at transcript 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_0000327734"
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 126..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 260
FT /note="Phosphoserine"
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; by PLK1"
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; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y266"
SQ SEQUENCE 332 AA; 38243 MW; 05F646A960A7AE6C CRC64;
MGGEQEEDRF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFVGGEEGM AEKLITQTFN
HHNQLAQKAR REKRARQETE RREKAERAAR LAKEAKSETS GPQIKELTDE EAERLQLEID
QKKDAENQEA QLKNGSLGSP GKQEAEEEEE EDDEKDKGKL KPNLGNGADL PSYRWTQTLS
ELDLAVPFCV NFRLKGKDVV VDIQRRHLRV GLKGQPAIVD GELYNEVKVE ESSWLIEDGK
VVTVHLEKIN KMEWWSRLVS SDPEINTKKI NPENSKLSDL DSETRSMVEK MMYDQRQKSM
GLPTSDEQKK QEILKKFMDQ HPEMDFSKAR FN
