ID   NUDC_CHICK              Reviewed;         341 AA.
AC   Q5ZIN1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Nuclear migration protein nudC;
DE   AltName: Full=Nuclear distribution protein C homolog;
GN   Name=NUDC; ORFNames=RCJMB04_24m10;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Plays a role in neurogenesis and neuronal migration.
CC       Necessary for correct formation of mitotic spindles and chromosome
CC       separation during mitosis. Necessary for cytokinesis and cell
CC       proliferation (By similarity). {ECO:0000250|UniProtKB:O35685,
CC       ECO:0000250|UniProtKB:Q9Y266}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Y266}. Midbody
CC       {ECO:0000250|UniProtKB:Q9Y266}. Note=In a filamentous pattern adjacent
CC       to the nucleus of migrating cerebellar granule cells. Colocalizes with
CC       tubulin and dynein and with the microtubule organizing center.
CC       Distributed throughout the cytoplasm of non-migrating cells (By
CC       similarity). Localizes to the mitotic spindle in a EML4-dependent
CC       manner (By similarity). {ECO:0000250|UniProtKB:Q9Y266}.
CC   -!- PTM: Reversibly phosphorylated on serine residues during the M phase of
CC       the cell cycle. Phosphorylation is necessary for correct formation of
CC       mitotic spindles and chromosome separation during mitosis (By
CC       similarity). {ECO:0000250|UniProtKB:Q9Y266}.
CC   -!- SIMILARITY: Belongs to the nudC family. {ECO:0000305}.
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DR   EMBL; AJ720753; CAG32412.1; -; mRNA.
DR   RefSeq; NP_001006311.1; NM_001006311.1.
DR   AlphaFoldDB; Q5ZIN1; -.
DR   SMR; Q5ZIN1; -.
DR   STRING; 9031.ENSGALP00000001315; -.
DR   PaxDb; Q5ZIN1; -.
DR   GeneID; 419578; -.
DR   KEGG; gga:419578; -.
DR   CTD; 10726; -.
DR   VEuPathDB; HostDB:geneid_419578; -.
DR   eggNOG; KOG2265; Eukaryota.
DR   InParanoid; Q5ZIN1; -.
DR   OrthoDB; 1474731at2759; -.
DR   PhylomeDB; Q5ZIN1; -.
DR   PRO; PR:Q5ZIN1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..341
FT                   /note="Nuclear migration protein nudC"
FT                   /id="PRO_0000057988"
FT   DOMAIN          177..268
FT                   /note="CS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT   REGION          66..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          65..137
FT                   /evidence="ECO:0000255"
FT   MOTIF           73..81
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        66..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y266"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y266"
SQ   SEQUENCE   341 AA;  39210 MW;  F9D187C303119FBE CRC64;
     MGLSAEEAAE QEDRFDGILL AMAQQHQGGV CELVNTFFSF LRRKTDFFTG GEDGVAEKLI
     TDSFNHHNKL AQKERKEKKA RQEAERREKA ERAAKLAKEA KQEANEPRIK ELTDEEAERL
     QLEIDQKKEA QKEVNNVPVK SSEDDGDSSD SNKQETDDEE KDENDKGKLK PNAGNGADLP
     NYRWTQTLSE LDLAIPFKVT FRLKGKDVVV DIQRRRLRVG LKGHPPVIDG ELFNEVKVEE
     SSWLIEDGKT VTVHLEKINK MEWWNKLVST DPEINTKKIN PENSKLSDLD SETRSMVEKM
     MYDQRQKSMG LPTSDEQKKQ DILKKFMEQH PEMDFSKAKF N