NDC_DROME
ID NDC_DROME Reviewed; 332 AA.
AC Q9VVA6; Q8SYK7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nuclear migration protein nudC {ECO:0000303|PubMed:9376324};
DE AltName: Full=Nuclear distribution protein C homolog {ECO:0000305};
GN Name=nudC {ECO:0000303|PubMed:9376324, ECO:0000312|FlyBase:FBgn0021768};
GN ORFNames=CG9710 {ECO:0000312|FlyBase:FBgn0021768};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAP93640.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9376324; DOI=10.1016/s0925-4773(97)00085-3;
RA Cunniff J., Chiu Y.H., Morris N.R., Warrior R.;
RT "Characterization of DnudC, the Drosophila homolog of an Aspergillus gene
RT that functions in nuclear motility.";
RL Mech. Dev. 66:55-68(1997).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAL49107.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL49107.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL49107.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26490864; DOI=10.1523/jneurosci.1610-15.2015;
RA Wang X., Zhang M.W., Kim J.H., Macara A.M., Sterne G., Yang T., Ye B.;
RT "The Krueppel-Like factor Dar1 determines multipolar neuron morphology.";
RL J. Neurosci. 35:14251-14259(2015).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PCID2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=33602059; DOI=10.1080/15476286.2021.1885198;
RA Glukhova A.A., Kurshakova M.M., Nabirochkina E.N., Georgieva S.G.,
RA Kopytova D.V.;
RT "PCID2, a subunit of the Drosophila TREX-2 nuclear export complex, is
RT essential for both mRNA nuclear export and its subsequent cytoplasmic
RT trafficking.";
RL RNA Biol. 18:1969-1980(2021).
CC -!- FUNCTION: Chaperone protein with functions in nuclear localization and
CC cytoplasmic mRNA trafficking (PubMed:9376324, PubMed:26490864,
CC PubMed:33602059). In postmitotic neurons, acts with nudE downstream of
CC dar1 to ensure correct positioning of the nuclei in primary dendrites
CC and as a consequence, is required for determining multipolar neuron
CC morphology (PubMed:26490864). Stabilizes PCID2 in the cytoplasm and
CC thereby is required for promoting cytoplasmic mRNA trafficking
CC (PubMed:33602059). {ECO:0000269|PubMed:26490864,
CC ECO:0000269|PubMed:33602059, ECO:0000269|PubMed:9376324}.
CC -!- SUBUNIT: Interacts with PCID2. {ECO:0000269|PubMed:33602059}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33602059}.
CC -!- DEVELOPMENTAL STAGE: Embryos (at protein level) (PubMed:33602059).
CC Detected in embryos and adults (PubMed:9376324).
CC {ECO:0000269|PubMed:33602059, ECO:0000269|PubMed:9376324}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in multipolar
CC Class I dendritic arborizing neurons forming a bipolar morphology
CC (PubMed:26490864). Dendritic arborization is unaffected
CC (PubMed:26490864). {ECO:0000269|PubMed:26490864}.
CC -!- SIMILARITY: Belongs to the nudC family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49407.2; -; Genomic_DNA.
DR EMBL; AY071485; AAL49107.1; -; mRNA.
DR EMBL; AY328470; AAP93640.1; -; mRNA.
DR EMBL; AE014296; AFH04476.1; -; Genomic_DNA.
DR RefSeq; NP_001246805.1; NM_001259876.1.
DR RefSeq; NP_648923.1; NM_140666.4.
DR SMR; Q9VVA6; -.
DR IntAct; Q9VVA6; 6.
DR STRING; 7227.FBpp0297079; -.
DR PRIDE; Q9VVA6; -.
DR DNASU; 39879; -.
DR EnsemblMetazoa; FBtr0075328; FBpp0075087; FBgn0021768.
DR EnsemblMetazoa; FBtr0305912; FBpp0297079; FBgn0021768.
DR GeneID; 39879; -.
DR KEGG; dme:Dmel_CG9710; -.
DR UCSC; CG9710-RA; d. melanogaster.
DR CTD; 10726; -.
DR FlyBase; FBgn0021768; nudC.
DR VEuPathDB; VectorBase:FBgn0021768; -.
DR eggNOG; KOG2265; Eukaryota.
DR GeneTree; ENSGT00940000155361; -.
DR HOGENOM; CLU_047332_1_0_1; -.
DR OMA; SYRWTQT; -.
DR OrthoDB; 1474731at2759; -.
DR Reactome; R-DME-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 39879; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39879; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0021768; Expressed in embryonic/larval hemocyte (Drosophila) and 52 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; ISS:FlyBase.
DR GO; GO:0051647; P:nucleus localization; IMP:FlyBase.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IGI:FlyBase.
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; IPR037898; NudC_fam.
DR InterPro; IPR025934; NudC_N_dom.
DR PANTHER; PTHR12356; PTHR12356; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF14050; Nudc_N; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; mRNA transport; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..332
FT /note="Nuclear migration protein nudC"
FT /id="PRO_0000455830"
FT DOMAIN 168..259
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
SQ SEQUENCE 332 AA; 37792 MW; 4A96349154388A1A CRC64;
MAAEEGKFDN ILLAVAEKHH GGVPEFLGTL ASFLRRKTDF FTGAKQTEWE KLLLDVFNKE
SKLAVTENYE KIKAREASQR LKAEKERAER KARKQEIDDN KICDITDEEA AAIIKEEETK
KRQQLLDSAG GEPSASNRDG ISKPIEKVDD ESDKSELGKL MPNAGNGCTL ENYTWTQTLE
EVELKIPFNL TFGLRARDLV ISIGKKSLKV GIKGQTPIID GELCGEVKTE ESVWVLQDSK
TVMITLDKIN KMNWWSRLVT TDPEISTRKI NPESSKLSDL DGETRSMVEK MMYDQRQKEL
GLPTSEDRKK QDILEKFKQQ HPEMDFSKCK FN
