NCD_DROME
ID NCD_DROME Reviewed; 700 AA.
AC P20480; Q9VAG8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Protein claret segregational;
GN Name=ncd; Synonyms=CA(ND); ORFNames=CG7831;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Ovary;
RX PubMed=1691829; DOI=10.1038/345081a0;
RA Endow S.A., Henikoff S., Soler-Niedziela L.;
RT "Mediation of meiotic and early mitotic chromosome segregation in
RT Drosophila by a protein related to kinesin.";
RL Nature 345:81-83(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-700.
RX PubMed=2140958; DOI=10.1016/0092-8674(90)90064-l;
RA McDonald H.B., Goldstein L.S.B.;
RT "Identification and characterization of a gene encoding a kinesin-like
RT protein in Drosophila.";
RL Cell 61:991-1000(1990).
RN [6]
RP FUNCTION.
RX PubMed=2146510; DOI=10.1038/347780a0;
RA Walker R.A., Salmon E.D., Endow S.A.;
RT "The Drosophila claret segregation protein is a minus-end directed motor
RT molecule.";
RL Nature 347:780-782(1990).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8112290; DOI=10.1002/j.1460-2075.1994.tb06317.x;
RA Lockhart A., Cross R.A.;
RT "Origins of reversed directionality in the ncd molecular motor.";
RL EMBO J. 13:751-757(1994).
RN [8]
RP MUTAGENESIS OF VAL-556.
RX PubMed=1825056; DOI=10.1002/j.1460-2075.1991.tb07963.x;
RA Komma D.J., Horne A.S., Endow S.A.;
RT "Separation of meiotic and mitotic effects of claret non-disjunctional on
RT chromosome segregation in Drosophila.";
RL EMBO J. 10:419-424(1991).
RN [9]
RP MUTAGENESIS OF VAL-556.
RX PubMed=8670831; DOI=10.1002/j.1460-2075.1996.tb00695.x;
RA Moore J.D., Song H., Endow S.A.;
RT "A point mutation in the microtubule binding region of the Ncd motor
RT protein reduces motor velocity.";
RL EMBO J. 15:3306-3314(1996).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-96, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 335-700.
RX PubMed=8606780; DOI=10.1038/380555a0;
RA Sablin E.P., Kull F.J., Cooke R., Vale R.D., Fletterick R.J.;
RT "Crystal structure of the motor domain of the kinesin-related motor ncd.";
RL Nature 380:555-559(1996).
CC -!- FUNCTION: NCD is required for normal chromosomal segregation in
CC meiosis, in females, and in early mitotic divisions of the embryo. The
CC NCD motor activity is directed toward the microtubule's minus end.
CC {ECO:0000269|PubMed:2146510}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; X52814; CAA36998.1; -; Genomic_DNA.
DR EMBL; M33932; AAA28716.1; -; mRNA.
DR EMBL; AE014297; AAF56942.1; -; Genomic_DNA.
DR EMBL; AY058596; AAL13825.1; -; mRNA.
DR EMBL; X57475; CAA40713.1; -; Genomic_DNA.
DR PIR; S09748; S09748.
DR RefSeq; NP_001287592.1; NM_001300663.1.
DR RefSeq; NP_476651.1; NM_057303.5.
DR PDB; 1CZ7; X-ray; 2.90 A; A/B/C/D=295-700.
DR PDB; 1N6M; X-ray; 2.50 A; A/B=293-700.
DR PDB; 2NCD; X-ray; 2.50 A; A=281-700.
DR PDB; 3L1C; X-ray; 2.75 A; A/B=293-674.
DR PDB; 3U06; X-ray; 2.35 A; A/B=293-700.
DR PDB; 5HLE; X-ray; 2.90 A; A=325-348, A=664-700.
DR PDB; 5HNW; EM; 6.60 A; K=325-348, K=664-700.
DR PDB; 5HNX; EM; 6.60 A; K=325-348, K=664-700.
DR PDB; 5HNY; EM; 6.30 A; K=325-348, K=447-493, K=695-700.
DR PDB; 5HNZ; EM; 5.80 A; K=325-348, K=430-700.
DR PDB; 5W3D; X-ray; 2.79 A; A/B=293-700.
DR PDBsum; 1CZ7; -.
DR PDBsum; 1N6M; -.
DR PDBsum; 2NCD; -.
DR PDBsum; 3L1C; -.
DR PDBsum; 3U06; -.
DR PDBsum; 5HLE; -.
DR PDBsum; 5HNW; -.
DR PDBsum; 5HNX; -.
DR PDBsum; 5HNY; -.
DR PDBsum; 5HNZ; -.
DR PDBsum; 5W3D; -.
DR AlphaFoldDB; P20480; -.
DR SMR; P20480; -.
DR BioGRID; 68381; 30.
DR DIP; DIP-21302N; -.
DR IntAct; P20480; 6.
DR MINT; P20480; -.
DR STRING; 7227.FBpp0084900; -.
DR iPTMnet; P20480; -.
DR PaxDb; P20480; -.
DR PRIDE; P20480; -.
DR DNASU; 43517; -.
DR EnsemblMetazoa; FBtr0085534; FBpp0084900; FBgn0002924.
DR EnsemblMetazoa; FBtr0344976; FBpp0311231; FBgn0002924.
DR GeneID; 43517; -.
DR KEGG; dme:Dmel_CG7831; -.
DR CTD; 43517; -.
DR FlyBase; FBgn0002924; ncd.
DR VEuPathDB; VectorBase:FBgn0002924; -.
DR eggNOG; KOG0239; Eukaryota.
DR GeneTree; ENSGT00940000156463; -.
DR HOGENOM; CLU_001485_12_4_1; -.
DR InParanoid; P20480; -.
DR OMA; TWTYHDE; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; P20480; -.
DR SignaLink; P20480; -.
DR BioGRID-ORCS; 43517; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P20480; -.
DR GenomeRNAi; 43517; -.
DR PRO; PR:P20480; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002924; Expressed in cleaving embryo and 34 other tissues.
DR ExpressionAtlas; P20480; baseline and differential.
DR Genevisible; P20480; DM.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0072687; C:meiotic spindle; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; NAS:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR GO; GO:0032837; P:distributive segregation; IMP:FlyBase.
DR GO; GO:0090306; P:meiotic spindle assembly; IMP:FlyBase.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0031534; P:minus-end directed microtubule sliding; IDA:FlyBase.
DR GO; GO:0007100; P:mitotic centrosome separation; IMP:FlyBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:FlyBase.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IMP:FlyBase.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IGI:FlyBase.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP:FlyBase.
DR GO; GO:0007056; P:spindle assembly involved in female meiosis; NAS:FlyBase.
DR GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Meiosis; Microtubule; Mitosis; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..700
FT /note="Protein claret segregational"
FT /id="PRO_0000125378"
FT DOMAIN 348..670
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 141..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 196..346
FT /evidence="ECO:0000255"
FT BINDING 434..441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 556
FT /note="V->F: In ncd(D); reduces motor velocity and shows
FT abnormal chromosomal segregation."
FT /evidence="ECO:0000269|PubMed:1825056,
FT ECO:0000269|PubMed:8670831"
FT CONFLICT 697
FT /note="S -> N (in Ref. 1; CAA36998)"
FT /evidence="ECO:0000305"
FT HELIX 293..345
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:3L1C"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:2NCD"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:3U06"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 416..423
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 428..435
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 440..444
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:1CZ7"
FT HELIX 453..468
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 473..485
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:2NCD"
FT HELIX 525..538
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:2NCD"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 554..565
FT /evidence="ECO:0007829|PDB:3U06"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 570..580
FT /evidence="ECO:0007829|PDB:3U06"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 601..614
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 626..631
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:3U06"
FT STRAND 635..638
FT /evidence="ECO:0007829|PDB:1N6M"
FT STRAND 640..647
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:3U06"
FT HELIX 654..670
FT /evidence="ECO:0007829|PDB:3U06"
SQ SEQUENCE 700 AA; 77474 MW; ADE043CBCE7FD561 CRC64;
MESRLPKPSG LKKPQMPIKT VLPTDRIRAG LGGGAAGAGA FNVNANQTYC GNLLPPLSRD
LNNLPQVLER RGGGARAASP EPMKLGHRAK LRRSRSACDI NELRGNKRTA AAPSLPSIPS
KVSRLGGALT VSSQRLVRPA APSSITATAV KRPPVTRPAP RAAGGAAAKK PAGTGAAASS
GAAAAAPKRI APYDFKARFH DLLEKHKVLK TKYEKQTEDM GELESMPQQL EETQNKLIET
ESSLKNTQSD NECLQRQVKQ HTAKIETITS TLGRTKEELS ELQAIHEKVK TEHAALSTEV
VHLRQRTEEL LRCNEQQAAE LETCKEQLFQ SNMERKELHN TVMDLRGNIR VFCRIRPPLE
SEENRMCCTW TYHDESTVEL QSIDAQAKSK MGQQIFSFDQ VFHPLSSQSD IFEMVSPLIQ
SALDGYNICI FAYGQTGSGK TYTMDGVPES VGVIPRTVDL LFDSIRGYRN LGWEYEIKAT
FLEIYNEVLY DLLSNEQKDM EIRMAKNNKN DIYVSNITEE TVLDPNHLRH LMHTAKMNRA
TASTAGNERS SRSHAVTKLE LIGRHAEKQE ISVGSINLVD LAGSESPKTS TRMTETKNIN
RSLSELTNVI LALLQKQDHI PYRNSKLTHL LMPSLGGNSK TLMFINVSPF QDCFQESVKS
LRFAASVNSC KMTKAKRNRY LNNSVANSST QSNNSGSFDK
