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Protein

Protein claret segregational

Gene

ncd

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NCD is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The NCD motor activity is directed toward the microtubule's minus end.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi434 – 4418ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent microtubule motor activity, minus-end-directed Source: FlyBase
  • microtubule motor activity Source: GO_Central
  • protein homodimerization activity Source: FlyBase

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • centrosome duplication Source: FlyBase
  • centrosome organization Source: FlyBase
  • chromosome segregation Source: FlyBase
  • distributive segregation Source: FlyBase
  • meiotic spindle organization Source: FlyBase
  • microtubule-based movement Source: FlyBase
  • microtubule bundle formation Source: FlyBase
  • minus-end directed microtubule sliding Source: FlyBase
  • mitotic centrosome separation Source: FlyBase
  • mitotic spindle assembly Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • mRNA transport Source: FlyBase
  • regulation of mitotic spindle assembly Source: FlyBase
  • regulation of mitotic spindle elongation Source: FlyBase
  • spindle assembly involved in female meiosis Source: FlyBase
  • spindle assembly involved in meiosis Source: FlyBase
  • spindle organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein claret segregational
Gene namesi
Name:ncd
Synonyms:CA(ND)
ORF Names:CG7831
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0002924. ncd.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: FlyBase
  • cytosol Source: Reactome
  • kinesin complex Source: GO_Central
  • meiotic spindle Source: FlyBase
  • minus-end kinesin complex Source: FlyBase
  • mitotic spindle microtubule Source: FlyBase
  • nucleus Source: FlyBase
  • spindle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi556 – 5561V → F in ncd(D); reduces motor velocity and shows abnormal chromosomal segregation. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 700700Protein claret segregationalPRO_0000125378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941Phosphoserine1 Publication
Modified residuei96 – 961Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20480.
PRIDEiP20480.

PTM databases

iPTMnetiP20480.

Expressioni

Gene expression databases

BgeeiP20480.
ExpressionAtlasiP20480. differential.
GenevisibleiP20480. DM.

Interactioni

GO - Molecular functioni

  • protein homodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi68381. 17 interactions.
DIPiDIP-21302N.
IntActiP20480. 6 interactions.
MINTiMINT-949768.
STRINGi7227.FBpp0084900.

Structurei

Secondary structure

1
700
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi293 – 34553Combined sources
Beta strandi348 – 3558Combined sources
Helixi360 – 3623Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi369 – 3746Combined sources
Beta strandi377 – 3815Combined sources
Helixi385 – 3884Combined sources
Helixi389 – 3913Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi399 – 4024Combined sources
Helixi408 – 4125Combined sources
Turni413 – 4153Combined sources
Helixi416 – 4238Combined sources
Beta strandi428 – 4358Combined sources
Helixi440 – 4445Combined sources
Beta strandi448 – 4514Combined sources
Helixi453 – 46816Combined sources
Helixi469 – 4713Combined sources
Beta strandi473 – 48513Combined sources
Beta strandi488 – 4914Combined sources
Beta strandi502 – 5043Combined sources
Beta strandi511 – 5144Combined sources
Beta strandi520 – 5223Combined sources
Helixi525 – 53814Combined sources
Beta strandi543 – 5453Combined sources
Helixi547 – 5504Combined sources
Beta strandi554 – 56512Combined sources
Turni566 – 5694Combined sources
Beta strandi570 – 58011Combined sources
Turni598 – 6003Combined sources
Helixi601 – 61414Combined sources
Helixi622 – 6243Combined sources
Helixi626 – 6316Combined sources
Helixi632 – 6343Combined sources
Beta strandi635 – 6384Combined sources
Beta strandi640 – 6478Combined sources
Helixi651 – 6533Combined sources
Helixi654 – 67017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZ7X-ray2.90A/B/C/D295-700[»]
1N6MX-ray2.50A/B293-700[»]
1OZXmodel-A345-667[»]
1SYJmodel-A345-667[»]
1SYPmodel-A345-667[»]
1SZ4model-A345-667[»]
1SZ5model-A345-667[»]
2NCDX-ray2.50A281-700[»]
3L1CX-ray2.75A/B293-674[»]
3U06X-ray2.35A/B293-700[»]
ProteinModelPortaliP20480.
SMRiP20480. Positions 233-670.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20480.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini348 – 670323Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili196 – 346151Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. NCD subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0239. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00550000074610.
InParanoidiP20480.
KOiK10405.
OMAiGWEYEIR.
OrthoDBiEOG72G16X.
PhylomeDBiP20480.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 3 hits.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESRLPKPSG LKKPQMPIKT VLPTDRIRAG LGGGAAGAGA FNVNANQTYC
60 70 80 90 100
GNLLPPLSRD LNNLPQVLER RGGGARAASP EPMKLGHRAK LRRSRSACDI
110 120 130 140 150
NELRGNKRTA AAPSLPSIPS KVSRLGGALT VSSQRLVRPA APSSITATAV
160 170 180 190 200
KRPPVTRPAP RAAGGAAAKK PAGTGAAASS GAAAAAPKRI APYDFKARFH
210 220 230 240 250
DLLEKHKVLK TKYEKQTEDM GELESMPQQL EETQNKLIET ESSLKNTQSD
260 270 280 290 300
NECLQRQVKQ HTAKIETITS TLGRTKEELS ELQAIHEKVK TEHAALSTEV
310 320 330 340 350
VHLRQRTEEL LRCNEQQAAE LETCKEQLFQ SNMERKELHN TVMDLRGNIR
360 370 380 390 400
VFCRIRPPLE SEENRMCCTW TYHDESTVEL QSIDAQAKSK MGQQIFSFDQ
410 420 430 440 450
VFHPLSSQSD IFEMVSPLIQ SALDGYNICI FAYGQTGSGK TYTMDGVPES
460 470 480 490 500
VGVIPRTVDL LFDSIRGYRN LGWEYEIKAT FLEIYNEVLY DLLSNEQKDM
510 520 530 540 550
EIRMAKNNKN DIYVSNITEE TVLDPNHLRH LMHTAKMNRA TASTAGNERS
560 570 580 590 600
SRSHAVTKLE LIGRHAEKQE ISVGSINLVD LAGSESPKTS TRMTETKNIN
610 620 630 640 650
RSLSELTNVI LALLQKQDHI PYRNSKLTHL LMPSLGGNSK TLMFINVSPF
660 670 680 690 700
QDCFQESVKS LRFAASVNSC KMTKAKRNRY LNNSVANSST QSNNSGSFDK
Length:700
Mass (Da):77,474
Last modified:February 1, 1991 - v1
Checksum:iADE043CBCE7FD561
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti697 – 6971S → N in CAA36998 (PubMed:1691829).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52814 Genomic DNA. Translation: CAA36998.1.
M33932 mRNA. Translation: AAA28716.1.
AE014297 Genomic DNA. Translation: AAF56942.1.
AY058596 mRNA. Translation: AAL13825.1.
X57475 Genomic DNA. Translation: CAA40713.1.
PIRiS09748.
RefSeqiNP_001287592.1. NM_001300663.1.
NP_476651.1. NM_057303.5.
UniGeneiDm.6668.

Genome annotation databases

EnsemblMetazoaiFBtr0085534; FBpp0084900; FBgn0002924.
FBtr0344976; FBpp0311231; FBgn0002924.
GeneIDi43517.
KEGGidme:Dmel_CG7831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52814 Genomic DNA. Translation: CAA36998.1.
M33932 mRNA. Translation: AAA28716.1.
AE014297 Genomic DNA. Translation: AAF56942.1.
AY058596 mRNA. Translation: AAL13825.1.
X57475 Genomic DNA. Translation: CAA40713.1.
PIRiS09748.
RefSeqiNP_001287592.1. NM_001300663.1.
NP_476651.1. NM_057303.5.
UniGeneiDm.6668.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZ7X-ray2.90A/B/C/D295-700[»]
1N6MX-ray2.50A/B293-700[»]
1OZXmodel-A345-667[»]
1SYJmodel-A345-667[»]
1SYPmodel-A345-667[»]
1SZ4model-A345-667[»]
1SZ5model-A345-667[»]
2NCDX-ray2.50A281-700[»]
3L1CX-ray2.75A/B293-674[»]
3U06X-ray2.35A/B293-700[»]
ProteinModelPortaliP20480.
SMRiP20480. Positions 233-670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68381. 17 interactions.
DIPiDIP-21302N.
IntActiP20480. 6 interactions.
MINTiMINT-949768.
STRINGi7227.FBpp0084900.

PTM databases

iPTMnetiP20480.

Proteomic databases

PaxDbiP20480.
PRIDEiP20480.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085534; FBpp0084900; FBgn0002924.
FBtr0344976; FBpp0311231; FBgn0002924.
GeneIDi43517.
KEGGidme:Dmel_CG7831.

Organism-specific databases

CTDi43517.
FlyBaseiFBgn0002924. ncd.

Phylogenomic databases

eggNOGiKOG0239. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00550000074610.
InParanoidiP20480.
KOiK10405.
OMAiGWEYEIR.
OrthoDBiEOG72G16X.
PhylomeDBiP20480.

Enzyme and pathway databases

ReactomeiR-DME-983189. Kinesins.

Miscellaneous databases

EvolutionaryTraceiP20480.
GenomeRNAii43517.
PROiP20480.

Gene expression databases

BgeeiP20480.
ExpressionAtlasiP20480. differential.
GenevisibleiP20480. DM.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 3 hits.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mediation of meiotic and early mitotic chromosome segregation in Drosophila by a protein related to kinesin."
    Endow S.A., Henikoff S., Soler-Niedziela L.
    Nature 345:81-83(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S and Oregon-R.
    Tissue: Ovary.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Identification and characterization of a gene encoding a kinesin-like protein in Drosophila."
    McDonald H.B., Goldstein L.S.B.
    Cell 61:991-1000(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-700.
  6. "The Drosophila claret segregation protein is a minus-end directed motor molecule."
    Walker R.A., Salmon E.D., Endow S.A.
    Nature 347:780-782(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Origins of reversed directionality in the ncd molecular motor."
    Lockhart A., Cross R.A.
    EMBO J. 13:751-757(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Separation of meiotic and mitotic effects of claret non-disjunctional on chromosome segregation in Drosophila."
    Komma D.J., Horne A.S., Endow S.A.
    EMBO J. 10:419-424(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-556.
  9. "A point mutation in the microtubule binding region of the Ncd motor protein reduces motor velocity."
    Moore J.D., Song H., Endow S.A.
    EMBO J. 15:3306-3314(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-556.
  10. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  11. "Crystal structure of the motor domain of the kinesin-related motor ncd."
    Sablin E.P., Kull F.J., Cooke R., Vale R.D., Fletterick R.J.
    Nature 380:555-559(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 335-700.

Entry informationi

Entry nameiNCD_DROME
AccessioniPrimary (citable) accession number: P20480
Secondary accession number(s): Q9VAG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.