KI59C_DROME
ID KI59C_DROME Reviewed; 626 AA.
AC Q9W1U4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Kinesin-like protein Klp59C;
DE AltName: Full=Kinesin-like protein at cytological position 59C;
GN Name=Klp59C; ORFNames=CG3219;
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 [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 [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14681690; DOI=10.1038/nature02256;
RA Rogers G.C., Rogers S.L., Schwimmer T.A., Ems-McClung S.C., Walczak C.E.,
RA Vale R.D., Scholey J.M., Sharp D.J.;
RT "Two mitotic kinesins cooperate to drive sister chromatid separation during
RT anaphase.";
RL Nature 427:364-370(2004).
CC -!- FUNCTION: Required during anaphase to drive sister chromatid separation
CC to actively depolymerize kinetochore microtubules at their kinetochore-
CC associated plus ends, thereby contributing to chromatid mobility
CC through a 'Pac-man' mechanism. {ECO:0000269|PubMed:14681690}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:14681690}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:14681690}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:14681690}. Note=Primarily restricted to centromeric
CC regions of chromosomes during both metaphase and anaphase. Not
CC localized on spindle poles throughout mitosis. Concentrated on the plus
CC ends of kinetochore microtubules embedded in the kinetochore.
CC -!- DISRUPTION PHENOTYPE: Defects in chromosome segregation, but does not
CC affect the mitotic spindle. {ECO:0000269|PubMed:14681690}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AE013599; AAF46959.1; -; Genomic_DNA.
DR RefSeq; NP_611759.1; NM_137915.4.
DR AlphaFoldDB; Q9W1U4; -.
DR SMR; Q9W1U4; -.
DR BioGRID; 63275; 2.
DR IntAct; Q9W1U4; 4.
DR STRING; 7227.FBpp0071885; -.
DR PaxDb; Q9W1U4; -.
DR PRIDE; Q9W1U4; -.
DR DNASU; 37671; -.
DR EnsemblMetazoa; FBtr0071975; FBpp0071885; FBgn0034824.
DR GeneID; 37671; -.
DR KEGG; dme:Dmel_CG3219; -.
DR UCSC; CG3219-RA; d. melanogaster.
DR CTD; 37671; -.
DR FlyBase; FBgn0034824; Klp59C.
DR VEuPathDB; VectorBase:FBgn0034824; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000154046; -.
DR HOGENOM; CLU_001485_19_1_1; -.
DR InParanoid; Q9W1U4; -.
DR OMA; EMSLQRD; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q9W1U4; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR BioGRID-ORCS; 37671; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37671; -.
DR PRO; PR:Q9W1U4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034824; Expressed in testis and 10 other tissues.
DR ExpressionAtlas; Q9W1U4; baseline and differential.
DR Genevisible; Q9W1U4; DM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003774; F:cytoskeletal motor activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..626
FT /note="Kinesin-like protein Klp59C"
FT /id="PRO_0000125425"
FT DOMAIN 187..521
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..183
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 68..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..150
FT /evidence="ECO:0000255"
FT COMPBIAS 70..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 626 AA; 70053 MW; 3715F0777881E27B CRC64;
MDKLSIEQKI FIRRSDGRVH LAEIIKLEGG DSKLITVEWP EGHTVRGKEL PLELVVLMNP
HIFDSPRCSG GNAASANQTA SISPRSMKQR IATGSLSPVL ATAPPRQQTA PPVREDEVVH
QAERMRKERE RRREAQARTR LDREQGKNED PGNPNWEVAR MIRLQREQME SQRVRSGTTN
ERINCHQIMV CVRKRPLRRK ELADREQDVV SIPSKHTLVV HEPRKHVNLV KFLENHSFRF
DYVFDEECSN ATVYEFTARP LIKHIFDGGM ATCFAYGQTG SGKTYTMGGQ FPGRHQSSMD
GIYAMAAKDV FSTLKTVPYN KLNLKVYCSF FEIYGTRVFD LLMPGKPQLR VLEDRNQQVQ
VVGLTQNPVQ NTAEVLDLLE LGNSVRTSGH TSANSKSSRS HAVFQIVLRS AAGEKLHGKF
SLIDLAGNER GADNSSADRQ TRLEGSEINK SLLVLKECIR ALGRQSSHLP FRGSKLTQVL
RDSFIGGKKV KTCMIAMISP CLHSVEHTLN TLRYADRVKE LSVESIPSKR MPDANLGSTS
MSDIVCQSST QRLFPCASST SMPGGGNQAQ QHTNTANDLN RSQKPTSKPT YPTSGQQLVQ
RKGSSQREAS MMLTKSLAQF RGRNFP
