KI10A_DROME
ID KI10A_DROME Reviewed; 805 AA.
AC Q960Z0;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Kinesin-like protein Klp10A;
DE AltName: Full=Kinesin-like protein at cytological position 10A;
GN Name=Klp10A {ECO:0000312|FlyBase:FBgn0030268};
GN ORFNames=CG1453 {ECO:0000312|FlyBase:FBgn0030268};
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 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 [4]
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-630; SER-795;
RP SER-797 AND SER-800, AND 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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20946984; DOI=10.1016/j.cell.2010.09.022;
RA Goodwin S.S., Vale R.D.;
RT "Patronin regulates the microtubule network by protecting microtubule minus
RT ends.";
RL Cell 143:263-274(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24100293; DOI=10.1083/jcb.201306001;
RA Wang H., Brust-Mascher I., Civelekoglu-Scholey G., Scholey J.M.;
RT "Patronin mediates a switch from kinesin-13-dependent poleward flux to
RT anaphase B spindle elongation.";
RL J. Cell Biol. 203:35-46(2013).
RN [9]
RP FUNCTION.
RX PubMed=26659188; DOI=10.1038/nature16443;
RA Derivery E., Seum C., Daeden A., Loubery S., Holtzer L., Juelicher F.,
RA Gonzalez-Gaitan M.;
RT "Polarized endosome dynamics by spindle asymmetry during asymmetric cell
RT division.";
RL Nature 528:280-285(2015).
RN [10]
RP INTERACTION WITH ALMS1A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=32965218; DOI=10.7554/elife.59368;
RA Chen C., Yamashita Y.M.;
RT "Alstrom syndrome gene is a stem-cell-specific regulator of centriole
RT duplication in the Drosophila testis.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Required during anaphase to drive sister chromatid separation
CC to promote flux by actively depolymerizing kinetochore microtubules at
CC their pole-associated minus ends, thereby moving chromatids through a
CC 'poleward flux' (PubMed:14681690, PubMed:20946984, PubMed:24100293).
CC Involved in asymmetric cell division of sensory organ precursor (SOP)
CC cells by playing a role in the asymmetric localization of Sara-
CC expressing endosomes to the pIIa daughter cell but not to the pIIb
CC cell. Klp98A targets Sara-expressing endosomes to the central spindle
CC which is symmetrically arranged in early cell division. During late
CC cytokinesis, central spindle asymmetry is generated by enrichment of
CC Patronin on the pIIb side which protects microtubules from
CC depolymerization by Klp10A while unprotected microtubules on the pIIa
CC side are disassembled by Klp10A, leading to the asymmetric delivery of
CC Sara-expressing endosomes to the pIIa daughter cell (PubMed:26659188).
CC {ECO:0000269|PubMed:14681690, ECO:0000269|PubMed:20946984,
CC ECO:0000269|PubMed:24100293, ECO:0000269|PubMed:26659188}.
CC -!- SUBUNIT: Interacts with Alms1a (via C-terminus).
CC {ECO:0000269|PubMed:32965218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14681690,
CC ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:32965218}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:14681690,
CC ECO:0000269|PubMed:24100293}. Chromosome, centromere
CC {ECO:0000269|PubMed:24100293}. Note=Localizes to mitotic centrosomes,
CC spindle poles and centromeres through metaphase (PubMed:14681690).
CC However, the centromeric localization diminishes markedly at the onset
CC of anaphase, leaving the majority of the protein on the spindle poles
CC (PubMed:14681690). Concentrated around the minus ends focused at the
CC poles (PubMed:14681690, PubMed:24100293). {ECO:0000269|PubMed:14681690,
CC ECO:0000269|PubMed:24100293}.
CC -!- TISSUE SPECIFICITY: Expressed in male germline stem cells and
CC spermatogonia (at protein level). {ECO:0000269|PubMed:32965218}.
CC -!- DISRUPTION PHENOTYPE: Marked perturbation of mitotic spindle
CC architecture (PubMed:14681690). RNAi-knockdown in the male germline
CC abolishes the asymmetric enrichment of Alms1a to the mother centrosome
CC (PubMed:32965218). {ECO:0000269|PubMed:14681690,
CC ECO:0000269|PubMed:32965218}.
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; AE014298; AAN09282.1; -; Genomic_DNA.
DR EMBL; AY051763; AAK93187.1; -; mRNA.
DR RefSeq; NP_001285109.1; NM_001298180.1.
DR RefSeq; NP_572687.1; NM_132459.4.
DR RefSeq; NP_727491.1; NM_167267.2.
DR RefSeq; NP_727492.1; NM_167268.2.
DR RefSeq; NP_727493.1; NM_167269.2.
DR RefSeq; NP_727494.1; NM_167270.2.
DR PDB; 3J2U; EM; 10.80 A; K=279-615.
DR PDB; 6B0C; EM; 3.51 A; K=279-615.
DR PDB; 6B0I; EM; 3.78 A; K=198-615.
DR PDB; 6B0L; EM; 3.98 A; K=198-615.
DR PDBsum; 3J2U; -.
DR PDBsum; 6B0C; -.
DR PDBsum; 6B0I; -.
DR PDBsum; 6B0L; -.
DR AlphaFoldDB; Q960Z0; -.
DR SMR; Q960Z0; -.
DR BioGRID; 58463; 10.
DR IntAct; Q960Z0; 2.
DR MINT; Q960Z0; -.
DR STRING; 7227.FBpp0073333; -.
DR iPTMnet; Q960Z0; -.
DR PaxDb; Q960Z0; -.
DR PRIDE; Q960Z0; -.
DR DNASU; 32049; -.
DR EnsemblMetazoa; FBtr0073475; FBpp0073331; FBgn0030268.
DR EnsemblMetazoa; FBtr0073476; FBpp0073332; FBgn0030268.
DR EnsemblMetazoa; FBtr0073477; FBpp0073333; FBgn0030268.
DR EnsemblMetazoa; FBtr0073478; FBpp0073334; FBgn0030268.
DR EnsemblMetazoa; FBtr0073479; FBpp0073335; FBgn0030268.
DR EnsemblMetazoa; FBtr0346270; FBpp0312027; FBgn0030268.
DR GeneID; 32049; -.
DR KEGG; dme:Dmel_CG1453; -.
DR UCSC; CG1453-RA; d. melanogaster.
DR CTD; 32049; -.
DR FlyBase; FBgn0030268; Klp10A.
DR VEuPathDB; VectorBase:FBgn0030268; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000154046; -.
DR HOGENOM; CLU_001485_19_1_1; -.
DR InParanoid; Q960Z0; -.
DR OMA; WQFLTMI; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q960Z0; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR BioGRID-ORCS; 32049; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32049; -.
DR PRO; PR:Q960Z0; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030268; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; Q960Z0; baseline and differential.
DR Genevisible; Q960Z0; DM.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0055028; C:cortical microtubule; IDA:FlyBase.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:UniProtKB.
DR GO; GO:0072687; C:meiotic spindle; IDA:FlyBase.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:FlyBase.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; 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: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:0008574; F:plus-end-directed microtubule motor activity; IDA:FlyBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0098534; P:centriole assembly; IMP:FlyBase.
DR GO; GO:0051298; P:centrosome duplication; IMP:FlyBase.
DR GO; GO:0051296; P:establishment of meiotic spindle orientation; IMP:FlyBase.
DR GO; GO:0061867; P:establishment of mitotic spindle asymmetry; IMP:FlyBase.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:FlyBase.
DR GO; GO:0070462; P:plus-end specific microtubule depolymerization; IMP:FlyBase.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IMP: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; Centromere;
KW Chromosome; Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..805
FT /note="Kinesin-like protein Klp10A"
FT /id="PRO_0000125424"
FT DOMAIN 278..610
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..274
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 68..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 205..244
FT /evidence="ECO:0000255"
FT COMPBIAS 80..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 368..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 630
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 805 AA; 88672 MW; 1667DE7C5478138D CRC64;
MDMITVGQSV KIKRTDGRVH MAVVAVINQS GKCITVEWYE RGETKGKEVE LDAILTLNPE
LMQDTVEQHA APEPKKQATA PMNLSRNPTQ SAIGGNLTSR MTMAGNMLNK IQESQSIPNP
IVSSNSVNTN SNSNTTAGGG GGTTTSTTTG LQRPRYSQAA TGQQQTRIAS AVPNNTLPNP
SAAASAGPAA QGVATAATTQ GAGGASTRRS HALKEVERLK ENREKRRARQ AEMKEEKVAL
MNQDPGNPNW ETAQMIREYQ STLEFVPLLD GQAVDDHQIT VCVRKRPISR KEVNRKEIDV
ISVPRKDMLI VHEPRSKVDL TKFLENHKFR FDYAFNDTCD NAMVYKYTAK PLVKTIFEGG
MATCFAYGQT GSGKTHTMGG EFNGKVQDCK NGIYAMAAKD VFVTLNMPRY RAMNLVVSAS
FFEIYSGKVF DLLSDKQKLR VLEDGKQQVQ VVGLTEKVVD GVEEVLKLIQ HGNAARTSGQ
TSANSNSSRS HAVFQIVLRP QGSTKIHGKF SFIDLAGNER GVDTSSADRQ TRMEGAEINK
SLLALKECIR ALGKQSAHLP FRVSKLTQVL RDSFIGEKSK TCMIAMISPG LSSCEHTLNT
LRYADRVKEL VVKDIVEVCP GGDTEPIEIT DDEEEEELNM VHPHSHQLHP NSHAPASQSN
NQRAPASHHS GAVIHNNNNN NNKNGNAGNM DLAMLSSLSE HEMSDELIVQ HQAIDDLQQT
EEMVVEYHRT VNATLETFLA ESKALYNLTN YVDYDQDSYC KRGESMFSQL LDIAIQCRDM
MAEYRAKLAK EEMLSCSFNS PNGKR
