KL98A_DROME
ID KL98A_DROME Reviewed; 1265 AA.
AC Q9VB25; A0A0B4K7N6; Q00088; Q8SZH6;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Kinesin-like protein Klp98A {ECO:0000305};
GN Name=Klp98A {ECO:0000312|FlyBase:FBgn0004387};
GN ORFNames=CG5658 {ECO:0000312|FlyBase:FBgn0004387};
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|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 [2] {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 [3] {ECO:0000312|EMBL:AAL48506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48506.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL48506.1};
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 [4] {ECO:0000312|EMBL:AEW43887.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AEW43887.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAA28659.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-184.
RC STRAIN=DP CN BW {ECO:0000312|EMBL:AAA28659.1};
RX PubMed=1924306; DOI=10.1073/pnas.88.19.8470;
RA Stewart R.J., Pesavento P.A., Woerpel D.N., Goldstein L.S.B.;
RT "Identification and partial characterization of six members of the kinesin
RT superfamily in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8470-8474(1991).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH ATG8A AND RAB14.
RX PubMed=26763909; DOI=10.1242/jcs.175224;
RA Mauvezin C., Neisch A.L., Ayala C.I., Kim J., Beltrame A., Braden C.R.,
RA Gardner M.K., Hays T.S., Neufeld T.P.;
RT "Coordination of autophagosome-lysosome fusion and transport by a Klp98A-
RT Rab14 complex.";
RL J. Cell Sci. 129:971-982(2016).
CC -!- FUNCTION: Plus end-directed motor protein involved in asymmetric cell
CC division of sensory organ precursor (SOP) cells by playing a role in
CC the asymmetric localization of Sara-expressing endosomes to the pIIa
CC daughter cell but not to the pIIb cell. Targets Sara-expressing
CC endosomes to the central spindle which is symmetrically arranged in
CC early cell division. During late cytokinesis, central spindle asymmetry
CC is generated by enrichment of Patronin on the pIIb side which protects
CC microtubules from depolymerization by Klp10A while unprotected
CC microtubules on the pIIa side are disassembled by Klp10A, leading to
CC the asymmetric delivery of Sara-expressing endosomes to the pIIa
CC daughter cell (PubMed:26659188). Also plays a role in regulation of
CC autophagosome formation, fusion and positioning and is required for
CC normal localization of Rab14 (PubMed:26763909).
CC {ECO:0000269|PubMed:26659188, ECO:0000269|PubMed:26763909}.
CC -!- SUBUNIT: Interacts with Atg8a and Rab14. {ECO:0000269|PubMed:26763909}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:26659188}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0004387};
CC IsoId=Q9VB25-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0004387};
CC IsoId=Q9VB25-2; Sequence=VSP_058298;
CC -!- DISRUPTION PHENOTYPE: Diffuse movement of Sara-expressing endosomes,
CC failed targeting of Sara-expressing endosomes to the central spindle
CC and symmetric endosome localization in daughter SOP cells.
CC {ECO:0000269|PubMed:26659188}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|RuleBase:RU000394}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48506.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF56718.2; -; Genomic_DNA.
DR EMBL; AE014297; AFH06656.1; -; Genomic_DNA.
DR EMBL; AY070884; AAL48506.1; ALT_FRAME; mRNA.
DR EMBL; BT132947; AEW43887.1; -; mRNA.
DR EMBL; M74432; AAA28659.1; -; Genomic_DNA.
DR PIR; F41298; F41298.
DR RefSeq; NP_001247339.1; NM_001260410.2. [Q9VB25-2]
DR RefSeq; NP_524532.2; NM_079808.4. [Q9VB25-1]
DR AlphaFoldDB; Q9VB25; -.
DR SMR; Q9VB25; -.
DR IntAct; Q9VB25; 5.
DR STRING; 7227.FBpp0084581; -.
DR PaxDb; Q9VB25; -.
DR PRIDE; Q9VB25; -.
DR DNASU; 43310; -.
DR EnsemblMetazoa; FBtr0085211; FBpp0084581; FBgn0004387. [Q9VB25-1]
DR EnsemblMetazoa; FBtr0304671; FBpp0293213; FBgn0004387. [Q9VB25-2]
DR GeneID; 43310; -.
DR KEGG; dme:Dmel_CG5658; -.
DR UCSC; CG5658-RA; d. melanogaster. [Q9VB25-1]
DR CTD; 43310; -.
DR FlyBase; FBgn0004387; Klp98A.
DR VEuPathDB; VectorBase:FBgn0004387; -.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000162977; -.
DR InParanoid; Q9VB25; -.
DR OMA; QVLNCRE; -.
DR PhylomeDB; Q9VB25; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR SignaLink; Q9VB25; -.
DR BioGRID-ORCS; 43310; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43310; -.
DR PRO; PR:Q9VB25; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004387; Expressed in mouthpart and 20 other tissues.
DR ExpressionAtlas; Q9VB25; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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:1901981; F:phosphatidylinositol phosphate binding; ISS:FlyBase.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:FlyBase.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0140024; P:plus-end-directed endosome transport along mitotic spindle midzone microtubule; IDA:FlyBase.
DR GO; GO:0045056; P:transcytosis; IMP:FlyBase.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027640; Kinesin-like_fam.
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 InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00787; PX; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Autophagy; Coiled coil; Endosome;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome;
KW Transport.
FT CHAIN 1..1265
FT /note="Kinesin-like protein Klp98A"
FT /id="PRO_0000436181"
FT DOMAIN 3..364
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 1129..1259
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 597..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 619..670
FT /evidence="ECO:0000255"
FT COILED 768..848
FT /evidence="ECO:0000255"
FT COILED 1035..1071
FT /evidence="ECO:0000255"
FT COMPBIAS 842..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT VAR_SEQ 700..740
FT /note="Missing (in isoform B)"
FT /id="VSP_058298"
FT CONFLICT 90
FT /note="E -> P (in Ref. 4; AAA28659)"
FT /evidence="ECO:0000305"
FT CONFLICT 172..173
FT /note="EH -> DD (in Ref. 4; AAA28659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1265 AA; 141562 MW; ABB9ED1CA784B1A3 CRC64;
MSSLKVAVRV RPFNSREIDM DAQLIMEMEN KKTRLLKPRL QSIRDAGRDN HHDFTFDYSY
WSFDAEDPHF ATQEQVYSDL GNDVVDCAYE GYNACVFAYG QTGSGKTFTM MGTPNNPGLI
PRICEELFAR MRVGQESGTG YRTHASYLEI YNERVKDLLA AQSTGHGLRV REHRSLGPYV
ENLSQHAVSD FDEIQECIAR GNAQRTTAST NMNDTSSRSH AIFTITFVQA VFMNDMPSET
VSKIHLVDLA GSERANATGA TGQRLKEGAH INKSLVTLGS VISALAEQTG GGHNSSSSAL
ATTPNGASKR VLYIPYRDSI LTWLLKDSLG GNSKTIMIAA LSPADCNYSE TLSTLRYANR
AKNIINKPTV NEDTNVKLIR ELREEINKLK SMLAGDIHSL QPSLKVLADL QKKEAQEKVL
TEEWTEKWKV AQSILQEQKS LGLRKSGVGV VLDSEMPHLI GIHNDVTTGV TLYSLKEGET
RIGSEDADVA QDIELAGDGI RAQHCSIFLK GGVVTLHPWP LAQCWVNAHL IDEPKQISQG
DIILLGRTNI FRFNNPAEAA KLRKDLSRSQ LDMSRLSLIT SSKENLLTCS IYSDEDGASP
YKRPERQYYP QRPMSRDDPE LQDENRKILD TIENALKQLN VERVQMHDQY KTKVRKLTEE
LIRLEQEEMD GLQLLNCREQ ELIARKDMLL WEKNNEKVQI DIVCRQISAF QTQLDSKKRD
FSEYVAKELQ ELQDCGKLDE MGMKIEEGTP LNDELLLQVS DSLDLFAAQF IKDTVRRNNE
EIRKLDEQIA EKERILNAST TKIAKVDETM LEIQAQLERL RLERAESEAE SQAMRAKKQN
MKLQLGNKSM STSTSTNEAD DVSKSDTYET CDTFHTAQSN LSLVSSPTIT EGQQSPLSNC
SCDAEDEAED TRKDDLSGSS EETSRTCTAG PSSGSGSGSV GIGGSGSAPS CTPSSQAIMS
DSGVCLDSRN QAILQNGHLN NYKQAVRTSD EDTGSCSSCE LGRHSDVARP YCPLHSLRRK
IAAQKALIMK NLETDLNKAQ LDEHIADLQD LQRRYIQMEQ EMLQSVQDLE AHAQCCADER
SGMERQYELA SSIMRSSVMS PTSMEESTSQ IYSPSMTRSC PSMREFPEGE HFITIPSFVM
RGAGKQTHYE YEVRIALPDG KLNILRRYSR FRELHLCMKH CYGAKISALP FPRRELFASN
SEPVAKHRRR LLELYLRRLF VVCSKIPQCP IYEGPGGTGL TRASLVQLSS FFKKGLFENG
KHGTG
