KLP68_DROME
ID KLP68_DROME Reviewed; 784 AA.
AC P46867; Q961H5; Q9VTN8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Kinesin-like protein Klp68D;
GN Name=Klp68D; Synonyms=KLP5; ORFNames=CG7293;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7525600; DOI=10.1083/jcb.127.4.1041;
RA Pesavento P.A., Stewart R.J., Goldstein L.S.B.;
RT "Characterization of the KLP68D kinesin-like protein in Drosophila:
RT possible roles in axonal transport.";
RL J. Cell Biol. 127:1041-1048(1994).
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=Head;
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 [GENOMIC DNA] OF 220-342.
RC STRAIN=DP CN BW;
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).
CC -!- FUNCTION: Plus-end directed microtubule motor that may be used for
CC anterograde axonal transport and could conceivably move cargos in fly
CC neurons different than those moved by kinesin heavy chain or other
CC plus-end directed motors. {ECO:0000269|PubMed:7525600}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in the central nervous system
CC and in a subset of the peripheral nervous system during embryogenesis.
CC {ECO:0000269|PubMed:7525600}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin II subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; U15974; AAA69929.1; -; mRNA.
DR EMBL; AE014296; AAF50008.1; -; Genomic_DNA.
DR EMBL; AY051583; AAK93007.1; -; mRNA.
DR EMBL; M74431; AAA28658.1; -; Genomic_DNA.
DR PIR; A55236; A55236.
DR RefSeq; NP_001261726.1; NM_001274797.1.
DR RefSeq; NP_524029.2; NM_079305.3.
DR AlphaFoldDB; P46867; -.
DR SMR; P46867; -.
DR BioGRID; 64693; 8.
DR IntAct; P46867; 1.
DR STRING; 7227.FBpp0075762; -.
DR PaxDb; P46867; -.
DR DNASU; 39332; -.
DR EnsemblMetazoa; FBtr0076030; FBpp0075762; FBgn0004381.
DR EnsemblMetazoa; FBtr0332129; FBpp0304439; FBgn0004381.
DR GeneID; 39332; -.
DR KEGG; dme:Dmel_CG7293; -.
DR CTD; 39332; -.
DR FlyBase; FBgn0004381; Klp68D.
DR VEuPathDB; VectorBase:FBgn0004381; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000153739; -.
DR HOGENOM; CLU_001485_22_4_1; -.
DR InParanoid; P46867; -.
DR OMA; CKHDHNQ; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; P46867; -.
DR Reactome; R-DME-5620924; Intraflagellar transport.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR BioGRID-ORCS; 39332; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39332; -.
DR PRO; PR:P46867; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004381; Expressed in second segment of antenna (Drosophila) and 30 other tissues.
DR ExpressionAtlas; P46867; baseline and differential.
DR Genevisible; P46867; DM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
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:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:FlyBase.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IMP:UniProtKB.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR Gene3D; 3.40.850.10; -; 1.
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 PANTHER; PTHR24115; PTHR24115; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..784
FT /note="Kinesin-like protein Klp68D"
FT /id="PRO_0000125392"
FT DOMAIN 19..344
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 371..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 351..385
FT /evidence="ECO:0000255"
FT COILED 426..582
FT /evidence="ECO:0000255"
FT COMPBIAS 417..431
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 220..221
FT /note="SS -> TC (in Ref. 5; AAA28658)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..342
FT /note="ASRAK -> VRGQV (in Ref. 5; AAA28658)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="A -> G (in Ref. 1; AAA69929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 88207 MW; 7A3C6716D22BC05D CRC64;
MSAKSRRPGT GSSQTPNECV QVVVRCRPMS NRERSERSPE VVNVYPNRGV VELQNVVDGN
KEQRKVFTYD AAYDASATQT TLYHEVVFPL VSSVLEGFNG CIFAYGQTGT GKTFTMEGVR
GNDELMGIIP RTFEQIWLHI NRTENFQFLV DVSYLEIYME ELRDLLKPNS KHLEVRERGS
GVYVPNLHAI NCKSVEDMIK VMQVGNKNRT VGFTNMNEHS SRSHAIFMIK IEMCDTETNT
IKVGKLNLID LAGSERQSKT GASAERLKEA SKINLALSSL GNVISALAES SPHVPYRDSK
LTRLLQDSLG GNSKTIMIAN IGPSNYNYNE TLTTLRYASR AKSIQNQPIK NEDPQDAKLK
EYQEEIERLK RLIGPQQQQR SEKQVTAKKQ RVKKPKKETV TKEMSDSLQV STIEQPVEDD
SDPEGAESES DKENEAEVAK SNEELERERV ENSKLAAKLA ELEGQLVRGG KNLLDTYSER
QIELEKKLVE IAERKKREIE IQQQLELQEE TTLEIRERNV SLEQEVELKK RKLSKCYAKY
LALQQELNDC KSDHNQDLRE LEMAQNELVK ELKRQLLIID NFVPIEVKQR LYTQAKYDEE
QEEWKFSSMS LPTPPGGDGK FSSKRPVSHP QRRRPTSEYA LQEAKSNSPS SLRFKSENIV
NYELEMPCRT TQEYRTPKVS ASLQAVLAQA MQTGGDDIDI VDSHTNSLRS RLENIINANA
NGGAGPGAGV AVGSSIPNVR NIKSSRGLPS AASNLDSNRR PPTGRLPAKK PASAYPKARG
LVNK
