KINH_DROME
ID KINH_DROME Reviewed; 975 AA.
AC P17210; Q9V7L9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Kinesin heavy chain;
GN Name=Khc; Synonyms=kin; ORFNames=CG7765;
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 DOMAIN.
RX PubMed=2522352; DOI=10.1016/0092-8674(89)90692-2;
RA Yang J.T., Laymon R.A., Goldstein L.S.B.;
RT "A three-domain structure of kinesin heavy chain revealed by DNA sequence
RT and microtubule binding analyses.";
RL Cell 56:879-889(1989).
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=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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=1384131; DOI=10.1126/science.1384131;
RA Gho M., McDonald K., Ganetzky B., Saxton W.M.;
RT "Effects of kinesin mutations on neuronal functions.";
RL Science 258:313-316(1992).
RN [6]
RP FUNCTION.
RX PubMed=16717129; DOI=10.1083/jcb.200601067;
RA Glater E.E., Megeath L.J., Stowers R.S., Schwarz T.L.;
RT "Axonal transport of mitochondria requires milton to recruit kinesin heavy
RT chain and is light chain independent.";
RL J. Cell Biol. 173:545-557(2006).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that may play a role in organelle transport. Milt and Miro form an
CC essential protein complex that links Khc to mitochondria for light
CC chain-independent, anterograde transport of mitochondria.
CC {ECO:0000269|PubMed:16717129, ECO:0000269|PubMed:2522352}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC -!- INTERACTION:
CC P17210; P46824: Klc; NbExp=4; IntAct=EBI-102445, EBI-77490;
CC P17210; Q99689: FEZ1; Xeno; NbExp=3; IntAct=EBI-102445, EBI-396435;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- DOMAIN: Composed of three structural domains: a large globular N-
CC terminal domain which is responsible for the motor activity of kinesin
CC (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC coiled coil domain that mediates the heavy chain dimerization; and a
CC small globular C-terminal domain which interacts with other proteins
CC (such as the kinesin light chains), vesicles and membranous organelles.
CC {ECO:0000269|PubMed:2522352}.
CC -!- DISRUPTION PHENOTYPE: Flies display impaired action potential
CC propagation and neurotransmitter release at neuromuscular junctions,
CC but are still capable of transporting certain membranes, including
CC synaptic vesicles, to the nerve terminal. {ECO:0000269|PubMed:1384131}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; M24441; AAA28652.1; -; mRNA.
DR EMBL; AE013599; AAF58029.1; -; Genomic_DNA.
DR EMBL; AY094959; AAM11312.1; -; mRNA.
DR PIR; A31497; A31497.
DR RefSeq; NP_476590.1; NM_057242.5.
DR PDB; 2Y5W; X-ray; 2.70 A; A/B=1-365.
DR PDB; 2Y65; X-ray; 2.20 A; A/B/C/D=1-365, W/X/Y=937-952.
DR PDB; 5JVR; X-ray; 2.10 A; A/B/C/D/E/F/G/H=345-358.
DR PDB; 5JVS; X-ray; 2.25 A; A=334-367.
DR PDB; 5JVU; X-ray; 1.95 A; A/B=334-367.
DR PDB; 7BJS; X-ray; 2.28 A; A/B=855-941.
DR PDBsum; 2Y5W; -.
DR PDBsum; 2Y65; -.
DR PDBsum; 5JVR; -.
DR PDBsum; 5JVS; -.
DR PDBsum; 5JVU; -.
DR PDBsum; 7BJS; -.
DR AlphaFoldDB; P17210; -.
DR SMR; P17210; -.
DR BioGRID; 62529; 56.
DR DIP; DIP-20367N; -.
DR IntAct; P17210; 7.
DR MINT; P17210; -.
DR STRING; 7227.FBpp0086328; -.
DR PaxDb; P17210; -.
DR PRIDE; P17210; -.
DR DNASU; 36810; -.
DR EnsemblMetazoa; FBtr0087184; FBpp0086328; FBgn0001308.
DR GeneID; 36810; -.
DR KEGG; dme:Dmel_CG7765; -.
DR CTD; 36810; -.
DR FlyBase; FBgn0001308; Khc.
DR VEuPathDB; VectorBase:FBgn0001308; -.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_001485_11_1_1; -.
DR InParanoid; P17210; -.
DR OMA; AAKQHEM; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; P17210; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR SignaLink; P17210; -.
DR BioGRID-ORCS; 36810; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36810; -.
DR PRO; PR:P17210; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001308; Expressed in oviduct (Drosophila) and 27 other tissues.
DR ExpressionAtlas; P17210; baseline and differential.
DR Genevisible; P17210; DM.
DR GO; GO:0030478; C:actin cap; IDA:FlyBase.
DR GO; GO:1904115; C:axon cytoplasm; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; 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; NAS:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0003777; F:microtubule motor activity; IDA:FlyBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0005523; F:tropomyosin binding; IPI:FlyBase.
DR GO; GO:0061572; P:actin filament bundle organization; IMP:FlyBase.
DR GO; GO:0098957; P:anterograde axonal transport of mitochondrion; IMP:FlyBase.
DR GO; GO:0098937; P:anterograde dendritic transport; IMP:FlyBase.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0051299; P:centrosome separation; IMP:FlyBase.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; TAS:FlyBase.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0001754; P:eye photoreceptor cell differentiation; IGI:FlyBase.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0046785; P:microtubule polymerization; IMP:FlyBase.
DR GO; GO:0051012; P:microtubule sliding; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IDA:FlyBase.
DR GO; GO:0048311; P:mitochondrion distribution; IMP:FlyBase.
DR GO; GO:0007097; P:nuclear migration; IMP:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:0007315; P:pole plasm assembly; IMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0035617; P:stress granule disassembly; IMP:BHF-UCL.
DR GO; GO:0048489; P:synaptic vesicle transport; IGI:FlyBase.
DR GO; GO:0010970; P:transport along microtubule; IDA: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; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..975
FT /note="Kinesin heavy chain"
FT /id="PRO_0000125350"
FT DOMAIN 12..333
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 180..321
FT /note="Microtubule-binding"
FT REGION 810..891
FT /note="Necessary for associating with milt"
FT REGION 932..975
FT /note="Globular"
FT COILED 335..931
FT BINDING 92..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 515
FT /note="A -> T (in Ref. 1; AAA28652)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2Y65"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 133..145
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:2Y65"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 211..223
FT /evidence="ECO:0007829|PDB:2Y65"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 300..310
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 317..330
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2Y65"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:2Y65"
FT HELIX 345..367
FT /evidence="ECO:0007829|PDB:5JVU"
FT HELIX 856..921
FT /evidence="ECO:0007829|PDB:7BJS"
SQ SEQUENCE 975 AA; 110399 MW; 24840EF414790888 CRC64;
MSAEREIPAE DSIKVVCRFR PLNDSEEKAG SKFVVKFPNN VEENCISIAG KVYLFDKVFK
PNASQEKVYN EAAKSIVTDV LAGYNGTIFA YGQTSSGKTH TMEGVIGDSV KQGIIPRIVN
DIFNHIYAME VNLEFHIKVS YYEIYMDKIR DLLDVSKVNL SVHEDKNRVP YVKGATERFV
SSPEDVFEVI EEGKSNRHIA VTNMNEHSSR SHSVFLINVK QENLENQKKL SGKLYLVDLA
GSEKVSKTGA EGTVLDEAKN INKSLSALGN VISALADGNK THIPYRDSKL TRILQESLGG
NARTTIVICC SPASFNESET KSTLDFGRRA KTVKNVVCVN EELTAEEWKR RYEKEKEKNA
RLKGKVEKLE IELARWRAGE TVKAEEQINM EDLMEASTPN LEVEAAQTAA AEAALAAQRT
ALANMSASVA VNEQARLATE CERLYQQLDD KDEEINQQSQ YAEQLKEQVM EQEELIANAR
REYETLQSEM ARIQQENESA KEEVKEVLQA LEELAVNYDQ KSQEIDNKNK DIDALNEELQ
QKQSVFNAAS TELQQLKDMS SHQKKRITEM LTNLLRDLGE VGQAIAPGES SIDLKMSALA
GTDASKVEED FTMARLFISK MKTEAKNIAQ RCSNMETQQA DSNKKISEYE KDLGEYRLLI
SQHEARMKSL QESMREAENK KRTLEEQIDS LREECAKLKA AEHVSAVNAE EKQRAEELRS
MFDSQMDELR EAHTRQVSEL RDEIAAKQHE MDEMKDVHQK LLLAHQQMTA DYEKVRQEDA
EKSSELQNII LTNERREQAR KDLKGLEDTV AKELQTLHNL RKLFVQDLQQ RIRKNVVNEE
SEEDGGSLAQ KQKISFLENN LDQLTKVHKQ LVRDNADLRC ELPKLEKRLR CTMERVKALE
TALKEAKEGA MRDRKRYQYE VDRIKEAVRQ KHLGRRGPQA QIAKPIRSGQ GAIAIRGGGA
VGGPSPLAQV NPVNS
