ID A4UZI0_DROME Unreviewed; 1899 AA.
AC A4UZI0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Kinesin heavy chain 73, isoform C {ECO:0000313|EMBL:AAF58129.2};
DE EC=3.6.1.3 {ECO:0000313|EMBL:AAF58129.2};
GN Name=Khc-73 {ECO:0000313|EMBL:AAF58129.2,
GN ECO:0000313|FlyBase:FBgn0019968};
GN Synonyms=anon-EST:fe3C9 {ECO:0000313|EMBL:AAF58129.2}, Dmel\CG8183
GN {ECO:0000313|EMBL:AAF58129.2}, DmKIN73 {ECO:0000313|EMBL:AAF58129.2},
GN DmKin73 {ECO:0000313|EMBL:AAF58129.2}, DmKlp73
GN {ECO:0000313|EMBL:AAF58129.2}, KHC-73 {ECO:0000313|EMBL:AAF58129.2},
GN khc-73 {ECO:0000313|EMBL:AAF58129.2}, Khc73
GN {ECO:0000313|EMBL:AAF58129.2}, KIF 13A {ECO:0000313|EMBL:AAF58129.2},
GN KIF13A/B {ECO:0000313|EMBL:AAF58129.2}, Kin73
GN {ECO:0000313|EMBL:AAF58129.2}, Kinesin-73
GN {ECO:0000313|EMBL:AAF58129.2}, KLP73 {ECO:0000313|EMBL:AAF58129.2};
GN ORFNames=CG8183 {ECO:0000313|EMBL:AAF58129.2,
GN ECO:0000313|FlyBase:FBgn0019968}, Dmel_CG8183
GN {ECO:0000313|EMBL:AAF58129.2};
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:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|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 [4] {ECO:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AAF58129.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; AE013599; AAF58129.2; -; Genomic_DNA.
DR RefSeq; NP_788356.2; NM_176176.3.
DR SMR; A4UZI0; -.
DR EnsemblMetazoa; FBtr0329955; FBpp0302987; FBgn0019968.
DR GeneID; 36718; -.
DR AGR; FB:FBgn0019968; -.
DR CTD; 36718; -.
DR FlyBase; FBgn0019968; Khc-73.
DR VEuPathDB; VectorBase:FBgn0019968; -.
DR GeneTree; ENSGT00940000168995; -.
DR OMA; GQENHNL; -.
DR OrthoDB; 126886at2759; -.
DR BioGRID-ORCS; 36718; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36718; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0019968; Expressed in brain and 26 other cell types or tissues.
DR ExpressionAtlas; A4UZI0; baseline and differential.
DR GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
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-UniRule.
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; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0051294; P:establishment of spindle orientation; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd22706; FHA_KIF13; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF5; -; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12473; DUF3694; 2.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000313|EMBL:AAF58129.2};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A4UZI0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803}.
FT DOMAIN 5..352
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1804..1846
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 830..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1865..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 589..621
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 838..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1899
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:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1899 AA; 212396 MW; B003144346E5047A CRC64;
MASDKIKVAV RVRPFNRREI ELDTKCIVEM EKQQTILQNP PPLEKIERKQ PKTFAFDHCF
YSLNPEDENF ASQETVFDCV GRGILDNAFQ GYNACIFAYG QTGSGKSYTM MGTQESKGII
PRLCDQLFSA IANKSTPELM YKVEVSYMEI YNEKVHDLLD PKPNKQSLKV REHNVMGPYV
DGLSQLAVTS YQDIDNLMTE GNKSRTVAAT NMNAESSRSH AVFSVVLTQI LTDQATGVSG
EKVSRMSLVD LAGSERAVKT GAVGDRLKEG SNINKSLTTL GLVISKLADQ SNGKKSGNDK
FVPYRDSVLT WLLKDNLGGN SRTVMVATIS PSADNYEETL STLRYADRAK RIVNHAVVNE
DPNARIIREL RHEVETLRSM LKHATGSPVG DVQDKLAESE NLMKQISQTW EEKLVKTERI
QNERQQALEK MGISVQASGI KVEKNKYYLV NLNADPSLNE LLVYYLKDRT LIGGRTISGQ
QPDIQLSGLG IQPEHCVITI EDSGLYMEPV QGARCFVNGS AAVEKTPLQN GDRILWGNHH
FFRVNSPKSN NTSMCASEPQ TPAQLIDYNF ARDEIMQNEL SNDPIQTAIA RLERQHEEDK
QVALEKQRQE YERQFQQLRN ILSPSTPYAP YAPYDPLRMG KITPNTPTSQ MRVEKWAQER
DEMFRRSLGQ LKTDIMRANS LVQEANFLAE EMEKKTKFSV TLQIPPANLS PNRRRGAFVS
EPAILVKRTN SGSQIWTMEK LENKLIDMRE MYQEHKERVL NGLDEDNAKP QDPFYESQEN
HNLIGVANIF LEVLFHDVKL DYHTPIISQQ GEVAGRLQVE IERIAGQMPQ DRMCESVSES
SGDSRDEYDD PVDPTSNQIT CRVTIKCASG LPLSLSNFVF CQYTFWGHQE MVVPVINAES
TAHDQNMVFK FEHTQDFTVT INEEFLEHCI EGALSIEVWG HRSAGFSKTK GWEVEQQQAK
ARSLVDRWAE LSRKIELWVE IHELNDNGEY SPVEVTNRNE VLTGGIYQLR QGQQRRVNVR
VKPVQNSGTL PIICQSIVNV AIGSVTVRSR LQRPLDSYQE EDLTVLREKW SEALGRRRQY
LDQQIQMLIK KEEKNEQERE RELSLVHQWV SLTEERNAVL VPAPGSGIPG APASWEPPSG
MEPHVPVLFL NLNGDDLSAQ NTNDELSVAG INSILSKEHG HKFYTLQILQ HLDKDVCCVA
SWDSSMHDSQ ALNRVTEANE RVYLILRTTV RLSHPAPMDL VLRKRLSINI KKGQTLTDRL
KKFRLVRGEN AIWQSGVTYE VVSNIPKASE ELEDRESLAQ LAASGDDCSA SDGETYIEKY
TRGVSAVESI LTLDRLRQNV AVKELETAHG QPLSMRKTVS VPNFSQIMRF DASMESLLNV
GRSESFADLN NSALGNKFTP AGHSPAGAGG VIRSRHSFGG KGSSDDSPGK AFGIASPATS
KLLGMRMTTL HEEPLGGHRS LDEEPEDSYS DSEYAAEYEQ ERQQNKSMAT RSRLTASKTM
DSFMDVSSHS NQSYLSYTSS ANANMKHLTG LATLSMSSST SSGYGSQAVS CNNLSNEDIA
SMRSMSIDET PDFDRVNSNS PPNRQARVNP FLKDMPKAKI QEQPEQQAKK LQEAFTHPLE
QLESSQNAQS DDDECAQLPK NNNNNLDLVN EPKPLSSQTD LEESMSQPKS KTEFATDNQN
GNRSSDELSH SSEDLLEGDG IVREELPAGK VVRRKKSNTQ PPSNGNSINN NNNGTTQAPR
INHRASVAKM EGLAAYLDSS IMTSSTEVDE ESKDVELVLP EWIVVGESVL IRPYNTSGVI
RFVGTTEFQP GAWIGVELDT PTGKNDGSVK GVQYFQCKPK HGMFVRSDKL MLDKRGKAMR
AYKAAEKSNS ISKEMSTSMT GSMTRSKSRG DSLNLSARK
//
