KIF1A_DROME
ID KIF1A_DROME Reviewed; 1670 AA.
AC A1ZAJ2; A8DX00; A8DYG5; Q9NBL1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Kinesin-like protein unc-104;
DE AltName: Full=Protein immaculate connections;
DE Short=DUnc104;
GN Name=unc-104; Synonyms=imac {ECO:0000303|PubMed:17643120}; ORFNames=CG8566;
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] {ECO:0000312|EMBL:AAF74192.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RA Grossberger R., Saxton W.M., Dickson B.J.;
RT "Characterization of the Drosophila Unc104/KIF1A homolog, DUnc104.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17643120; DOI=10.1038/nn1936;
RA Pack-Chung E., Kurshan P.T., Dickman D.K., Schwarz T.L.;
RT "A Drosophila kinesin required for synaptic bouton formation and synaptic
RT vesicle transport.";
RL Nat. Neurosci. 10:980-989(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1406; SER-1416 AND THR-1419,
RP 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 [6]
RP FUNCTION, INTERACTION WITH ARL8, AND SUBCELLULAR LOCATION.
RX PubMed=30174114; DOI=10.1016/j.neuron.2018.08.004;
RA Vukoja A., Rey U., Petzoldt A.G., Ott C., Vollweiter D., Quentin C.,
RA Puchkov D., Reynolds E., Lehmann M., Hohensee S., Rosa S., Lipowsky R.,
RA Sigrist S.J., Haucke V.;
RT "Presynaptic Biogenesis Requires Axonal Transport of Lysosome-Related
RT Vesicles.";
RL Neuron 99:1216-1232(2018).
CC -!- FUNCTION: Required for presynaptic maturation, has a role in axonal
CC transport of dense-core vesicles carrying synaptic vesicle precursors,
CC components required for the morphological transformation of axonal
CC growth cones to mature boutons. {ECO:0000269|PubMed:17643120,
CC ECO:0000269|PubMed:30174114}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with Arl8
CC (PubMed:30174114). {ECO:0000250|UniProtKB:Q60575,
CC ECO:0000269|PubMed:30174114}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17643120}. Cell projection, axon
CC {ECO:0000269|PubMed:30174114}. Note=Microtubule-associated.
CC {ECO:0000269|PubMed:17643120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B; Synonyms=C;
CC IsoId=A1ZAJ2-1; Sequence=Displayed;
CC Name=D;
CC IsoId=A1ZAJ2-2; Sequence=VSP_030269;
CC Name=E;
CC IsoId=A1ZAJ2-3; Sequence=VSP_030268;
CC -!- TISSUE SPECIFICITY: Expressed in muscles.
CC {ECO:0000269|PubMed:17643120}.
CC -!- DISRUPTION PHENOTYPE: Flies prevent nerve endings from transforming to
CC synaptic boutons: growth cones become constricted but remain within
CC contact fields as thin processes that lack varicosities or boutons.
CC Mutant embryos die at late stage, they are paralyzed and lacked the
CC coordinated muscle peristalsis required for hatching.
CC {ECO:0000269|PubMed:17643120}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AF247761; AAF74192.1; -; mRNA.
DR EMBL; AE013599; AAF57957.3; -; Genomic_DNA.
DR EMBL; AE013599; AAM70884.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM70886.2; -; Genomic_DNA.
DR EMBL; AE013599; ABV53825.1; -; Genomic_DNA.
DR RefSeq; NP_001097346.1; NM_001103876.3. [A1ZAJ2-3]
DR RefSeq; NP_611155.3; NM_137311.5. [A1ZAJ2-2]
DR RefSeq; NP_725607.2; NM_166190.4. [A1ZAJ2-1]
DR RefSeq; NP_725610.2; NM_166192.4. [A1ZAJ2-1]
DR AlphaFoldDB; A1ZAJ2; -.
DR SMR; A1ZAJ2; -.
DR BioGRID; 62585; 7.
DR IntAct; A1ZAJ2; 5.
DR STRING; 7227.FBpp0086227; -.
DR iPTMnet; A1ZAJ2; -.
DR PRIDE; A1ZAJ2; -.
DR EnsemblMetazoa; FBtr0087079; FBpp0086227; FBgn0267002. [A1ZAJ2-2]
DR EnsemblMetazoa; FBtr0113087; FBpp0112000; FBgn0267002. [A1ZAJ2-1]
DR EnsemblMetazoa; FBtr0113088; FBpp0112001; FBgn0267002. [A1ZAJ2-1]
DR EnsemblMetazoa; FBtr0113089; FBpp0112002; FBgn0267002. [A1ZAJ2-3]
DR GeneID; 36876; -.
DR KEGG; dme:Dmel_CG8566; -.
DR UCSC; CG8566-RB; d. melanogaster. [A1ZAJ2-1]
DR CTD; 36876; -.
DR FlyBase; FBgn0267002; unc-104.
DR VEuPathDB; VectorBase:FBgn0267002; -.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000168546; -.
DR InParanoid; A1ZAJ2; -.
DR PhylomeDB; A1ZAJ2; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR SignaLink; A1ZAJ2; -.
DR BioGRID-ORCS; 36876; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36876; -.
DR PRO; PR:A1ZAJ2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0267002; Expressed in head capsule and 21 other tissues.
DR ExpressionAtlas; A1ZAJ2; baseline and differential.
DR Genevisible; A1ZAJ2; DM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043679; C:axon terminus; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
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; IMP: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:0030742; F:GTP-dependent protein binding; IPI: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; IBA:GO_Central.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:FlyBase.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:FlyBase.
DR GO; GO:0098930; P:axonal transport; IMP:FlyBase.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0046847; P:filopodium assembly; IMP:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:FlyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0040012; P:regulation of locomotion; IMP:FlyBase.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:FlyBase.
DR GO; GO:0016188; P:synaptic vesicle maturation; IMP:FlyBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:FlyBase.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 3.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 2.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1670
FT /note="Kinesin-like protein unc-104"
FT /id="PRO_0000299496"
FT DOMAIN 3..351
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 499..565
FT /note="FHA"
FT /evidence="ECO:0000255"
FT DOMAIN 1537..1635
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 951..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..436
FT /evidence="ECO:0000255"
FT COILED 576..674
FT /evidence="ECO:0000255"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 1406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 390
FT /note="E -> GPDGKVVCEKRDANK (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_030268"
FT VAR_SEQ 809
FT /note="R -> RYRLELMRQIYNVESPPSSMLFDTSGMEALSGWISPPSQHPGQQAQL
FT LPLEPPVESERGRLTLANLIPSR (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_030269"
FT CONFLICT 288
FT /note="V -> VS (in Ref. 1; AAF74192)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1670 AA; 189345 MW; 263A8EF721B214E0 CRC64;
MSSVKVAVRV RPFNSREIAR ESKCIIEMAG ATTAITNPKV PPNTSDSVKR FNFDYSYWSH
DHHDADFSTQ SMVYKDIGEE MLQHSFDGYN VCIFAYGQTG AGKSYTMMGR QEEQQEGIIP
MICKDLFTRI QDTETDDLKY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTDYQ DIHDLIDEGN KARTVAATNM NETSSRSHAV FTIFFTQRRH DLMTNLTTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVAS KKKNTKKADF
IPYRDSALTW LLRENLGGNS KTAMIAAISP ADINYDETLS TLRYADRAKQ IVCKAVVNED
ANAKLIRELK EEIQKLRDLL KAEGIEVQEE DELTKSTVIK SPTKSRNRNG STTEMAVDQL
QASEKLIAEL NETWEEKLKR TEEIRVQREA VFAEMGVAVK EDGITVGVFS PKKTPHLVNL
NEDPNLSECL LYYIKEGLTR LGTHEANVPQ DIQLSGSHIL KEHCTFENKN STVTLLPHKD
AIIYVNGRKL VEPEVLKTGS RVILGKNHVF RFTNPEQARE LRDKIETENE AENEVEKTDT
QQVDWNFAQC ELLEKQGIDL KAEMKKRLDN LEEQYKREKL QADQQFEEQR KTYEARIDAL
QKQVEEQSMT MSMYSSYSPE DFHQEEDVYT NPMYESCWTA REAGLAAWAF RKWRYHQFTS
LRDDLWGNAI FLKEANAISV ELKKKVQFQF TLLTDTLYSP LPPELASTVA PVHQEDEFGA
PPVSKTLVAV EVTDTKNGAT HHWSLEKLRQ RLELMREMYH NEAEMSPTSP DYNVESLTGG
DPFYDRFPWF RMVGRSFIYL SNLLYPVPLV HKVAIVNERG DVRGYLRIAV QPVLDEESID
FNNGVKQSAR LVFNEDDAKP KYRALNEKDD VQRYIDNGGL DSKLEELEDV DSGRGIDSNS
ASECHENSEE PGEHLQVGKE FTFRVTVLQA TGIGAEYADI FCQFNFLHRH EEAFSTEPVK
NSASGAPLGF YHVQNITVPV TKSFIEYLKT QPIMFKIFGH YQTHPLHKDA KQDFVSRPPP
RRMLPPSIPI SQPVRSPKFG PLPCAPTSTV LAKHDVLVWF EICELAPNGE YVPSVVEHSD
DLPCRGLFLL HQGIQRRIRI TIVHEPTTEV KWKDINELVV GRIRNTPESS DEQDEDACVL
SLGLFPGEAL EVPGDDRSFY RFEAAWDSSL HNSALLNRVS QGGETIYITL SAYLELENCA
RPAIITKDLS MVIYGRDART GPRSLKHLFS GQYRNPEANR LTGVYELALR RASEAGSPGV
QRRQRRVLDT SSTYVRGEEN LHGWRPRGDS LIFDHQWELE KLTRLEEVGR MRHLLLLRER
LGMDTNPNPT TKTEKDVCNL AARAATSPVH MVIPQSPQTP VKDPQQIIPE REYNQREQDL
MLKCLKLVQG RYTKSEANDT QTQSDVSPSD EGCADMTVSC ISSNSMENNK FVIRRRLCSP
DRADAPNGWE APAPATQPAL PLRLYVPELE EIRVSPVVAR KGLLNVLEHG GSGWKKRWVI
VRRPYVFIYR SEKDPVERAV LNLATAHVEC SEDQAAMVKI PNTFSVVTKH RGYLLQTLGD
KEVHDWLYAI NPLLAGQIKS RLARRTLEPA SQTASQIQAT NAANANSASK
