ID KIF1A_DROPS Reviewed; 1671 AA.
AC Q28WQ1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Kinesin-like protein unc-104;
GN Name=unc-104 {ECO:0000250|UniProtKB:A1ZAJ2}; ORFNames=GA21168;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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:0000250|UniProtKB:A1ZAJ2}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q60575}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:A1ZAJ2}. Note=Microtubule-associated.
CC {ECO:0000250|UniProtKB:A1ZAJ2}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL26616.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000071; EAL26616.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_004444576.1; XM_004444519.2.
DR AlphaFoldDB; Q28WQ1; -.
DR SMR; Q28WQ1; -.
DR STRING; 46245.Q28WQ1; -.
DR EnsemblMetazoa; FBtr0334361; FBpp0306467; FBgn0081156.
DR GeneID; 4805677; -.
DR KEGG; dpo:4805677; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_10_0_1; -.
DR InParanoid; Q28WQ1; -.
DR PhylomeDB; Q28WQ1; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0081156; Expressed in insect adult head and 2 other cell types or tissues.
DR ExpressionAtlas; Q28WQ1; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0048489; P:synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:UniProtKB.
DR CDD; cd22705; FHA_KIF1; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR049780; PH_KIFIA_KIFIB.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF5; -; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1671
FT /note="Kinesin-like protein unc-104"
FT /id="PRO_0000299497"
FT DOMAIN 3..351
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 500..566
FT /note="FHA"
FT /evidence="ECO:0000255"
FT DOMAIN 1538..1636
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..437
FT /evidence="ECO:0000255"
FT COILED 577..674
FT /evidence="ECO:0000255"
FT COMPBIAS 397..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1671 AA; 189344 MW; EB24053755554292 CRC64;
MSSVKVAVRV RPFNSREIGR ESKCIIEMTG ATTAITNPKV PPNTSEAVKR FNFDYSYWSH
DPRDSDFSTQ TMVYKDIGEE MLQHSFDGYN VCIFAYGQTG AGKSYTMMGR QEEQQEGIIP
MICQDLFTRI HDTETDELKY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTDYQ DIHDLIDEGN KARTVAATNM NETSSRSHAV FTIFFTQRRH DTMTDLTTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVAS KKKHNKKADF
IPYRDSALTW LLRENLGGNS KTAMIAAISP ADINYDETLS TLRYADRAKQ IVCKAVVNED
ANAKLIRELK EEIQKLRDLL KAEGIEVQEE DELNKSTTGI KSPSKSRNRN GSTTEMAVDQ
LQASEKLIAE LNETWEEKLK RTEEIRLQRE AVFAEMGVAV KEDGITVGVF SPKKTPHLVN
LNEDPNLSEC LLYYIKDGLT RLGTHEANVP QDIQLSGSHI LKEHCTFENR NSTVTLLPHK
DAIIFVNGRQ LVEPEVLKTG SRVILGKNHV FRFTNPEQAR ELREKITENE AENEVEKADA
PQVDWNFAQC ELLEKQGIDL KAEMKKRLDN LEEQYKREKM QADQQFEEQR KTYEARIDAL
QKQVEEQSMT MSMYSSYSPE DFHQEEDVYN NPMYESCWTA REAGLAAWAF RKWRYHQFTS
LRDDLWGNAI FLKEANAISV ELKKKVQFQF TLLTDTLYSP LPPELASSVA PLQQEDEFGA
PPVSKTLVAV EVTDTKNGAT HYWSLEKLRQ RLELMREMYH NEAEMSPTSP DYNVESLTGG
DPFYDRFPWF RMVGRSFIYL SNLLYPVPLV HKVAIVNERG DVRGYLRIAV QPVLDEESID
FNNGVKQSAR LVFNEDDAKP KYRALNEKDD VQRYIDNGGH DSKLEELEDV DSGRGIDSNS
ASDCPENAEE PGEHLQVGKE FTFRVTVLQA TGIGAEYADI FCQFNFLHRH EEAFSTEPVK
NSASGAPLGF YHVQNITVPV TKSFIEYLKT QPIMFKIFGH YQTHPLHKDA KQDFVSRPPP
RRMLPPSIPI SQPVRSPKFG PLPCPPSSTV LAKHDVLVWF EICELAPNGE YVPSVVEHSD
DLPCRGLFLL HQGIQRRIRI TIVHEPTPEV KWKDINELVV GRIRNTPESS DEQDEDACVL
SLGLFPGEVL DVPGDDRSFY RFEAAWDSSL HNSALLNRVS QGGETIYITL SAYLELENCA
RPAIVTKDLS MVIYGRDART GPRSLKHLFS GQYRNPEANR LSGVYELSLR RASEAGSPGV
QRRQRRVLDT SSTYVRGEEN LHGWRPRGDS LIFDHQWELE KLTRLEEVGR MRHLLLLRER
LGMDTNPNPT TKTEKDVCNL AARAATSPVH MVIPQSPQTP VKDPQQIMPE REYNQREQDL
MLKCLKLVQA GRYAKNEAND TQTQSDVSPS DEGCADMTVS CISSNSMEDN KFVIRRRLCS
PDRADAPNGW EAPAPATQPA LPLRLYVPEL EEIRVSPVVA RKGLLNVLEH GGSGWKKRWV
TVRRPYVFIY RSEKDPVERA VLNLATAQVE CSEDQAAMVK IPNTFSVVTK HRGYLLQTLG
DKEVHDWLYA INPLLAGQIK SRLARRTLEP ASQTASQIQA SSAANANSAN K
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