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KIF1A_DROPS
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   03-AUG-2022, entry version 103.
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; 7237.FBpp0278781; -.
DR   PRIDE; Q28WQ1; -.
DR   EnsemblMetazoa; FBtr0334361; FBpp0306467; FBgn0081156.
DR   GeneID; 4805677; -.
DR   KEGG; dpo:Dpse_GA21168; -.
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 tissues.
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; 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; 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   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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