KIF1A_AEDAE
ID KIF1A_AEDAE Reviewed; 1644 AA.
AC Q17BU3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Kinesin-like protein unc-104;
GN Name=unc-104 {ECO:0000250|UniProtKB:A1ZAJ2}; ORFNames=AAEL004812;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT43769.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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}.
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DR EMBL; CH477316; EAT43769.1; -; Genomic_DNA.
DR RefSeq; XP_001649847.1; XM_001649797.1.
DR AlphaFoldDB; Q17BU3; -.
DR SMR; Q17BU3; -.
DR STRING; 7159.AAEL004812-PA; -.
DR PRIDE; Q17BU3; -.
DR VEuPathDB; VectorBase:AAEL027393; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_10_2_1; -.
DR InParanoid; Q17BU3; -.
DR OMA; KITICHE; -.
DR PhylomeDB; Q17BU3; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
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; 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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1644
FT /note="Kinesin-like protein unc-104"
FT /id="PRO_0000299494"
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 1542..1640
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 574..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..436
FT /evidence="ECO:0000255"
FT COILED 631..672
FT /evidence="ECO:0000255"
FT COMPBIAS 574..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1441
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 1644 AA; 185610 MW; 1B9C0F9E71427FCF CRC64;
MSSVKVAVRV RPFNSREISR ESKCIIEMSG NTTCITNPKV PPGTSDSIKR FNYDYSYWSH
DPRDAEFSTQ SMVYADIGEE MLQHSFDGYN VCIFAYGQTG AGKSYTMMGK QEESQEGVIP
MICKDLFRRI QETEGVDLKY SVEVSYMEIY CERVRDLLNP KNKGNLKVRE HPLLGPYVED
LSKLAVTSYQ DIHDLIDEGN KARTVAATNM NETSSRSHAV FTIFFTQRRV DKMTSLETEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVAS KSKKSKKADF
IPYRDSVLTW LLRENLGGNS KTAMIAAISP ADINYDETLS TLRYADRAKQ IVCKAVVNED
ANAKLIRELK EEIQKLRELL KAEGIEVQEG NRRTPTPMIC SPNRLRKRTG SSTEMAVDQL
QASEKLIAEL NETWEEKLKR TEQIRLQREA VFAEMGVAVK EDGITVGVFS PKKSPHLVNL
NEDPTLSECL LYYIKDGLTR LGTSEANVPQ DIQLSGSHIL KEHCVFENKD GVVTLVPHKD
ALVYLNGRKL VEPEVLQTGS RVILGKNHVF RFTHPEQARE KREKPKDKDV GENPGGNAEA
ADWNFAQCEL LEKQGIDLKA EMQKRLCALE EQFKREKLAA DQEFEEQRKT YEARIDALQK
QVEEQSMTMS MYSSYSPEDF HQEEDIFVNP LFESCWTARE AGLAAWAFRK WRYHQFTSLR
DDLWGNAIFL KEANAISVEL KKKVQFQFTL LTDTLYSPLP PELAPSPIIG GALTNGQEDE
FGQSPIPRTI VAVEVTDTKN GATHHWSLDK LRQRLELMRE MYHNEAELSP TSPDYNVESL
TGGDPFYDRF PWFRMVGRSF VYLSNLLYPV PLVHKVAIVN ERGDVRGYLR VAVQPVMDEE
NADFNNGVKQ SARIVFDEEQ NGGHKIPKIR TIHDKDEKYI EGSNDIMKLE ELEQEDADSG
RGDSSVASEL HESNEHEPGE HLQPGKEFTF RVTVLQATGI AAEYADIFCQ FNFLHRHEEA
FSTEPVKNSG SGAPLGFYHV QNITVPVTKS FIEYLKTQPI VFKVFGHYQN HPLHKDAKQD
CQITRPPPRR MLPPSIPISQ PVRSPKFGPL PCPPSSTVLA KHDVLVWFEI CELAPNGEYV
PAVVDHSDDL PCRGLYLLHQ GIQRRIRITI VHEPTAEVKW KDIRELVVGR IRNQPEPADE
LDDSDSCVLS LGLFPGEVLE VPGDDRSFFR FEAAWDSSLH NSALLNRVTQ TGEQIFITLS
AYLELENCAR PAIITKDLSM IIYGRDARTG PRSLKHLFSG QYRNPEANRL SGVYELSLRR
ASEAGSPGVQ RRQRRVLDTS STYVRGEENL HGWRPRGDSL IFDHQWELEK LTRLEEVGRV
RHLLMLRERL GMDTTPNPTT KTEKDVCNLA QRASASPVHM VIPPSPQTPV KDQQTPTLPE
RELTPRETEL VWKCVKLIQG RIGGKGDPSD TSNQLAVDAS PGDEGCADMN ASYISGNSIE
LCSPDRVDIP NGWEAPAPVP QSQEVSLRLY VPELEEIRVS PVVARKGYLN VLEHGGSGWK
KRWVTVRRPY VFIFRSDKDP VERAVLNLAT AQVECSEDQA AMVKVPNTFS VVTKHRGYLL
QTLGDKEVHD WLYAINPLLA GQIR
