ID A0A087WQE8_MOUSE Unreviewed; 1791 AA.
AC A0A087WQE8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Kinesin family member 1A {ECO:0000313|Ensembl:ENSMUSP00000140163.2};
GN Name=Kif1a {ECO:0000313|Ensembl:ENSMUSP00000140163.2,
GN ECO:0000313|MGI:MGI:108391};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000140163.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000140163.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140163.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000140163.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140163.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR RefSeq; XP_006529221.1; XM_006529158.3.
DR SMR; A0A087WQE8; -.
DR jPOST; A0A087WQE8; -.
DR ProteomicsDB; 361439; -.
DR Antibodypedia; 1377; 64 antibodies from 17 providers.
DR DNASU; 16560; -.
DR Ensembl; ENSMUST00000190723.7; ENSMUSP00000140163.2; ENSMUSG00000014602.16.
DR AGR; MGI:108391; -.
DR MGI; MGI:108391; Kif1a.
DR VEuPathDB; HostDB:ENSMUSG00000014602; -.
DR GeneTree; ENSGT00940000156474; -.
DR HOGENOM; CLU_001485_10_0_1; -.
DR OrthoDB; 126886at2759; -.
DR PhylomeDB; A0A087WQE8; -.
DR BioGRID-ORCS; 16560; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Kif1a; mouse.
DR Proteomes; UP000000589; Chromosome 1.
DR Bgee; ENSMUSG00000014602; Expressed in superior frontal gyrus and 168 other cell types or tissues.
DR ExpressionAtlas; A0A087WQE8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22726; FHA_KIF1A; 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; IPR049779; FHA_KIF1A.
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:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 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; 1.
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; PS50006; FHA_DOMAIN; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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|EPD:A0A087WQE8,
KW ECO:0007829|MaxQB:A0A087WQE8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 5..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 525..581
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1676..1774
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 884..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1620..1660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..466
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 637..671
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 884..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..930
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1537
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:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1791 AA; 202174 MW; 21ABE7C7F5FCA0D7 CRC64;
MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKETPKSF SFDYSYWSHT
SPEDINYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEKDQQGIIP
QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETNITTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAII
NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD ITDTNTVPGG PKLTNALVGM SPSSSLSALS
SRAASVSSLH ERILFAPGSE EAIERLKETE KIIAELNETW EEKLRRTEAI RMEREALLAE
MGVAMREDGG TLGVFSPKKT PHLVNLNEDP LMSECLLYYI KDGVTRVGRE DAERRQDIVL
SGHFIKEEHC IFRSDSRGGG EAVVTLEPCE GADTYVNGKK VTEPSILRSG NRIIMGKSHV
FRFNHPEQAR QERERTPCAE TPAEPVDWAF AQRELLEKQG IDMKQEMEQR LQELEDQYRR
EREEATYLLE QQRLDYESKL EALQKQMDSR YYPEVNEEEE EPEDEVQWTE RECELALWAF
RKWKWYQFTS LRDLLWGNAI FLKEANAISV ELKKKVQFQF VLLTDTLYSP LPPDLLPPEA
AKDRETRPFP RTIVAVEVQD QKNGATHYWT LEKLRQRLDL MREMYDRAAE VPSSVVEDCD
NVVTGGDPFY DRFPWFRLVG SSVISGCNSY PLLNTCMSER MAALTPSPTF SSPDSDTTEP
AEEQSVGEEE EEEEEEEEEE EEEDLEDDVF PEHTLCDGQD PFYDRPPLFS LVGRAFVYLS
NLLYPVPLVH RVAIVSEKGE VKGFLRVAVQ AISADEEAPD YGSGVRQSGT AKISFDDQHF
EKFQSESCPV VGMSRSGTSQ EELRIVEGQG QGADAGPSAD EVNNNTCSAV PPEGLMDSPE
KAALDGPLDT ALDHLRLGST FTFRVTVLQA SSISAEYADI FCQFNFIHRH DEAFSTEPLK
NTGRGPPLGF YHVQNIAVEV TKSFIEYIKS QPIVFEVFGH YQQHPFPPLC KDVLSPLRPS
RRHFPRVMPL SKPVPATKLS TMTRPSPGPC HCKYDLLVYF EICELEANGD YIPAVVDHRG
GMPCMGTFLL HQGIQRRITV TLLHETGSHI RWKEVRELVV GRIRNTPETD EALIDPNILS
LNILSSGYVH PAQDDRTFYQ FEAAWDSSMH NSLLLNRVTP YREKIYMTLS AYIEMENCTQ
PAVITKDFCM VFYSRDAKLP ASRSIRNLFG SGSLRATEGN RVTGVYELSL CHVADAGSPG
MQRRRRRVLD TSVAYVRGEE NLAGWRPRSD SLILDHQWEL EKLSLLQEVE KTRHYLLLRE
KLETTQRPGP EVLSPASSED SESRSSSGAS SPLSAEGQPS PLEAPNERQR ELAVKCLRLL
MHTFNREYTH SHVCISASES KLSEMSVTLM RDPSMSPLGA ATLTPSSTCP SLIEGRYGAT
DVRTPQPCSR PASPEPELLP ELDSKKTPSP VRATETEKEP QRLLVPDIQE IRVSPIVSKK
GYLHFLEPHT AGWAKRFVVV RRPYAYMYNS DKDTVERFVL NLSTAQVEYS EDQQAMLKTP
NTFAVCTEHR GILLQANSDK DMHDWLYAFN PLLAGTIRSK LSRRRSAQMR V
//
