KIF3A_MOUSE
ID KIF3A_MOUSE Reviewed; 701 AA.
AC P28741; Q7TSZ7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Kinesin-like protein KIF3A;
DE AltName: Full=Microtubule plus end-directed kinesin motor 3A;
GN Name=Kif3a; Synonyms=Kif3;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1447303; DOI=10.1083/jcb.119.5.1287;
RA Aizawa H., Sekine Y., Takemura R., Zhang Z., Nangaku M., Hirokawa N.;
RT "Kinesin family in murine central nervous system.";
RL J. Cell Biol. 119:1287-1296(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBUNIT.
RX PubMed=7559760; DOI=10.1083/jcb.130.6.1387;
RA Yamazaki H., Nakata T., Okada Y., Hirokawa N.;
RT "KIF3A/B: a heterodimeric kinesin superfamily protein that works as a
RT microtubule plus end-directed motor for membrane organelle transport.";
RL J. Cell Biol. 130:1387-1399(1995).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and Testis;
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 [7]
RP INTERACTION WITH PIFO.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21670265; DOI=10.1073/pnas.1016214108;
RA Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J.,
RA Pontoglio M., Somlo S., Igarashi P.;
RT "Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase
RT anchoring protein complex that is disrupted in cystic kidney diseases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011).
RN [9]
RP FUNCTION, INTERACTION WITH DCTN1, AND SUBCELLULAR LOCATION.
RX PubMed=23386061; DOI=10.1038/emboj.2013.3;
RA Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
RA Reiter J.F.;
RT "Kif3a interacts with Dynactin subunit p150 Glued to organize centriole
RT subdistal appendages.";
RL EMBO J. 32:597-607(2013).
CC -!- FUNCTION: Microtubule-based anterograde translocator for membranous
CC organelles. Plus end-directed microtubule sliding activity in vitro.
CC Plays a role in primary cilia formation (PubMed:21670265). Plays a role
CC in centriole cohesion and subdistal appendage organization and
CC function. Regulates the formation of the subdistal appendage via
CC recruitment of DCTN1 to the centriole. Also required for ciliary basal
CC feet formation and microtubule anchoring to mother centriole
CC (PubMed:23386061). {ECO:0000269|PubMed:21670265,
CC ECO:0000269|PubMed:23386061}.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3B (PubMed:7559760). Interacts
CC with PIFO (PubMed:20643351). Interacts with CLN3 (By similarity).
CC Interacts with DCTN1 (PubMed:23386061). Interacts with FLCN (By
CC similarity). Interacts with AP3B1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y496, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:7559760}.
CC -!- INTERACTION:
CC P28741; Q6A078: Cep290; NbExp=3; IntAct=EBI-6169413, EBI-1811999;
CC P28741; O08788: Dctn1; NbExp=4; IntAct=EBI-6169413, EBI-776180;
CC P28741; Q61771: Kif3b; NbExp=6; IntAct=EBI-6169413, EBI-6395332;
CC P28741; P70188: Kifap3; NbExp=4; IntAct=EBI-6169413, EBI-6169443;
CC P28741; Q8VI40: Trim60; NbExp=5; IntAct=EBI-6169413, EBI-6395249;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:21670265}. Cell projection, cilium
CC {ECO:0000269|PubMed:21670265}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}.
CC Note=Localizes to the subdistal appendage region of the centriole.
CC {ECO:0000269|PubMed:23386061}.
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in adult brain tissue
CC (mainly in the cerebellar granular layer) within a single type of
CC neuronal cell.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin II subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; D12645; BAA02166.1; -; mRNA.
DR EMBL; AL596095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052707; AAH52707.1; -; mRNA.
DR CCDS; CCDS48795.1; -.
DR PIR; B44259; B44259.
DR RefSeq; NP_001277734.1; NM_001290805.1.
DR RefSeq; NP_001277735.1; NM_001290806.1.
DR RefSeq; NP_032469.2; NM_008443.4.
DR PDB; 5JVR; X-ray; 2.10 A; A/B/C/D/E/F/G/H=352-359.
DR PDB; 5JX1; X-ray; 1.67 A; A=352-376.
DR PDBsum; 5JVR; -.
DR PDBsum; 5JX1; -.
DR AlphaFoldDB; P28741; -.
DR SMR; P28741; -.
DR BioGRID; 200941; 12.
DR ComplexPortal; CPX-3202; KIF3 complex variant AC.
DR ComplexPortal; CPX-3203; KIF3 complex variant AB.
DR ComplexPortal; CPX-3204; KIF3 complex variant AB-KAP3.
DR ComplexPortal; CPX-3205; KIF3 complex variant AC-KAP3.
DR CORUM; P28741; -.
DR DIP; DIP-46318N; -.
DR IntAct; P28741; 17.
DR MINT; P28741; -.
DR STRING; 10090.ENSMUSP00000112782; -.
DR iPTMnet; P28741; -.
DR PhosphoSitePlus; P28741; -.
DR EPD; P28741; -.
DR jPOST; P28741; -.
DR MaxQB; P28741; -.
DR PaxDb; P28741; -.
DR PRIDE; P28741; -.
DR ProteomicsDB; 263605; -.
DR Antibodypedia; 14507; 226 antibodies from 32 providers.
DR DNASU; 16568; -.
DR Ensembl; ENSMUST00000120613; ENSMUSP00000112782; ENSMUSG00000018395.
DR GeneID; 16568; -.
DR KEGG; mmu:16568; -.
DR UCSC; uc007iwl.2; mouse.
DR CTD; 11127; -.
DR MGI; MGI:107689; Kif3a.
DR VEuPathDB; HostDB:ENSMUSG00000018395; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156386; -.
DR InParanoid; P28741; -.
DR OMA; NMRKHIE; -.
DR TreeFam; TF105223; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-5635838; Activation of SMO.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16568; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Kif3a; mouse.
DR PRO; PR:P28741; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P28741; protein.
DR Bgee; ENSMUSG00000018395; Expressed in ventromedial nucleus of hypothalamus and 231 other tissues.
DR ExpressionAtlas; P28741; baseline and differential.
DR Genevisible; P28741; MM.
DR GO; GO:1904115; C:axon cytoplasm; ISO:MGI.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016939; C:kinesin II complex; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0097470; C:ribbon synapse; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0120170; F:intraciliary transport particle B binding; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0003341; P:cilium movement; IMP:MGI.
DR GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:BHF-UCL.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0036334; P:epidermal stem cell homeostasis; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0044458; P:motile cilium assembly; IMP:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:1905128; P:positive regulation of axo-dendritic protein transport; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:2000771; P:positive regulation of establishment or maintenance of cell polarity regulating cell shape; ISO:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:MGI.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:1902414; P:protein localization to cell junction; ISO:MGI.
DR GO; GO:0015031; P:protein transport; ISO:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..701
FT /note="Kinesin-like protein KIF3A"
FT /id="PRO_0000125394"
FT DOMAIN 14..345
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 365..701
FT /note="Interaction with DCTN1"
FT /evidence="ECO:0000269|PubMed:23386061"
FT REGION 373..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..701
FT /note="Globular"
FT REGION 665..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..592
FT /evidence="ECO:0000255"
FT COMPBIAS 382..397
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 404
FT /note="K -> R (in Ref. 1; BAA02166)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="M -> T (in Ref. 1; BAA02166)"
FT /evidence="ECO:0000305"
FT HELIX 355..376
FT /evidence="ECO:0007829|PDB:5JX1"
SQ SEQUENCE 701 AA; 80170 MW; 15EB43A6F6CC08A3 CRC64;
MPINKSEKPE SCDNVKVVVR CRPLNEREKS MCYRQAVSVD EMRGTITVHK TDSSNEPPKT
FTFDTVFGPE SKQLDVYNLT ARPIIDSVLE GYNGTIFAYG QTGTGKTFTM EGVRAVPGLR
GVIPNSFAHI FGHIAKAEGD TRFLVRVSYL EIYNEEVRDL LGKDQTQRLE VKERPDVGVY
IKDLSAYVVN NADDMDRIMT LGHKNRSVGA TNMNEHSSRS HAIFTITIEC SEKGVDGNMH
VRMGKLHLVD LAGSERQAKT GATGQRLKEA TKINLSLSTL GNVISALVDG KSTHVPYRNS
KLTRLLQDSL GGNSKTMMCA NIGPADYNYD ETISTLRYAN RAKNIKNKAR INEDPKDALL
RQFQKEIEEL KKKLEEGEEV SGSDISGSEE DDEEGELGED GEKKKKRRDQ AGKKKVSPDK
MVEMQAKIDE ERKALETKLD MEEEERNKAR AELERREKDL LKAQQEHQSL LEKLSALEKK
VIVGGVDLLA KAEEQEKLLE ESNMELEERR RRAEQLRKEL EEKEQERLDI EEKYTSLQEE
AQGKTKKLKK VWTMLMAAKS EMADLQQEHQ REIEGLLENI RQLSRELRLQ MLIIDNFIPQ
DYQEMIENYV HWNEDIGEWQ LKCVAYTGNN MRKQTPVPDK KERDPFEVDL SHVYLAYTEE
SLRQSLMKLE RPRTSKGKAR PKMGRRKRSA KPETVIDSLL Q
