KIF3A_HUMAN
ID KIF3A_HUMAN Reviewed; 699 AA.
AC Q9Y496; A8MSW9; Q59EN1; Q86XE9; Q9Y6V4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Kinesin-like protein KIF3A;
DE AltName: Full=Microtubule plus end-directed kinesin motor 3A;
GN Name=KIF3A; Synonyms=KIF3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=10548469; DOI=10.1006/exer.1999.0724;
RA Whitehead J.L., Wang S.Y., Bost-Usinger L., Hoang E., Frazer K.A.,
RA Burnside B.;
RT "Photoreceptor localization of the KIF3A and KIF3B subunits of the
RT heterotrimeric microtubule motor kinesin II in vertebrate retina.";
RL Exp. Eye Res. 69:491-503(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-172.
RC TISSUE=Testis;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP INTERACTION WITH AP3B1.
RX PubMed=19934039; DOI=10.1073/pnas.0909176106;
RA Azevedo C., Burton A., Ruiz-Mateos E., Marsh M., Saiardi A.;
RT "Inositol pyrophosphate mediated pyrophosphorylation of AP3B1 regulates
RT HIV-1 Gag release.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21161-21166(2009).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INTERACTION WITH CLN3.
RX PubMed=22261744; DOI=10.1007/s00018-011-0913-1;
RA Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K.,
RA Neefjes J., Olkkonen V.M., Jalanko A.;
RT "Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins
RT and modifies location of late endosomal compartments.";
RL Cell. Mol. Life Sci. 69:2075-2089(2012).
RN [11]
RP 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).
RN [12]
RP INTERACTION WITH FLCN.
RX PubMed=27072130; DOI=10.1074/jbc.m116.719997;
RA Zhong M., Zhao X., Li J., Yuan W., Yan G., Tong M., Guo S., Zhu Y.,
RA Jiang Y., Liu Y., Jiang Y.;
RT "Tumor suppressor folliculin regulates mTORC1 through primary cilia.";
RL J. Biol. Chem. 291:11689-11697(2016).
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. Plays a role in centriole
CC cohesion and subdistal appendage organization and function. Regulates
CC the formation of the subdistal appendage via recruitment of DCTN1 to
CC the centriole. Also required for ciliary basal feet formation and
CC microtubule anchoring to mother centriole.
CC {ECO:0000250|UniProtKB:P28741}.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3B (By similarity). Interacts with
CC PIFO (PubMed:20643351). Interacts with CLN3 (PubMed:22261744).
CC Interacts with DCTN1 (By similarity). Interacts with FLCN
CC (PubMed:27072130). Interacts with AP3B1 (PubMed:19934039).
CC {ECO:0000250|UniProtKB:P28741, ECO:0000269|PubMed:19934039,
CC ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:22261744,
CC ECO:0000269|PubMed:27072130}.
CC -!- INTERACTION:
CC Q9Y496; O00203-1: AP3B1; NbExp=5; IntAct=EBI-1104844, EBI-15816315;
CC Q9Y496; Q9NRI5: DISC1; NbExp=5; IntAct=EBI-1104844, EBI-529989;
CC Q9Y496; Q92845: KIFAP3; NbExp=7; IntAct=EBI-1104844, EBI-954040;
CC Q9Y496; Q9BXF6: RAB11FIP5; NbExp=2; IntAct=EBI-1104844, EBI-1387068;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:P28741}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:23386061}. Note=Localizes to the subdistal
CC appendage region of the centriole. {ECO:0000269|PubMed:23386061}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin II subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC04475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD93017.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF041853; AAC72294.1; -; mRNA.
DR EMBL; AB209780; BAD93017.1; ALT_INIT; mRNA.
DR EMBL; AC004039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004237; AAC04475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC045542; AAH45542.1; -; mRNA.
DR CCDS; CCDS34235.1; -.
DR RefSeq; NP_001287720.1; NM_001300791.1.
DR RefSeq; NP_001287721.1; NM_001300792.1.
DR RefSeq; NP_008985.3; NM_007054.6.
DR AlphaFoldDB; Q9Y496; -.
DR SMR; Q9Y496; -.
DR BioGRID; 116300; 116.
DR ComplexPortal; CPX-3138; KIF3 complex variant AB.
DR ComplexPortal; CPX-3199; KIF3 complex variant AC.
DR ComplexPortal; CPX-3200; KIF3 complex variant AC-KAP3.
DR ComplexPortal; CPX-3201; KIF3 complex variant AB-KAP3.
DR CORUM; Q9Y496; -.
DR DIP; DIP-33237N; -.
DR IntAct; Q9Y496; 69.
DR MINT; Q9Y496; -.
DR STRING; 9606.ENSP00000385808; -.
DR BindingDB; Q9Y496; -.
DR ChEMBL; CHEMBL5544; -.
DR iPTMnet; Q9Y496; -.
DR MetOSite; Q9Y496; -.
DR PhosphoSitePlus; Q9Y496; -.
DR BioMuta; KIF3A; -.
DR DMDM; 296439481; -.
DR EPD; Q9Y496; -.
DR jPOST; Q9Y496; -.
DR MassIVE; Q9Y496; -.
DR MaxQB; Q9Y496; -.
DR PaxDb; Q9Y496; -.
DR PeptideAtlas; Q9Y496; -.
DR PRIDE; Q9Y496; -.
DR ProteomicsDB; 86139; -.
DR Antibodypedia; 14507; 226 antibodies from 32 providers.
DR DNASU; 11127; -.
DR Ensembl; ENST00000378746.8; ENSP00000368020.3; ENSG00000131437.16.
DR GeneID; 11127; -.
DR KEGG; hsa:11127; -.
DR UCSC; uc003kxo.4; human.
DR CTD; 11127; -.
DR DisGeNET; 11127; -.
DR GeneCards; KIF3A; -.
DR HGNC; HGNC:6319; KIF3A.
DR HPA; ENSG00000131437; Tissue enhanced (brain, retina).
DR MIM; 604683; gene.
DR neXtProt; NX_Q9Y496; -.
DR OpenTargets; ENSG00000131437; -.
DR PharmGKB; PA30102; -.
DR VEuPathDB; HostDB:ENSG00000131437; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156386; -.
DR HOGENOM; CLU_001485_22_3_1; -.
DR InParanoid; Q9Y496; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; Q9Y496; -.
DR TreeFam; TF105223; -.
DR PathwayCommons; Q9Y496; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-5635838; Activation of SMO.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9Y496; -.
DR SIGNOR; Q9Y496; -.
DR BioGRID-ORCS; 11127; 16 hits in 1076 CRISPR screens.
DR ChiTaRS; KIF3A; human.
DR GeneWiki; KIF3A; -.
DR GenomeRNAi; 11127; -.
DR Pharos; Q9Y496; Tbio.
DR PRO; PR:Q9Y496; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y496; protein.
DR Bgee; ENSG00000131437; Expressed in Brodmann (1909) area 23 and 180 other tissues.
DR ExpressionAtlas; Q9Y496; baseline and differential.
DR Genevisible; Q9Y496; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016939; C:kinesin II complex; IDA:BHF-UCL.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; TAS:BHF-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0006996; P:organelle organization; TAS:ProtInc.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; TAS:BHF-UCL.
DR GO; GO:1902414; P:protein localization to cell junction; IMP:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IMP:BHF-UCL.
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 ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..699
FT /note="Kinesin-like protein KIF3A"
FT /id="PRO_0000125393"
FT DOMAIN 14..345
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 372..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..699
FT /note="Globular"
FT COILED 355..590
FT /evidence="ECO:0000255"
FT COMPBIAS 382..398
FT /note="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 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 172
FT /note="K -> I (in dbSNP:rs17854353)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055319"
FT CONFLICT 151
FT /note="E -> G (in Ref. 4; AAH45542)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="E -> A (in Ref. 1; AAC72294)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="R -> RDQA (in Ref. 2; BAD93017)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="R -> RDQT (in Ref. 4; AAH45542)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="R -> RIQI (in Ref. 1; AAC72294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 80041 MW; A0BF5BB1F699DF12 CRC64;
MPINKSEKPE SCDNVKVVVR CRPLNEREKS MCYKQAVSVD EMRGTITVHK TDSSNEPPKT
FTFDTVFGPE SKQLDVYNLT ARPIIDSVLE GYNGTIFAYG QTGTGKTFTM EGVRAIPELR
GIIPNSFAHI FGHIAKAEGD TRFLVRVSYL EIYNEEVRDL LGKDQTQRLE VKERPDVGVY
IKDLSAYVVN NADDMDRIMT LGHKNRSVGA TNMNEHSSRS HAIFTITIEC SEKGIDGNMH
VRMGKLHLVD LAGSERQAKT GATGQRLKEA TKINLSLSTL GNVISALVDG KSTHVPYRNS
KLTRLLQDSL GGNSKTMMCA NIGPADYNYD ETISTLRYAN RAKNIKNKAR INEDPKDALL
RQFQKEIEEL KKKLEEGEEI SGSDISGSEE DDDEEGEVGE DGEKRKKRRG KKKVSPDKMI
EMQAKIDEER KALETKLDME EEERNKARAE LEKREKDLLK AQQEHQSLLE KLSALEKKVI
VGGVDLLAKA EEQEKLLEES NMELEERRKR AEQLRRELEE KEQERLDIEE KYTSLQEEAQ
GKTKKLKKVW TMLMAAKSEM ADLQQEHQRE IEGLLENIRQ LSRELRLQML IIDNFIPRDY
QEMIENYVHW NEDIGEWQLK CVAYTGNNMR KQTPVPDKKE KDPFEVDLSH VYLAYTEESL
RQSLMKLERP RTSKGKARPK TGRRKRSAKP ETVIDSLLQ
