KIF3B_MOUSE
ID KIF3B_MOUSE Reviewed; 747 AA.
AC Q61771; Q3UFZ8; Q8BNH4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Kinesin-like protein KIF3B;
DE AltName: Full=Microtubule plus end-directed kinesin motor 3B;
DE Contains:
DE RecName: Full=Kinesin-like protein KIF3B, N-terminally processed;
GN Name=Kif3b {ECO:0000312|MGI:MGI:107688};
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], SUBUNIT, INTERACTION WITH KIF3A, AND FUNCTION.
RC STRAIN=ICR; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=9865700; DOI=10.1016/s0092-8674(00)81705-5;
RA Nonaka S., Tanaka Y., Okada Y., Takeda S., Harada A., Kanai Y., Kido M.,
RA Hirokawa N.;
RT "Randomization of left-right asymmetry due to loss of nodal cilia
RT generating leftward flow of extraembryonic fluid in mice lacking KIF3B
RT motor protein.";
RL Cell 95:829-837(1998).
RN [4]
RP SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH KIB3A AND KIFAP3.
RX PubMed=8710890; DOI=10.1073/pnas.93.16.8443;
RA Yamazaki H., Nakata T., Okada Y., Hirokawa N.;
RT "Cloning and characterization of KAP3: a novel kinesin superfamily-
RT associated protein of KIF3A/3B.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8443-8448(1996).
RN [5]
RP INTERACTION WITH IFT20.
RX PubMed=12821668; DOI=10.1074/jbc.m300156200;
RA Baker S.A., Freeman K., Luby-Phelps K., Pazour G.J., Besharse J.C.;
RT "IFT20 links kinesin II with a mammalian intraflagellar transport complex
RT that is conserved in motile flagella and sensory cilia.";
RL J. Biol. Chem. 278:34211-34218(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 SUBCELLULAR LOCATION.
RX PubMed=25243405; DOI=10.1371/journal.pone.0108470;
RA Broekhuis J.R., Verhey K.J., Jansen G.;
RT "Regulation of cilium length and intraflagellar transport by the RCK-
RT kinases ICK and MOK in renal epithelial cells.";
RL PLoS ONE 9:E108470-E108470(2014).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=31746486; DOI=10.15252/embj.2018101090;
RA Alsabban A.H., Morikawa M., Tanaka Y., Takei Y., Hirokawa N.;
RT "Kinesin Kif3b mutation reduces NMDAR subunit NR2A trafficking and causes
RT schizophrenia-like phenotypes in mice.";
RL EMBO J. 39:e101090-e101090(2020).
CC -!- FUNCTION: Microtubule-based molecular motor that transport
CC intracellular cargos, such as vesicles, organelles and protein
CC complexes. Uses ATP hydrolysis to generate force to bind and move along
CC the microtubule (PubMed:7559760). Plays a role in cilia formation
CC (PubMed:9865700). Involved in photoreceptor integrity and opsin
CC trafficking in rod photoreceptors (By similarity). Transports vesicles
CC containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into
CC neuronal dendrites (PubMed:31746486). {ECO:0000250|UniProtKB:O15066,
CC ECO:0000269|PubMed:31746486, ECO:0000269|PubMed:7559760,
CC ECO:0000269|PubMed:9865700}.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3B (PubMed:7559760). KIF3A/KIF3B
CC heterodimer interacts with KIFAP3 forming a heterotrimeric
CC (KIF3A/KIF3B/KIFAP3) complex (PubMed:8710890). Interacts with the SMC3
CC subunit of the cohesin complex (By similarity). Interacts directly with
CC IFT20 (PubMed:12821668). Interacts with FLCN (By similarity).
CC {ECO:0000250|UniProtKB:O15066, ECO:0000269|PubMed:12821668,
CC ECO:0000269|PubMed:7559760, ECO:0000269|PubMed:8710890}.
CC -!- INTERACTION:
CC Q61771; P28741: Kif3a; NbExp=6; IntAct=EBI-6395332, EBI-6169413;
CC Q61771; Q8VI40: Trim60; NbExp=3; IntAct=EBI-6395332, EBI-6395249;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, cilium {ECO:0000269|PubMed:25243405,
CC ECO:0000269|PubMed:9865700}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:31746486}. Note=Colocalized with GRIN2A in
CC dendritic shafts and in DLG4-positive spines.
CC {ECO:0000269|PubMed:31746486}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice do not survive beyond
CC midgestation, exhibiting growth retardation, pericardial sac
CC ballooning, and neural tube disorganization (PubMed:9865700). Kif3b
CC +/- mice exhibit schizophrenia-like phenotypes, both behaviorally and
CC histologically. Hippocampal neurons have altered spine morphology and
CC synapse function, and at the cellular level, they display abnormal
CC growth cone morphology (PubMed:31746486). {ECO:0000269|PubMed:31746486,
CC ECO:0000269|PubMed:9865700}.
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; D26077; BAA05070.1; -; mRNA.
DR EMBL; AK148200; BAE28411.1; -; mRNA.
DR EMBL; AK083700; BAC38996.1; -; mRNA.
DR CCDS; CCDS16911.1; -.
DR PIR; A57107; A57107.
DR RefSeq; NP_032470.3; NM_008444.4.
DR AlphaFoldDB; Q61771; -.
DR SMR; Q61771; -.
DR BioGRID; 200942; 14.
DR ComplexPortal; CPX-3203; KIF3 complex variant AB.
DR ComplexPortal; CPX-3204; KIF3 complex variant AB-KAP3.
DR CORUM; Q61771; -.
DR IntAct; Q61771; 8.
DR MINT; Q61771; -.
DR STRING; 10090.ENSMUSP00000028977; -.
DR iPTMnet; Q61771; -.
DR PhosphoSitePlus; Q61771; -.
DR EPD; Q61771; -.
DR MaxQB; Q61771; -.
DR PaxDb; Q61771; -.
DR PRIDE; Q61771; -.
DR ProteomicsDB; 269219; -.
DR Antibodypedia; 1560; 115 antibodies from 22 providers.
DR DNASU; 16569; -.
DR Ensembl; ENSMUST00000028977; ENSMUSP00000028977; ENSMUSG00000027475.
DR GeneID; 16569; -.
DR KEGG; mmu:16569; -.
DR UCSC; uc008nhp.2; mouse.
DR CTD; 9371; -.
DR MGI; MGI:107688; Kif3b.
DR VEuPathDB; HostDB:ENSMUSG00000027475; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000153739; -.
DR HOGENOM; CLU_001485_22_4_1; -.
DR InParanoid; Q61771; -.
DR OMA; LESKMLC; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; Q61771; -.
DR TreeFam; TF105223; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16569; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Kif3b; mouse.
DR PRO; PR:Q61771; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61771; protein.
DR Bgee; ENSMUSG00000027475; Expressed in spermatocyte and 239 other tissues.
DR ExpressionAtlas; Q61771; baseline and differential.
DR Genevisible; Q61771; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
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:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005819; C:spindle; 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:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0036372; P:opsin transport; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
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 Acetylation; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Synapse.
FT CHAIN 1..747
FT /note="Kinesin-like protein KIF3B"
FT /id="PRO_0000424496"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:O15066"
FT CHAIN 2..747
FT /note="Kinesin-like protein KIF3B, N-terminally processed"
FT /id="PRO_0000125396"
FT DOMAIN 9..340
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 374..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..747
FT /note="Globular"
FT REGION 698..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..579
FT /evidence="ECO:0000255"
FT COMPBIAS 392..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O15066"
FT MOD_RES 2
FT /note="N-acetylserine; in Kinesin-like protein KIF3B, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:O15066"
FT CONFLICT 13
FT /note="V -> M (in Ref. 2; BAE28411)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="V -> A (in Ref. 2; BAC38996)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="S -> N (in Ref. 2; BAE28411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 85288 MW; FA369A4190EC8B47 CRC64;
MSKLKSSESV RVVVRCRPMN GKEKAASYDK VVDVDVKLGQ VSVKNPKGTS HEMPKTFTFD
AVYDWNAKQF ELYDETFRPL VDSVLQGFNG TIFAYGQTGT GKTYTMEGVR GDPEKRGVIP
NSFDHIFTHI SRSQNQQYLV RASYLEIYQE EIRDLLSKDQ TKRLELKERP DTGVYVKDLS
SFVTKSVKEI EHVMNVGNQN RSVGATNMNE HSSRSHAIFV ITIECSEVGL DGENHIRVGK
LNLVDLAGSE RQAKTGAQGE RLKEATKINL SLSALGNVIS ALVDGKSTHI PYRDSKLTRL
LQDSLGGNAK TVMVANVGPA SYNVEETLTT LRYANRAKNI KNKPRVNEDP KDALLREFQE
EIARLKAQLE KRSIGRRKRR EKRREGGGSG GGGEEEEEEG EEGEEDGDDK DDYWREQQEK
LEIEKRAIVE DHSLVAEEKM RLLKEKEKKM EDLRREKDAA EMLGAKIKAM ESKLLVGGKN
IVDHTNEQQK ILEQKRQEIA EQKRREREIQ QQMESRDEET LELKETYTSL QQEVDIKTKK
LKKLFSKLQA VKAEIHDLQE EHIKERQELE QTQNELTREL KLKHLIIENF IPLEEKNKIM
NRSFFDDEED HWKLHPITRL ENQQMMKRPV SAVGYKRPLS QHARMSMMIR PEPRYRAENI
MLLELDMPSR TTRDYEGPAI SPKVQAALDA ALQDEDEIQV DASSFESTAS RKPKARPKSG
RKSGSSSSSS GNPASQFYPQ SRGLVPK
