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   27-MAR-2024, entry version 165.
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   SASBDB; 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   GlyGen; Q61771; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61771; -.
DR   PhosphoSitePlus; Q61771; -.
DR   EPD; Q61771; -.
DR   MaxQB; Q61771; -.
DR   PaxDb; 10090-ENSMUSP00000028977; -.
DR   ProteomicsDB; 269219; -.
DR   Pumba; Q61771; -.
DR   Antibodypedia; 1560; 139 antibodies from 23 providers.
DR   DNASU; 16569; -.
DR   Ensembl; ENSMUST00000028977.7; ENSMUSP00000028977.7; ENSMUSG00000027475.10.
DR   GeneID; 16569; -.
DR   KEGG; mmu:16569; -.
DR   UCSC; uc008nhp.2; mouse.
DR   AGR; MGI:107688; -.
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; 5481713at2759; -.
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 77 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 241 other cell types or tissues.
DR   ExpressionAtlas; Q61771; baseline and differential.
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: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   CDD; cd01371; KISc_KIF3; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF29; KINESIN-LIKE PROTEIN; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   Genevisible; Q61771; MM.
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
//