KIF3B_DANRE
ID KIF3B_DANRE Reviewed; 775 AA.
AC F1QN54; A6H8R7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Kinesin-like protein KIF3B;
GN Name=kif3b {ECO:0000312|ZFIN:ZDB-GENE-050119-3};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22308397; DOI=10.1073/pnas.1116035109;
RA Zhao C., Omori Y., Brodowska K., Kovach P., Malicki J.;
RT "Kinesin-2 family in vertebrate ciliogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:2388-2393(2012).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=28855254; DOI=10.1074/jbc.m117.784017;
RA Feng D., Chen Z., Yang K., Miao S., Xu B., Kang Y., Xie H., Zhao C.;
RT "The cytoplasmic tail of rhodopsin triggers rapid rod degeneration in
RT kinesin-2 mutants.";
RL J. Biol. Chem. 292:17375-17386(2017).
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 (By similarity). Plays a role in cilia formation.
CC Required for photoreceptor development (PubMed:22308397,
CC PubMed:28855254). {ECO:0000250|UniProtKB:Q61771,
CC ECO:0000269|PubMed:22308397, ECO:0000269|PubMed:28855254}.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3B. KIF3A/KIF3B heterodimer
CC interacts with KIFAP3 forming a heterotrimeric (KIF3A/KIF3B/KIFAP3)
CC complex. {ECO:0000250|UniProtKB:Q61771}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q61771}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q61771}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q61771}.
CC -!- DISRUPTION PHENOTYPE: Loss of function of Kif3b only results in
CC ciliogenesis defects in a subset of cilia. Robust cilia are still
CC present in the central nervous system. Mutant have rapid rod
CC degeneration and delayed outer segment genesis, but cones appear
CC normal. The mild phenotype of kif3b mutants may be related to the
CC presence of the kif3c protein. {ECO:0000269|PubMed:22308397,
CC ECO:0000269|PubMed:28855254}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; CU914163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO904971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146722; AAI46723.1; -; mRNA.
DR RefSeq; NP_001093615.1; NM_001100145.1.
DR RefSeq; XP_009294904.1; XM_009296629.2.
DR AlphaFoldDB; F1QN54; -.
DR SMR; F1QN54; -.
DR STRING; 7955.ENSDARP00000105893; -.
DR PaxDb; F1QN54; -.
DR Ensembl; ENSDART00000168199; ENSDARP00000133077; ENSDARG00000101120.
DR Ensembl; ENSDART00000186852; ENSDARP00000150665; ENSDARG00000101120.
DR GeneID; 100101641; -.
DR KEGG; dre:100101641; -.
DR CTD; 9371; -.
DR ZFIN; ZDB-GENE-050119-3; kif3b.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000153739; -.
DR InParanoid; F1QN54; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; F1QN54; -.
DR TreeFam; TF105223; -.
DR Reactome; R-DRE-5620924; Intraflagellar transport.
DR Reactome; R-DRE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DRE-983189; Kinesins.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR ExpressionAtlas; F1QN54; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IDA:ZFIN.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IMP:ZFIN.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0048884; P:neuromast development; IMP:ZFIN.
DR GO; GO:0043584; P:nose development; IMP:ZFIN.
DR GO; GO:0036372; P:opsin transport; ISS:UniProtKB.
DR GO; GO:0042461; P:photoreceptor cell development; IMP:UniProtKB.
DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP:ZFIN.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IGI:ZFIN.
DR GO; GO:0048793; P:pronephros development; IMP:ZFIN.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ZFIN.
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 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Synapse.
FT CHAIN 1..775
FT /note="Kinesin-like protein KIF3B"
FT /id="PRO_0000453041"
FT DOMAIN 9..341
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 372..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 501..591
FT /evidence="ECO:0000255"
FT COMPBIAS 392..415
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..766
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:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 133
FT /note="R -> C (in Ref. 2; AAI46723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 88477 MW; 9346279BA81D3689 CRC64;
MSKSKSSESV KVVVRCRPMN EKERVANFNR VVSVDVKLGQ VAVCNPRGAS SHEHPKVFTF
DSVYDWNSKQ MELYDETFRP LVDSVLFGFN GTIFAYGQTG TGKTYTMEGV RNDPERRGVI
PNSFEHIFTH ISRSQNQQYL VRASYLEIYQ EEIRDLLSKD QARRLELKER PDTGVYVKDL
SSFVTKSVRE IEHVMNVGNQ NRSVGATNMN EHSSRSHAIF VITIECSELG PDGENHIRVG
KLNLVDLAGS ERQTKTGAQG ERLKEATKIN LSLSALGNVI SALVDGRSTH IPYRDSKLTR
LLQDSLGGNA RTVMVANIGP ASYNVEETLT TLRYANRAKN IKNKPRVNED PKDALLREFQ
EEIARLKEQL EKRSGRKRRR RRRRRVGEGG EEFEDGEDEE DDDDDDEDEE EGVDADKNIA
DYWHEQQEKL EKERRAIMED HSLVAEEKQR LLKEKERKMT DLHKEKEASE MLTAKVKAME
SKLLVGGKNI VDHTNEQQKV LELKRQEIAE QKRREREMKQ EMECRDEETL ELKETYSSLQ
QEVDIKTKKL KKLFSKLQSV KSEIQDAQDE HVKYRQELEQ TQNELTRELK LKHLIIENFI
PMEEKNKIVT RATFDEEDDL WKMTPITRIQ NSDHQMMKRP VSAVGYRRPL SQHARMAMLM
RPDVRYKAEN ILLLELDLPS RTTKDYEGPV IAPKVAAALE DALREEDEIQ VDASGFHASL
GSSPGLSASA AGFSKKPKSG RPKTGKKVST PTSAHSPLSG SGSPLYPQSR GLVPK
