KIF17_MOUSE
ID KIF17_MOUSE Reviewed; 1038 AA.
AC Q99PW8; A2AM73;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Kinesin-like protein KIF17;
DE Short=MmKIF17;
GN Name=Kif17;
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], FUNCTION, SUBUNIT, INTERACTION WITH APBA1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF 939-MET--LEU-1038.
RC TISSUE=Brain;
RX PubMed=10846156; DOI=10.1126/science.288.5472.1796;
RA Setou M., Nakagawa T., Seog D.-H., Hirokawa N.;
RT "Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-
RT containing vesicle transport.";
RL Science 288:1796-1802(2000).
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 INTERACTION WITH PIWIL1.
RX PubMed=16787948; DOI=10.1242/jcs.03022;
RA Kotaja N., Lin H., Parvinen M., Sassone-Corsi P.;
RT "Interplay of PIWI/Argonaute protein MIWI and kinesin KIF17b in chromatoid
RT bodies of male germ cells.";
RL J. Cell Sci. 119:2819-2825(2006).
RN [4]
RP INTERACTION WITH TBATA.
RX PubMed=17196196; DOI=10.1016/j.yexcr.2006.11.011;
RA Saade M., Irla M., Govin J., Victorero G., Samson M., Nguyen C.;
RT "Dynamic distribution of Spatial during mouse spermatogenesis and its
RT interaction with the kinesin KIF17b.";
RL Exp. Cell Res. 313:614-626(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP INTERACTION WITH IFT52; IFT57 AND TTC30B.
RX PubMed=23810713; DOI=10.1016/j.yexcr.2013.06.010;
RA Howard P.W., Jue S.F., Maurer R.A.;
RT "Interaction of mouse TTC30/DYF-1 with multiple intraflagellar transport
RT complex B proteins and KIF17.";
RL Exp. Cell Res. 319:2275-2281(2013).
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).
CC -!- FUNCTION: Dendrite-specific motor protein which, in association with
CC the Apba1-containing complex (LIN-10-LIN-2-LIN-7 complex), transports
CC vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B
CC along microtubules. {ECO:0000269|PubMed:10846156}.
CC -!- SUBUNIT: Homodimer (PubMed:10846156). Interacts with APBA1 (via PDZ
CC domain); the interaction is direct and is required for association of
CC KIF17 with the cargo that is to be transported (PubMed:10846156).
CC Interacts with IFT B complex components IFT52 and IFT57
CC (PubMed:23810713). Interacts with TTC30B (PubMed:23810713). Interacts
CC with PIWIL1 (PubMed:16787948). Interacts with TBATA (PubMed:17196196).
CC {ECO:0000269|PubMed:10846156, ECO:0000269|PubMed:16787948,
CC ECO:0000269|PubMed:17196196, ECO:0000269|PubMed:23810713}.
CC -!- INTERACTION:
CC Q99PW8; Q9Z0V2: Kcnd2; NbExp=3; IntAct=EBI-959754, EBI-959779;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10846156}. Cell projection, cilium
CC {ECO:0000269|PubMed:25243405}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10846156}. Note=Localizes to dendrites of pyramidal
CC neurons (PubMed:10846156). Does not localize to the axons or nuclei in
CC cerebral cortex, hippocampus or olfactory bulb (PubMed:10846156). Co-
CC localizes with NR2B-containing vesicles along microtubules
CC (PubMed:10846156). {ECO:0000269|PubMed:10846156}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the gray matter of the brain,
CC especially in the hippocampus. {ECO:0000269|PubMed:10846156}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryonic day 16, and expression
CC increases to postnatal week 3. {ECO:0000269|PubMed:10846156}.
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; AB008867; BAB21099.1; -; mRNA.
DR EMBL; AL807249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18823.1; -.
DR RefSeq; NP_034753.1; NM_010623.4.
DR AlphaFoldDB; Q99PW8; -.
DR SMR; Q99PW8; -.
DR BioGRID; 200934; 5.
DR CORUM; Q99PW8; -.
DR DIP; DIP-36586N; -.
DR IntAct; Q99PW8; 2.
DR MINT; Q99PW8; -.
DR STRING; 10090.ENSMUSP00000030539; -.
DR iPTMnet; Q99PW8; -.
DR PhosphoSitePlus; Q99PW8; -.
DR MaxQB; Q99PW8; -.
DR PaxDb; Q99PW8; -.
DR PRIDE; Q99PW8; -.
DR ProteomicsDB; 263444; -.
DR Antibodypedia; 15106; 130 antibodies from 21 providers.
DR DNASU; 16559; -.
DR Ensembl; ENSMUST00000030539; ENSMUSP00000030539; ENSMUSG00000028758.
DR GeneID; 16559; -.
DR KEGG; mmu:16559; -.
DR UCSC; uc008vkq.2; mouse.
DR CTD; 57576; -.
DR MGI; MGI:1098229; Kif17.
DR VEuPathDB; HostDB:ENSMUSG00000028758; -.
DR eggNOG; KOG0239; Eukaryota.
DR GeneTree; ENSGT00940000158776; -.
DR HOGENOM; CLU_001485_22_0_1; -.
DR InParanoid; Q99PW8; -.
DR OMA; KKEAVWD; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; Q99PW8; -.
DR TreeFam; TF105223; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 16559; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Kif17; mouse.
DR PRO; PR:Q99PW8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99PW8; protein.
DR Bgee; ENSMUSG00000028758; Expressed in primary oocyte and 67 other tissues.
DR ExpressionAtlas; Q99PW8; baseline and differential.
DR Genevisible; Q99PW8; MM.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:1990075; C:periciliary membrane compartment; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA: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:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IDA:MGI.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IDA:SynGO.
DR GO; GO:0030030; P:cell projection organization; IBA:GO_Central.
DR GO; GO:0042073; P:intraciliary transport; IC:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA: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 ATP-binding; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1038
FT /note="Kinesin-like protein KIF17"
FT /id="PRO_0000125451"
FT DOMAIN 5..335
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 379..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..470
FT /evidence="ECO:0000255"
FT COILED 748..855
FT /evidence="ECO:0000255"
FT COMPBIAS 535..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 939..1038
FT /note="Missing: Abolishes interaction with APBA1. Abolishes
FT transport of vesicles containing N-methyl-D-aspartate
FT (NMDA) receptor subunit NR2B along microtubules."
FT /evidence="ECO:0000269|PubMed:10846156"
SQ SEQUENCE 1038 AA; 116373 MW; 2BED852A3AFDBD46 CRC64;
MASESVKVVV RCRPMNKRER ELSCQSVVTV DSARGQCFIQ NPGAADEPPK QFTFDGAYYI
EHFTEQIYNE IAYPLVEGVT EGYNGTIFAY GQTGSGKSFT MQGLPDPPCQ RGIIPRAFEH
VFESVQCAEN TKFLVRASYL EIYNEDVHDL LGADTKQRLE LKEHPEKGVY VKGLSMHTVH
NVAQCERVME TGWKNRAVGY TLMNKDSSRS HSIFTINIEI YAVDERGKDH LRAGKLNLVD
LAGSERQSKT GATGERLKEA TKINLSLSAL GNVISALVDG RCKHIPYRDS KLTRLLQDSL
GGNTKTLMVA CLSPADNNYD ETLSTLRYAN RAKNIKNKPR INEDPKDALL REYQEEIKRL
KAILAQQMGP GNLSALLSTQ TPPGPVQSEE KLLSPTTVQQ DTEAEKQLIR EEYEERLARL
KADYEAEQES RVRLQEDITA MRNSYDVKLS TLQENLRKEK ETEAILKAEV LCKTEVMSRA
ELASGPEYSP PLQYETAVKP TILSMPDMPP SGKVTKSQAP LAFEEPHGET SRSEFSFESN
ECSTLEDSAT SEAFPGPEEF SNMEFSMAAA LTESRYLPEE YLGGQEAAAS PLEAERYVQE
NEPSLEPLRI LASLQDPFAE VEAKLARLSS TVAMSDSSQT VVPQIPKQPS SADLLEPSDT
KSEADVAVAD NVVLGTEPDV NLRVAEEVVS EAETGVWMES EAQVAHVAQV SEEAQPQPLL
AMVSVRRESV GVEVAVLTEE ELQPVDQQQV LARLQLLEQQ VVGGEQAKNK DLREKHKRRK
RYADERKKQL VAALQNSDED GGDWVLLNVY DSIQEEVRAK SKLLEKMQRK LRAAEVEIKD
LQSEFQLEKI DYLATIRRQE RDSMLFQQLL EQVQPLIRRD CNYSNLEKIR RESSWDEDNG
FWKIPDPIIL KTSLPVVPTG TQNKPARKTS AVDSGEPHMQ EEDRYKLMLS RSDSENIASN
YFRSKRASQI LSTDPMKSLT YHNSPPGLNS SLSNNSALPP TQTPEMPQPR PFRLESLDIP
FSKAKRKKSK NSFGGEPL
