KIF9_MOUSE
ID KIF9_MOUSE Reviewed; 790 AA.
AC Q9WV04; E9QMT7; O35070;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Kinesin-like protein KIF9;
GN Name=Kif9;
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].
RC STRAIN=B6 X SJ; TISSUE=Hippocampus;
RA Piddini E., Hellias B., Dotti C.G.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 114-253.
RC STRAIN=ICR;
RX PubMed=9275178; DOI=10.1073/pnas.94.18.9654;
RA Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y.,
RA Hirokawa N.;
RT "Identification and classification of 16 new kinesin superfamily (KIF)
RT proteins in mouse genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP AND INTERACTION WITH HYDIN.
RX PubMed=32072696; DOI=10.1096/fj.201902755r;
RA Miyata H., Shimada K., Morohoshi A., Oura S., Matsumura T., Xu Z.,
RA Oyama Y., Ikawa M.;
RT "Testis-enriched kinesin KIF9 is important for progressive motility in
RT mouse spermatozoa.";
RL FASEB J. 34:5389-5400(2020).
CC -!- FUNCTION: Essential for normal male fertility and for progressive
CC motility of spermatozoa. {ECO:0000269|PubMed:32072696}.
CC -!- SUBUNIT: Interacts with HYDIN. {ECO:0000269|PubMed:32072696}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, cilium, flagellum {ECO:0000269|PubMed:32072696}. Cytoplasm,
CC cytoskeleton, flagellum axoneme {ECO:0000305|PubMed:32072696}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis (at protein level)
CC (PubMed:32072696). Weakly expressed in the brain, thymus, lung and
CC heart (PubMed:32072696). {ECO:0000269|PubMed:32072696}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit impaired sperm motility and male
CC subfertility and flagella show an asymmetric waveform pattern, which
CC leads to a circular motion of spermatozoa.
CC {ECO:0000269|PubMed:32072696}.
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; AJ132889; CAB46016.1; -; mRNA.
DR EMBL; AC132103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB001437; BAA22397.1; -; mRNA.
DR CCDS; CCDS23568.1; -.
DR RefSeq; NP_034758.2; NM_010628.3.
DR AlphaFoldDB; Q9WV04; -.
DR SMR; Q9WV04; -.
DR BioGRID; 200950; 3.
DR IntAct; Q9WV04; 1.
DR STRING; 10090.ENSMUSP00000057896; -.
DR iPTMnet; Q9WV04; -.
DR PhosphoSitePlus; Q9WV04; -.
DR MaxQB; Q9WV04; -.
DR PaxDb; Q9WV04; -.
DR PRIDE; Q9WV04; -.
DR ProteomicsDB; 269307; -.
DR Antibodypedia; 12887; 123 antibodies from 21 providers.
DR DNASU; 16578; -.
DR Ensembl; ENSMUST00000084952; ENSMUSP00000082016; ENSMUSG00000032489.
DR GeneID; 16578; -.
DR KEGG; mmu:16578; -.
DR UCSC; uc009rud.2; mouse.
DR CTD; 64147; -.
DR MGI; MGI:1098237; Kif9.
DR VEuPathDB; HostDB:ENSMUSG00000032489; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000158533; -.
DR InParanoid; Q9WV04; -.
DR OrthoDB; 424630at2759; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16578; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9WV04; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9WV04; protein.
DR Bgee; ENSMUSG00000032489; Expressed in spermatid and 88 other tissues.
DR ExpressionAtlas; Q9WV04; baseline and differential.
DR Genevisible; Q9WV04; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0002102; C:podosome; ISO:MGI.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; 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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1903008; P:organelle disassembly; ISO:MGI.
DR GO; GO:1901317; P:regulation of flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0071801; P:regulation of podosome assembly; ISO: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; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Flagellum; Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..790
FT /note="Kinesin-like protein KIF9"
FT /id="PRO_0000125443"
FT DOMAIN 6..340
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 482..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 342..442
FT /evidence="ECO:0000255"
FT COILED 600..695
FT /evidence="ECO:0000255"
FT COMPBIAS 547..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 530
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAQ2"
FT CONFLICT 245..253
FT /note="DLAGSERLS -> KLIDTVDLE (in Ref. 3; BAA22397)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="A -> D (in Ref. 1; CAB46016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 89898 MW; 0E43EFE48342ECE7 CRC64;
MGTRKKVQAF VRVRPTDDFA HEMIKYGEDN KSIDIHLKKD TRRGVVNNQQ TDWSFKLDGV
LHNASQDLVY ETVAKDAVSQ ALDGYNGTIM CYGQTGAGKT YTMTGATENY KHRGILPRAL
QQVFRMIEER PTHAITVRVS YLEIYNENLF DLLSTLPYVG PSVTPMTIVE NPQGIFIKGL
SVHLTSQEED AFSLLFEGET NRIIASHTMN KNSSRSHCIF TIYMEAHSRT LSDEKYITSK
INLVDLAGSE RLSKTGSEGR VLKEATYINK SLSFLEQAII ALGDQNRDHV PFRQSKLTHA
LKDSLGGNCN MVLVTNIYGE AAQLDETLSS LRFASRMKLV TTEPAINEKY DAERMVKNLE
KELALLKQEL AIHDSLSNRT LVNYDPMDEI QIAEINSQVR RYLEGTLDEI DIINLRQIQE
VFNQFRVVLS QQEQEVESAL RRKYTLIDKN DFAAISAVQK VGLMDIEGNL VGEPDGQSFG
LGVAPFSVKP GKKPKTKKTP KDQFSSSARK EGASSPVSGK DFDVASISKT QLIPSSKDGD
LKDMLARERE TSSIEPLISD SPKEELRAPR PSTPPSRTVA FEEFKNERGS EINRIFKENK
SILNERKKRA SETTQRINAI KQEIDETKDA LNFQKSLREK QGEYENKGLM IIDEEEFLLI
LKLKDLKKQY RNEYQELRDL RAEIQYCQRL VDQCRHRLLM EFDIWYNESF MIPEDVQVAL
KLGSSIRPGM VPISRIVCLG EDDQDRFSHL QQTVLPEGLD SITFYNAKVK TDQKHNYMKT
MVGLQQSHRK
