KIF24_MOUSE
ID KIF24_MOUSE Reviewed; 1356 AA.
AC Q6NWW5; A2BGK6; Q8BUI2; Q99PT7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Kinesin-like protein KIF24;
GN Name=Kif24;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-450, AND TISSUE SPECIFICITY.
RX PubMed=11416179; DOI=10.1073/pnas.111145398;
RA Miki H., Setou M., Kaneshiro K.;
RT "All kinesin superfamily protein, KIF, genes in mouse and human.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7004-7011(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-640; SER-817 AND
RP SER-820, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, 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).
CC -!- FUNCTION: Microtubule-dependent motor protein that acts as a negative
CC regulator of ciliogenesis by mediating recruitment of CCP110 to mother
CC centriole in cycling cells, leading to restrict nucleation of cilia at
CC centrioles. Mediates depolymerization of microtubules of centriolar
CC origin, possibly to suppress aberrant cilia formation. Following
CC activation by NEK2 involved in disassembly of primary cilium during
CC G2/M phase but does not disassemble fully formed ciliary axonemes. As
CC cilium assembly and disassembly is proposed to coexist in a dynamic
CC equilibrium may suppress nascent cilium assembly and, potentially,
CC ciliar re-assembly in cells that have already disassembled their cilia
CC ensuring the completion of cilium removal in the later stages of the
CC cell cycle (By similarity). Plays an important role in recruiting
CC MPHOSPH9, a negative regulator of cilia formation to the distal end of
CC mother centriole (By similarity). {ECO:0000250|UniProtKB:Q5T7B8}.
CC -!- SUBUNIT: Interacts with CCP110, CEP97, TALPID3 (By similarity).
CC Interacts with MPHOSPH9 (By similarity).
CC {ECO:0000250|UniProtKB:Q5T7B8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q5T7B8}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q5T7B8}. Note=Primarily localizes to the mother
CC centriole/basal body and is either absent at daughter centriole.
CC {ECO:0000250|UniProtKB:Q5T7B8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NWW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NWW5-2; Sequence=VSP_023214;
CC -!- TISSUE SPECIFICITY: Expressed in brain, spinal cord, and small
CC intestine. {ECO:0000269|PubMed:11416179}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH67395.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC39323.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK084967; BAC39323.1; ALT_SEQ; mRNA.
DR EMBL; AL807823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX470237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067395; AAH67395.1; ALT_INIT; mRNA.
DR EMBL; AB054028; BAB32492.1; -; Genomic_DNA.
DR CCDS; CCDS18060.2; -. [Q6NWW5-1]
DR RefSeq; NP_077203.2; NM_024241.2. [Q6NWW5-1]
DR RefSeq; XP_006537612.1; XM_006537549.3. [Q6NWW5-1]
DR RefSeq; XP_011248205.1; XM_011249903.2.
DR AlphaFoldDB; Q6NWW5; -.
DR SMR; Q6NWW5; -.
DR STRING; 10090.ENSMUSP00000103690; -.
DR iPTMnet; Q6NWW5; -.
DR PhosphoSitePlus; Q6NWW5; -.
DR PaxDb; Q6NWW5; -.
DR PeptideAtlas; Q6NWW5; -.
DR PRIDE; Q6NWW5; -.
DR ProteomicsDB; 263531; -. [Q6NWW5-1]
DR ProteomicsDB; 263532; -. [Q6NWW5-2]
DR Antibodypedia; 11186; 113 antibodies from 18 providers.
DR Ensembl; ENSMUST00000030148; ENSMUSP00000030148; ENSMUSG00000028438. [Q6NWW5-2]
DR Ensembl; ENSMUST00000108055; ENSMUSP00000103690; ENSMUSG00000028438. [Q6NWW5-1]
DR GeneID; 109242; -.
DR KEGG; mmu:109242; -.
DR UCSC; uc008sio.1; mouse. [Q6NWW5-1]
DR UCSC; uc012dcb.1; mouse. [Q6NWW5-2]
DR CTD; 347240; -.
DR MGI; MGI:1918345; Kif24.
DR VEuPathDB; HostDB:ENSMUSG00000028438; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000154046; -.
DR HOGENOM; CLU_007560_0_0_1; -.
DR InParanoid; Q6NWW5; -.
DR OMA; NLFVWIS; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q6NWW5; -.
DR TreeFam; TF336001; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 109242; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Kif24; mouse.
DR PRO; PR:Q6NWW5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6NWW5; protein.
DR Bgee; ENSMUSG00000028438; Expressed in morula and 147 other tissues.
DR ExpressionAtlas; Q6NWW5; baseline and differential.
DR Genevisible; Q6NWW5; MM.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
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 InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1356
FT /note="Kinesin-like protein KIF24"
FT /id="PRO_0000278249"
FT DOMAIN 1..64
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 218..541
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 93..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..702
FT /note="Interaction with MPHOSPH9"
FT /evidence="ECO:0000250|UniProtKB:Q5T7B8"
FT REGION 552..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 308..315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T7B8"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T7B8"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 615
FT /note="Phosphothreonine; by NEK2"
FT /evidence="ECO:0000250|UniProtKB:Q5T7B8"
FT MOD_RES 616
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000250|UniProtKB:Q5T7B8"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T7B8"
FT VAR_SEQ 265..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023214"
FT CONFLICT 413
FT /note="A -> T (in Ref. 1; BAC39323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1356 AA; 150207 MW; CA1009620C23BF43 CRC64;
MASWLYECLC EAELAQYYPH FTALGLQKID ELAKVTMKDY SRLGVHDMND RKRLFQLIKI
IKIMQEEDKA LGIPEHPLQA SSLYTKPREF RSGPRRQLHF DSPSASKDKM ANNETGSLSN
FSVDEQKSTY LKVLEHMLPD DSQCQTKIRA PDASAADASM QTETNAPLFS SNYFSPQLGN
CDIPVIQRVS HVSGYNYGIP HSCVRQITSE NPWTEMEKIR VCVRKRPLGV REVRRGEVNV
ITVEDKETLL VHEKKEAVDL TQYILQHVFY FDEVFGEACS NQDVYLKTAH PLIQHIFNGG
SATCFAYGQT GAGKTYTMIG THQNPGLYAL AAKDIFRQLK VSQSRRNLFV WISFYEIYCG
QLYDLLNRRK RLFAREDSKH VVQIAGLREL QVDSVELLLQ VILKGSKERS TGATGVNADS
SRSHAIIQIQ IKDSAKRTFG RISFIDLAGS ERAADARDSD RQTKMEGAEI NQSLLALKEC
IRALDQEHTH TPFRQSKLTQ VLKDSFIGNA KTCMIANISP SHIATEHTLN TLRYADRVKE
LKKGVKCCAS ATSQNQTSAN ASPKRIQSSP VTLPGDKCSP KKVKLGLQQS LTVAPGPTKV
KAHPLASHVP NVPFTSGPKT PGKKSSSRGS PTPEWDMKAS PRKGTTRSGH SIKKGAESAP
LCSEKSQIGS KIAVGWEGRA SDPGEGLLRV RLPTRGKKVQ PVQPVQKQLL SRPRLLANSH
HLEATQDSKV GTPAGLAPEA WTNPILQQKE REEHLRFYHQ QFQQPPLLKQ KLNYQPLQRL
LCQHRPSEGR LQSETGFPLH SNPENRDGAQ AEDLDDSDFS EDSFSHGSSQ PAMKQGSTAL
ERSGSSFFLH QDREHSPEEQ AAERQQCLLF SSETDGSKKR PADSWVYSRD PIISHRRGAL
SQSHSPSMVC PDWSKEEDSA SSGPSPKDNR AQKPSSSQVD FVHHQKPGEA QVSDIRLEAF
TSEVPEQAEG SLSSPSPENG LSFPLSHVAV SGSPDQRDRV CTPLREVSEN RVTHTPGRVN
SSTPFQEDSG EQIQMCSANA SGLMAPLTMS LLETPCHEDL SSLEQIAQDG AGYGFMAEIV
GGPAAGHTVP SYDQEAALPV SSATECLWLS SSPPDNRPSG DLPALSPSPI HQHSPDKLPG
REAYQTRRPI LLPENHMGSK LYDDRAEETE LGGSLTFPRK PSSNIHAGVP YSTPFLTSCT
GSSNGVGRPW AQERKHPTGV SCQELVSSTD SNKPHYNEDI AWLRHRPISR CLDSDSPVVP
SCSSKALRTY CPLTPEQAQQ VIIRAHKEQL DEMAELDLKE ETLMTQMDSN DFEDFVTQLD
EIMALKSRCI QSLRSQLQLY LTSHRPAAAP ERTVVS
