ID   KI18A_MOUSE             Reviewed;         886 AA.
AC   Q91WD7; Q3TP77; Q8BLL1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Kinesin-like protein KIF18A;
GN   Name=Kif18a;
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].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Stomach;
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 MRNA].
RC   TISSUE=Eye;
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).
CC   -!- FUNCTION: Microtubule-depolymerizing kinesin which plays a role in
CC       chromosome congression by reducing the amplitude of preanaphase
CC       oscillations and slowing poleward movement during anaphase, thus
CC       suppressing chromosome movements. May stabilize the CENPE-BUB1B complex
CC       at the kinetochores during early mitosis and maintains CENPE levels at
CC       kinetochores during chromosome congression (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CENPE and ESR1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, ruffle {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250}.
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; AK044795; BAC32095.2; -; mRNA.
DR   EMBL; AK164649; BAE37860.1; -; mRNA.
DR   EMBL; BC016095; AAH16095.1; -; mRNA.
DR   CCDS; CCDS16507.1; -.
DR   RefSeq; NP_647464.1; NM_139303.1.
DR   AlphaFoldDB; Q91WD7; -.
DR   SMR; Q91WD7; -.
DR   BioGRID; 230733; 11.
DR   IntAct; Q91WD7; 8.
DR   STRING; 10090.ENSMUSP00000028527; -.
DR   iPTMnet; Q91WD7; -.
DR   PhosphoSitePlus; Q91WD7; -.
DR   EPD; Q91WD7; -.
DR   MaxQB; Q91WD7; -.
DR   PaxDb; 10090-ENSMUSP00000028527; -.
DR   PeptideAtlas; Q91WD7; -.
DR   ProteomicsDB; 269215; -.
DR   Antibodypedia; 25467; 168 antibodies from 26 providers.
DR   DNASU; 228421; -.
DR   Ensembl; ENSMUST00000028527.8; ENSMUSP00000028527.8; ENSMUSG00000027115.15.
DR   GeneID; 228421; -.
DR   KEGG; mmu:228421; -.
DR   UCSC; uc008lmb.1; mouse.
DR   AGR; MGI:2446977; -.
DR   CTD; 81930; -.
DR   MGI; MGI:2446977; Kif18a.
DR   VEuPathDB; HostDB:ENSMUSG00000027115; -.
DR   eggNOG; KOG0242; Eukaryota.
DR   GeneTree; ENSGT00940000159058; -.
DR   HOGENOM; CLU_001485_21_5_1; -.
DR   InParanoid; Q91WD7; -.
DR   OMA; HPQKSAL; -.
DR   OrthoDB; 239968at2759; -.
DR   PhylomeDB; Q91WD7; -.
DR   TreeFam; TF105231; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-MMU-983189; Kinesins.
DR   BioGRID-ORCS; 228421; 13 hits in 77 CRISPR screens.
DR   ChiTaRS; Kif18a; mouse.
DR   PRO; PR:Q91WD7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q91WD7; Protein.
DR   Bgee; ENSMUSG00000027115; Expressed in animal zygote and 173 other cell types or tissues.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IDA:MGI.
DR   GO; GO:0005828; C:kinetochore microtubule; ISS:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR   GO; GO:0061673; C:mitotic spindle astral microtubule; IBA:GO_Central.
DR   GO; GO:1990023; C:mitotic spindle midzone; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; ISS:UniProtKB.
DR   GO; GO:0070463; F:tubulin-dependent ATPase activity; ISS:UniProtKB.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR   GO; GO:0007140; P:male meiotic nuclear division; IMP:MGI.
DR   GO; GO:0007019; P:microtubule depolymerization; ISS:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; IMP:MGI.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:MGI.
DR   GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR   CDD; cd01370; KISc_KIP3_like; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF13; 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; Q91WD7; MM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Glycoprotein; Isopeptide bond; Microtubule; Motor protein;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation.
FT   CHAIN           1..886
FT                   /note="Kinesin-like protein KIF18A"
FT                   /id="PRO_0000125459"
FT   DOMAIN          11..355
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          774..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          370..404
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        776..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         113..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         674
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT   MOD_RES         695
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT   MOD_RES         826
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT   CROSSLNK        24
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT   CROSSLNK        683
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT   CROSSLNK        782
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT   CROSSLNK        862
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NI77"
SQ   SEQUENCE   886 AA;  100935 MW;  F611802A899AF0E1 CRC64;
     MSGTEEDLCH RMKVVVRVRP ENTKEKAVQF CKVVHVVDKH ILSFDPKQEE ISFFHRKKTT
     NFDITKRQNK DLKFVFDAVF DETSTQMEVF EHTTKPILHS FLNGYNCTVF AYGATGSGKT
     HTMLGSAAEP GVMYLTMLDL FKCIDEIKEE KECSTAVSYL EVYNEQIRDL LTNSGPLAVR
     EDSQKGVVVQ GLTLHQPKSS EEILQLLDNG NKNRTQHPTD VNAVSSRSHA VFQIYLRQQD
     KTASINQNVR IAKMSLIDLA GSERASVSGA KGSRFVEGTN INKSLLALGN VINALANTKR
     RNQHIPYRNS KLTRLLKDSL GGNCQTIMIA AVSPSSLFYD DTYNTLKYAN RAKEIKSSLK
     SNVLNLNSHI SQYVKICNMQ KAEILMLKEK LKAYEEQKAL SDRNDCAKLV HSNPEDRETE
     RFQEILNCLF QNREGIRQEY LKLEMLLKAN ALKSSYHQQC HKQIEMMCSE DKVEKATCKR
     DHRLEKLKTN SCFLEKKKEE VSKQFDENTN WLHRVENEMR LLGQNGDIPE ALNKELHCHH
     LHLQNKELKT QMAHMTALAC LQEQQHKQTE AVLNALLPVL RKQYWKLKET GLSNAAFDSD
     FKDIEHLVER KKVVAWADQT NEHSNRNDLP GISLLMTFPQ LEPIQSISCC TSVSDPNVLK
     LTPQRRTRRK IIPSPLKVQH TQKSALSEST QLNDSFSKEL QPIVYTPEDC KKAQDLFPSL
     TRTSSQSANV MNDNSQKALC RIESPLSRTE CKQGLYSTST LCDSIRGLKN KWPEQEPLAS
     SKSSVHRIES SSFSTKDSMP ESAGVPSYMA MTTAAKRKWK QMSSTSNASI KSDESCGFAK
     RIRRDNSSVK PMQENRLKVG YKRNTNKTNS NMLRKFRRNT SKENVQ
//