KI18B_RAT
ID KI18B_RAT Reviewed; 826 AA.
AC Q4KLL9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Kinesin-like protein KIF18B;
GN Name=Kif18b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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: In complex with KIF2C, constitutes the major microtubule
CC plus-end depolymerizing activity in mitotic cells. Its major role may
CC be to transport KIF2C and/or MAPRE1 along microtubules (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAPRE1; this interaction is required for
CC efficient accumulation at microtubule plus ends. Interacts with KIF2C
CC at microtubule tips; this interaction increases the affinity of both
CC partners for microtubule plus ends and is required for robust
CC microtubule depolymerization. KIF2C phosphorylation by AURKA or AURKB
CC strongly reduces KIF18B-binding. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000305}. Note=Present predominantly in
CC the nucleus and to a lesser extent in the cytoplasm of interphase
CC cells. During mitosis, found to be closely associated with astral
CC microtubule plus ends emanating from the spindle pole during
CC prometaphase and metaphase (By similarity). {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; BC099126; AAH99126.1; -; mRNA.
DR RefSeq; NP_001034108.1; NM_001039019.1.
DR RefSeq; XP_006247567.1; XM_006247505.3.
DR AlphaFoldDB; Q4KLL9; -.
DR SMR; Q4KLL9; -.
DR STRING; 10116.ENSRNOP00000034491; -.
DR PhosphoSitePlus; Q4KLL9; -.
DR PaxDb; Q4KLL9; -.
DR PRIDE; Q4KLL9; -.
DR Ensembl; ENSRNOT00000032339; ENSRNOP00000034491; ENSRNOG00000021713.
DR GeneID; 303575; -.
DR KEGG; rno:303575; -.
DR CTD; 146909; -.
DR RGD; 1310360; Kif18b.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000161200; -.
DR InParanoid; Q4KLL9; -.
DR OMA; HQEEKRF; -.
DR OrthoDB; 703086at2759; -.
DR PhylomeDB; Q4KLL9; -.
DR TreeFam; TF105231; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:Q4KLL9; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000021713; Expressed in testis and 15 other tissues.
DR ExpressionAtlas; Q4KLL9; baseline and differential.
DR Genevisible; Q4KLL9; RN.
DR GO; GO:0000235; C:astral microtubule; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; ISO:RGD.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; 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:0003774; F:cytoskeletal motor activity; ISO:RGD.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007019; P:microtubule depolymerization; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
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 cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..826
FT /note="Kinesin-like protein KIF18B"
FT /id="PRO_0000318971"
FT DOMAIN 9..353
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 396..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..403
FT /evidence="ECO:0000255"
FT MOTIF 618..626
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 396..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 668
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
SQ SEQUENCE 826 AA; 91195 MW; 0CD86CDECC8C59DA CRC64;
MVMAVEDSVV RVVVRVRPPT PKELESQRRP VIQVVDERML VFDPEECDGG FPGLKWSGSL
SGPKKKGKDL TFVFDRVFSE VATQQDVFQH TTHNILDSFL QGYNCSVFAY GATGAGKTHT
MLGREGDPGI MYLTTMELYR RLEACQEEKQ FEVLISYLEV YNEQIYDLLE PKGPLTIRED
PDKGVVVPGL SFHQPASAQQ LLEMLTRGNC SRTQHPTDAN ATSSRSHAIF QIFVKQQDRV
PGLTQALRVA KMSLIDLAGS ERASSTHAKG ERLREGANIN RSLLALINVL NALADAKGRK
SHVPYRDSKL TRLLKDSIGG NCRTVMIAAV SPSSLTYEDT YNTLKYADRA KEIRLTLKSN
VISLDHHISQ YATICQQLQA EVAALREKLQ TYEAGAQALQ QRSPQPPKLS IPQNLSSSPL
QPGHSSQSCA PEFHAKYDAP QEESLGTDSQ GQGTVEENAP EQEQPPQDKQ FPTQMPEPNL
PGSPCPTVQA KQGMNQHSLQ RLDAEHSKQL ALRVLRLAQR QYSLLQAANL LTPDMISEFE
TLQQLVLEES MEHGAESPRS PGLARGIPLA QELCSESKSS RYCGPVTRTM AKQLSGLTHT
LGIPLAPDCT SDKTSQKPTK EKKRKLNLEE PGSLPAPSVE MKRQRQSFLP CLRRGSLPKI
QPSSEPRTPK GERASSPSPS SRVCPATVIK SRVPLGPSAL QNCSTPLTLP TRDLNTTFNV
SEESPSKPSF PEPIDWEKVS PELNGTDQPF LPSAPVFIFT TKGRKPSLPT TTASKKRRTV
RPSVSRGRSC IARLPSSTLK KPDRPFTVPD PPLSLHCLDD HQVIRD
