KI18B_CHICK
ID KI18B_CHICK Reviewed; 797 AA.
AC Q5ZLK6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Kinesin-like protein KIF18B;
GN Name=KIF18B; ORFNames=RCJMB04_5l15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: May play an important role in microtubule plus-end
CC depolymerizing activity in mitotic cells. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000305}.
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; AJ719728; CAG31387.1; -; mRNA.
DR RefSeq; NP_001026099.1; NM_001030928.1.
DR AlphaFoldDB; Q5ZLK6; -.
DR SMR; Q5ZLK6; -.
DR STRING; 9031.ENSGALP00000001290; -.
DR PaxDb; Q5ZLK6; -.
DR PRIDE; Q5ZLK6; -.
DR Ensembl; ENSGALT00000065551; ENSGALP00000055265; ENSGALG00000031553.
DR GeneID; 419968; -.
DR KEGG; gga:419968; -.
DR CTD; 146909; -.
DR VEuPathDB; HostDB:geneid_419968; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000161200; -.
DR HOGENOM; CLU_001485_21_5_1; -.
DR InParanoid; Q5ZLK6; -.
DR OMA; HQEEKRF; -.
DR OrthoDB; 703086at2759; -.
DR PhylomeDB; Q5ZLK6; -.
DR TreeFam; TF105231; -.
DR Reactome; R-GGA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-983189; Kinesins.
DR PRO; PR:Q5ZLK6; -.
DR Proteomes; UP000000539; Chromosome 27.
DR Bgee; ENSGALG00000031553; Expressed in testis and 5 other tissues.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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:0005634; C:nucleus; IBA:GO_Central.
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; 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; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..797
FT /note="Kinesin-like protein KIF18B"
FT /id="PRO_0000318972"
FT DOMAIN 11..352
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 412..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 367..402
FT /evidence="ECO:0000255"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 797 AA; 86582 MW; 198553E6FEFB3E0D CRC64;
MAMGPPPEDG TVAVVVRVRP PTPSERDGAA HPVLHVVDQH ILVFDPEEPG GPPGAALPPR
GPKHRGKDLK FVFDRVFGEG ATQEEVFQHT TREVLDGVLN GYNCSVFAYG ATGAGKTYTM
LGSEQSPGIM YLTMAELYRR IEARRDEKSC EVLVSYQEVY NEQIHDLLEP KGPLAIREDP
EKGVVVQGLS FHQPKSAEQL LEMLANGNKN RTQHPTDANA TSSRSHAVFQ IYVKQQDRVV
GLSQDLQVAK MSLIDLAGSE RASVTNTKGE RLREGANINR SLLALINVIN ALADAKSKKT
HIPYRDSKLT RLLKDSIGGN CRTIMIAAVS PSSLAYEDTY NTLKYANRAK EIKLSLKSNV
LSLDCHISKY ATICEQLKTE VADLQAKLRA YEDAARDAGK QIPALLPPPR MEEAVPESCS
APNVCRESDG EQQELGAGQD AQLGGEEEVL EEMPPSSPSP TQQTDLQLGM KKPNRLPQRL
SRSHTEMLMA TILSVAQKQY SLLKAANLLT PDMVSEFEEL QLLVQKEAAV SPQPTDTSGA
PPALRTQRGC DASPSTLSAE PSVPTTRAAL RRLQQLTALS SPKLVAKKRR RSEMSNTSRL
ETPHSLNTRA KRQRKSSPLS AGGEVEAQRS PHTPCLKEPQ SPPLLPCCTP KICPLTVTKR
RAPLMTSAAQ NCCTPTVCDL NVTYSLSEDV AKPGALSLPR FPGWENAPCA LKKQEGPFVP
RASIPVFSMK GSSIPKPSSI SKGSVQKRRG AVSNASRSLG GIQSHITSSS SRRSAQPQSI
PEHPPPGLTW KGRSGPR
