KIF11_XENTR
ID KIF11_XENTR Reviewed; 1067 AA.
AC B2GU58; D0PPG2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Kinesin-like protein KIF11 {ECO:0000250|UniProtKB:P52732, ECO:0000312|EMBL:AAI66147.1};
DE AltName: Full=Costal2 {ECO:0000250|UniProtKB:P52732, ECO:0000312|EMBL:ABX55790.1};
GN Name=kif11 {ECO:0000312|EMBL:AAI66147.1};
GN Synonyms=cos2 {ECO:0000312|EMBL:ABX55790.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:ABX55790.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Aguero T.H., Fernandez J.P., Vega Lopez G., Aybar M.J.;
RT "Molecular cloning of Xenopus Costal2.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:ABX55790.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAI66147.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plus end-directed motor protein required for establishing a
CC bipolar spindle. Associates with both interphase and mitotic spindle
CC microtubules. May be involved in nuclear divisions taking place during
CC the development of unfertilized eggs. Required in non-mitotic cells for
CC transport of secretory proteins from the Golgi complex to the cell
CC surface. {ECO:0000250|UniProtKB:P52732, ECO:0000250|UniProtKB:Q91783}.
CC -!- SUBUNIT: Heterotetramer of two heavy and two light chains. Interacts
CC with aurka (By similarity). {ECO:0000250|UniProtKB:P28025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28025}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P28025}.
CC Note=Concentrated around the polar ends of both meiotic and mitotic
CC spindles. {ECO:0000250|UniProtKB:P28025}.
CC -!- PTM: Phosphorylation of Thr-937 during mitosis controls the association
CC of this protein with the spindle apparatus. {ECO:0000250}.
CC -!- PTM: A subset of this protein primarily localized at the spindle pole
CC is phosphorylated by NEK6 during mitosis. {ECO:0000250}.
CC -!- PTM: Phosphorylated on a serine residue by aurka.
CC {ECO:0000250|UniProtKB:P28025}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF524557; ABX55790.1; -; mRNA.
DR EMBL; EF524558; ABX55791.1; -; Genomic_DNA.
DR EMBL; BC166147; AAI66147.1; -; mRNA.
DR RefSeq; NP_001016116.2; NM_001016116.3.
DR AlphaFoldDB; B2GU58; -.
DR SMR; B2GU58; -.
DR STRING; 8364.ENSXETP00000026683; -.
DR PaxDb; B2GU58; -.
DR PRIDE; B2GU58; -.
DR GeneID; 548870; -.
DR KEGG; xtr:548870; -.
DR CTD; 3832; -.
DR Xenbase; XB-GENE-978999; kif11.
DR eggNOG; KOG0243; Eukaryota.
DR InParanoid; B2GU58; -.
DR OrthoDB; 179272at2759; -.
DR Reactome; R-XTR-983189; Kinesins.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR025901; Kinesin-assoc_MT-bd_dom.
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 Pfam; PF00225; Kinesin; 1.
DR Pfam; PF13931; Microtub_bind; 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 Phosphoprotein; Reference proteome.
FT CHAIN 1..1067
FT /note="Kinesin-like protein KIF11"
FT /id="PRO_0000399385"
FT DOMAIN 18..359
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1048..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..480
FT /evidence="ECO:0000255"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15066,
FT ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 937
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P28025"
FT MOD_RES 1046
FT /note="Phosphoserine; by NEK6"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1067 AA; 119832 MW; 2CE112F5CC838448 CRC64;
MSSQNSFMSS KKDDKGKNIQ VVVRCRPFNQ LERKASSHSV LECDAPRKEV CVRTGGINDK
LGKKTYTFDM VFGPAAKQID VYRSVVCPIL DEVIMGYNCT VFAYGQTGTG KTFTMEGERS
ADEEFTWEQD PLAGIIPRTL HQIFEKLSEN GTEFSVKVSL LEIYNEELFD LLSPSPDVGE
RLQMFDDPRN KRGVIIKGLE EVSVHNKDEV YHILERGAAR RKTASTLMNA YSSRSHSVFS
VTIHMKETTV DGEELVKIGK LNLVDLAGSE NIGRSGAVDK RAREAGNINQ SLLTLGRVIT
ALVERAPHIP YRESKLTRIL QDSLGGRTKT SIIATVSPAS INLEETVSTL EYANRAKNIM
NKPEVNQKLT KRALIKEYTE EIERLKRDLA TAREKNGVYL SNENYEQLQG KVLSQEEIIT
EYTEKITAME EEIKRINELF AENKKELEEC TTILQCKEKE LEETQKNLHE SKEQLAQEAF
VVTALETTEK KLHGTANKLL TTVRETSKDV SGLHAKLDRK RAVDQHNTQV HENFAEQMDK
RFSVIERSVD EYSVKQQGML DFYTNSIDNL LGASSAALSV TATAVAKSFT SVQETVSEKV
SHSVDEILKQ ETLSSQAKDD LQKLMAAHRT GLEQALRTDL LPVVTAVLNL NSHLSHCLQN
FQAVADKIDS HKEEMNSFFT EHSRSLHRLR LDSGSALSSI QSEYESLKVE IETAQSMHSE
GVNNLIGSLQ NQLNLLAMET QQNFSGFLAK GGKLQKSVGC LQQDLDSISS DAIEHTSSHH
DKFAGQSQDI AVEIRQLAAS NMGTLEESSK QCEKLTGSIN AISRESQHWC ESASQQIDSL
LEEQVCYLRT SKKHLQSLQK DVEVGCGASV VEITEHVNAQ RQAEEKALTS LVEQVRDDKE
MLGEQRLELH EQVQSGQNKV NSYLNEELRN DVPTGTTPQR RDYVYPSLLV RTKPRDVLLE
QFRQQQQEYL ESISSVISEA VEPPVEQDSL EDEPPVAVND SVMSEKSCID LSMVCQENGG
VPFFQQKKAL RKEKENRANT TLLERSKIMD EAEQSLPKSK LPLRMQN
