KI11A_XENLA
ID KI11A_XENLA Reviewed; 1067 AA.
AC Q91783;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Kinesin-like protein KIF11-A;
DE AltName: Full=Kinesin-5;
DE AltName: Full=Kinesin-related motor protein Eg5-2;
DE Short=XLEg5K2;
GN Name=kif11-a; Synonyms=eg5;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Egg;
RX PubMed=8026619; DOI=10.1006/dbio.1994.1187;
RA Houliston E., le Guellec R., Kress M., Philippe M., le Guellec K.;
RT "The kinesin-related protein Eg5 associates with both interphase and
RT spindle microtubules during Xenopus early development.";
RL Dev. Biol. 164:147-159(1994).
RN [2]
RP FUNCTION.
RX PubMed=15583027; DOI=10.1083/jcb.200407126;
RA Miyamoto D.T., Perlman Z.E., Burbank K.S., Groen A.C., Mitchison T.J.;
RT "The kinesin Eg5 drives poleward microtubule flux in Xenopus laevis egg
RT extract spindles.";
RL J. Cell Biol. 167:813-818(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-1046.
RX PubMed=19001501; DOI=10.1242/jcs.035360;
RA Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C.,
RA Avruch J., Roig J.;
RT "The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site
RT necessary for mitotic spindle formation.";
RL J. Cell Sci. 121:3912-3921(2008).
RN [4]
RP PHOSPHORYLATION AT THR-937, AND MUTAGENESIS OF THR-937.
RX PubMed=19079595; DOI=10.1371/journal.pone.0003936;
RA Cahu J., Olichon A., Hentrich C., Schek H., Drinjakovic J., Zhang C.,
RA Doherty-Kirby A., Lajoie G., Surrey T.;
RT "Phosphorylation by Cdk1 increases the binding of Eg5 to microtubules in
RT vitro and in Xenopus egg extract spindles.";
RL PLoS ONE 3:E3936-E3936(2008).
CC -!- FUNCTION: Plus end-directed motor protein required for establishing a
CC bipolar spindle (PubMed:15583027). Associates with both interphase and
CC spindle microtubules (PubMed:15583027). May be involved in nuclear
CC divisions taking place during the development of unfertilized eggs
CC (PubMed:15583027). Required in non-mitotic cells for transport of
CC secretory proteins from the Golgi complex to the cell surface (By
CC similarity). {ECO:0000250|UniProtKB:P52732,
CC ECO:0000269|PubMed:15583027}.
CC -!- SUBUNIT: Heterotetramer of two heavy and two light chains. Interacts
CC with aurka (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle pole.
CC Note=Concentrated around the polar ends of both meiotic and mitotic
CC spindles.
CC -!- TISSUE SPECIFICITY: Highly expressed in unfertilized eggs, especially
CC in the germinal vesicle and in the radial yolk-poor channels. Also
CC present in testis.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Accumulates during the
CC latter stages of oogenesis and levels increase three-fold during oocyte
CC maturation. Levels decrease after fertilization.
CC {ECO:0000269|PubMed:8026619}.
CC -!- PTM: Phosphorylation of Thr-937 during mitosis controls the association
CC of this protein with the spindle apparatus.
CC {ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:19079595}.
CC -!- PTM: A subset of this protein primarily localized at the spindle pole
CC is phosphorylated by NEK6 during mitosis.
CC -!- PTM: Phosphorylated on a serine residue by aurka. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; X71864; CAA50695.1; -; mRNA.
DR PIR; I51616; S33417.
DR AlphaFoldDB; Q91783; -.
DR SMR; Q91783; -.
DR iPTMnet; Q91783; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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 1: Evidence at protein 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-A"
FT /id="PRO_0000125374"
FT DOMAIN 18..359
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 365..480
FT /evidence="ECO:0000255"
FT COILED 692..721
FT /evidence="ECO:0000255"
FT COILED 882..915
FT /evidence="ECO:0000255"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 937
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:19079595"
FT MOD_RES 1046
FT /note="Phosphoserine; by NEK6"
FT /evidence="ECO:0000269|PubMed:19001501"
FT MUTAGEN 937
FT /note="T->A: Disrupts spindle binding."
FT /evidence="ECO:0000269|PubMed:19079595"
SQ SEQUENCE 1067 AA; 119885 MW; 48A477D1E2559115 CRC64;
MSSQNSFMSS KKDDKGKNIQ VVVRCRPFNQ LERKASSHSV LECESQRKEV CVRTGEVNDK
LGKKTYTFDM VFGPAAKQID VYRSVVCPIL DEVIMGYNCT IFAYGQTGTG KTFTMEGERS
SDEEFTWEQD PLAGIIPRTL HQIFEKLSEI GTEFSVKVSL LEIYNEELFD LLSPSPDVGE
RLQMFDDPRN KRGVIIKGLE EISVHNKDEV YQILERGAAK RKTASTLMNA YSSRSHSVFS
VTIHMKETTI DGEELVKIGK LNLVDLAGSE NIGRSGAVDK RAREAGNINQ SLLTLGRVIT
ALVERAPHIP YRESKLTRIL QDSLGGRTKT SIIATVSPAS INLEETMSTL DYASRAKNIM
NKPEVNQKLT KKALIKEYTE EIERLKRELA TAREKNGVYL SNENYEQLQG KVLSQEEMIT
EYSEKIAAME EEIKRIGELF ADNKKELEEC TTILQCKEKE LEATQNNLQE SKEQLAQEAF
VVSAMETTEK KLHGTANKLL STVRETTRDV SGLHEKLDRK RAVEQHNSQV HENFAEQINR
RFSVIQQTVD EYSVKQQGML DFYTNSIDDL LGASSSALSA TATAVAKSFA SVQETVSKQV
SHSVEEILKQ ETLSSQAKDD LQKLMTAHRT GLEQALRTDL LPVVTAVLDL NSHLSHCLQS
FLGVADKIDS HKEDMNSFFT EHSRSLHKLR LDSSSALSSI QSEYESLKEE IATAQSTHSE
GVNNLISSLQ NQLNLLAMET RQQFSGFLSK GGKLQESVGC LQQDLDLVSS DAIECISSHH
SKFTEQSQAV TVEIRQLAGS NMSTLEESSK QCEKLTNSIN TICQESQQWC ESAGQKMDSL
LEEQVCYLHS SKKQIQTLHK DVEDGCGSSV VEITDRVNVQ CQAQEKALTS LVEQVKDDKE
MLGEQRLELN EQVQSGLNKV HVYLKEELRN DVPTGTTPQR RDYVYPSLLI KTKPRDVLLE
QFRQQQQEYL ESICSVISEA VEPPVEQDSL EDEPPVAVND SVISEKSCID LSMTCQEKGG
VPFFQQKKAL RKEKENRGNA TLLERSKIMD EVEQSLPKSK LPLRMQN
