ID   KIF2A_XENLA             Reviewed;         682 AA.
AC   Q91637;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Kinesin-like protein KIF2A;
DE   AltName: Full=Kinesin-related protein xKIF2;
GN   Name=kif2a; Synonyms=kif2;
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], AND SEQUENCE REVISION.
RC   TISSUE=Ovary;
RA   Walczak C.E.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 124-682.
RC   TISSUE=Ovary;
RX   PubMed=8548824; DOI=10.1016/s0092-8674(00)80991-5;
RA   Walczak C.E., Mitchison T.J., Desai A.;
RT   "XKCM1: a Xenopus kinesin-related protein that regulates microtubule
RT   dynamics during mitotic spindle assembly.";
RL   Cell 84:37-47(1996).
RN   [3]
RP   FUNCTION, INTERACTION WITH PLK1 AND AURKA, PHOSPHORYLATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19351716; DOI=10.1242/jcs.044321;
RA   Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.;
RT   "Plk1 and Aurora A regulate the depolymerase activity and the cellular
RT   localization of Kif2a.";
RL   J. Cell Sci. 122:1334-1341(2009).
CC   -!- FUNCTION: Plus end-directed microtubule-dependent motor. May regulate
CC       microtubule dynamics during axonal growth (By similarity). Required for
CC       normal progression through mitosis. Required for normal congress of
CC       chromosomes at the metaphase plate. Required for normal spindle
CC       dynamics during mitosis. Promotes spindle turnover. Implicated in
CC       formation of bipolar mitotic spindles Has microtubule depolymerization
CC       activity. {ECO:0000250, ECO:0000269|PubMed:19351716}.
CC   -!- SUBUNIT: Interacts with aurka and plk1. {ECO:0000269|PubMed:19351716}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:19351716}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000269|PubMed:19351716}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:19351716}. Note=Localized to the spindle
CC       microtubules and spindle poles from prophase to metaphase. Efficient
CC       targeting to spindle microtubules and spindle poles requires the kinase
CC       activity of plk1.
CC   -!- PTM: Phosphorylation by plk1 promotes location at spindle microtubules
CC       and spindle poles, and enhances its microtubule depolymerization
CC       activity. {ECO:0000269|PubMed:19351716}.
CC   -!- PTM: Phosphorylation by AURKA interferes with location at spindle
CC       microtubules and spindle poles, and inhibits its microtubule
CC       depolymerization activity. {ECO:0000269|PubMed:19351716}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC59744.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U36486; AAC59744.2; ALT_INIT; mRNA.
DR   RefSeq; NP_001079931.1; NM_001086462.1.
DR   AlphaFoldDB; Q91637; -.
DR   SMR; Q91637; -.
DR   PRIDE; Q91637; -.
DR   DNASU; 379622; -.
DR   GeneID; 379622; -.
DR   KEGG; xla:379622; -.
DR   CTD; 379622; -.
DR   Xenbase; XB-GENE-951759; kif2a.L.
DR   OrthoDB; 418348at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 379622; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0007052; P:mitotic spindle organization; 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   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..682
FT                   /note="Kinesin-like protein KIF2A"
FT                   /id="PRO_0000125416"
FT   DOMAIN          198..528
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..192
FT                   /note="Globular"
FT                   /evidence="ECO:0000255"
FT   REGION          39..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          638..673
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        97..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         288..295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   682 AA;  77414 MW;  3DA295BB319063F8 CRC64;
     MVTSLNEDSE SITVEWIENG DTKGKEIDLE SIFSLNHDLA PDEEIDPGPE MPPPPAPTTK
     VNKIVKNRRT VAPVKNETPA KDNRVAAVGS ARARPIQPIE QSASRQQNGS VSDISPDQPG
     KKDFGLASRR KSNCVKEVEK LQEKRERRRL QQQELREKKA QDFDATNPNY EIMCMIKDFR
     GSLDYRPLTT SDPIDEHRIC VCVRKRPLNK KETTIKDLDV ITIPIKDVVM VHEPKQKVDL
     TRFLENQTFR FDYAFDETAP NETVYRFTAR PLVETIFERG MATCFAYGQT GSGKTHTMGG
     DFSGKNQDCS KGIYALAARD VFQMLKKPNY KKLELQVYAT FFEIYSGKVF DLLNRKTKLR
     VLEDGKQQVQ VVGLQEREVK CVEDVLKLIE IGNSCRTSGQ TSANAHSSRS HAVFQIILRK
     KGKMHGKFSL IDLAGNERGA DTSSADRQTR LEGAEINKSL LALKECIRAL GRNKPHTPFR
     ASKLTQVLRD SFIGENSRTC MIATISPGMA SCENTLNTLR YANRVKELDP SRCRRPPPHD
     TSCPQTSWMT WKQCGEWGVA PQRDDLKLLC EQNEEEVSPQ LFTFHEAVSQ MVEMEEQVVE
     DHRAVFPGTS IRWLEGLKKC LLEMTEEVDY DADSYATQLE AILEKKIDIL TELRDKVKSF
     RAALQEEEHA SKQINPKRPR AL