KIF2A_RAT
ID KIF2A_RAT Reviewed; 705 AA.
AC Q9WV63; Q5BJW1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Kinesin-like protein KIF2A;
DE AltName: Full=Kinesin-2;
GN Name=Kif2a {ECO:0000250|UniProtKB:O00139};
GN Synonyms=Kif2 {ECO:0000312|RGD:70974};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD39241.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 497-705 (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAD39241.1};
RA Gould R.M., Freund C.M., Hawkins G.A.;
RT "Rat kinesin probes to use for Northern blot analysis.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH91304.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 502-705 (ISOFORM 1).
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH91304.1};
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-572 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plus end-directed microtubule-dependent motor required for
CC normal brain development. May regulate microtubule dynamics during
CC axonal growth. Required for normal progression through mitosis.
CC Required for normal congress of chromosomes at the metaphase plate.
CC Required for normal spindle dynamics during mitosis. Promotes spindle
CC turnover. Implicated in formation of bipolar mitotic spindles. Has
CC microtubule depolymerization activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AURKA, PSRC1 and PLK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28740}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P28740}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Note=Localized to the spindle microtubules and spindle poles from
CC prophase to metaphase. Efficient targeting to spindle microtubules and
CC spindle poles requires the kinase activity of PLK1. Recruited to
CC mitotic spindles by interaction with PSRC1 (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=Q9WV63-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.2};
CC IsoId=Q9WV63-2; Sequence=VSP_052553;
CC -!- MISCELLANEOUS: [Isoform 1]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AC105687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF155824; AAD39241.1; -; mRNA.
DR EMBL; BC091304; AAH91304.1; -; mRNA.
DR AlphaFoldDB; Q9WV63; -.
DR SMR; Q9WV63; -.
DR IntAct; Q9WV63; 2.
DR MINT; Q9WV63; -.
DR STRING; 10116.ENSRNOP00000019225; -.
DR iPTMnet; Q9WV63; -.
DR PhosphoSitePlus; Q9WV63; -.
DR jPOST; Q9WV63; -.
DR PRIDE; Q9WV63; -.
DR RGD; 70974; Kif2a.
DR eggNOG; KOG0246; Eukaryota.
DR InParanoid; Q9WV63; -.
DR PhylomeDB; Q9WV63; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:Q9WV63; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:RGD.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0097228; C:sperm principal piece; ISO:RGD.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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; ISO:RGD.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
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 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Microtubule; Mitosis; Motor protein; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..705
FT /note="Kinesin-like protein KIF2A"
FT /id="PRO_0000306273"
FT DOMAIN 222..552
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 65..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..186
FT /evidence="ECO:0000255"
FT COILED 659..698
FT /evidence="ECO:0000255"
FT COMPBIAS 119..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 312..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28740"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT VAR_SEQ 551
FT /note="E -> EFGISPSDIPFSQGSGSRPDLSPSYDYDDFSPSITRVKE (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_052553"
FT MOD_RES Q9WV63-2:572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 705 AA; 79792 MW; 7B6A50DB6B27B6DA CRC64;
MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF
SLNPDLVPDE DIEPSPEIPP PSSSSKVNKI VKNRRTVASI KNDPPPRDNR VVGSARARPS
QLPEQSSSAQ QNGSVSDISP VQAAKKEFGP PSRRKSNCVK EVEKLQEKRE KRRLQQQELR
EKRAQDVDAT NPNYEIMCMI RDFRGSLDYR PLTTADPIDE HRICVCVRKR PLNKKETQMK
DLDVITIPSK DVVMVHEPKQ KVDLTRYLEN QTFRFDYAFD DSAPNEMVYR FTARPLVETI
FERGMATCFA YGQTGSGKTH TMGGDCSGKN QDCSKGIYAL AARDVFLMLK KPNYKKLELQ
VYATFFEIYS GKVFDLLNRK TKLRVLEDGK QQVQVVGLQE REVKCVEDVL KLIDIGNSCR
TSGQTSANAH SSRSHAVFQI ILRRKGKLHG KFSLIDLAGN ERGADTSSAD RQTRLEGAEI
NKSLLALKEC IRALGRNKPH TPFRASKLTQ VLRDSFIGEN SRTCMIATIS PGMASCENTL
NTLRYANRVK ELTVDPTAAG DVRPIMHHPP SQIDDLETQW GVGSSPQRDD LKLLCEQNEE
EVSPQLFTFH EAVSQMVEME EQVVEDHRAV FQESIRWIED EKALLEMTEE VDYDVDSYAT
QLEAILEQKI DILTELRDKV KSFRAALQEE EQASKQINPK RPRAL
