KIF2A_BOVIN
ID KIF2A_BOVIN Reviewed; 660 AA.
AC Q2NL05;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Kinesin-like protein KIF2A;
GN Name=KIF2A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Note=Localized to the spindle microtubules and
CC spindle poles from prophase to metaphase. Efficient targeting to
CC spindle microtubules and spindle poles requires the kinase activity of
CC PLK1. Recruited to mitotic spindles by interaction with PSRC1 (By
CC similarity). {ECO:0000250}.
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; BC111267; AAI11268.1; -; mRNA.
DR RefSeq; NP_001070541.1; NM_001077073.1.
DR AlphaFoldDB; Q2NL05; -.
DR SMR; Q2NL05; -.
DR STRING; 9913.ENSBTAP00000055986; -.
DR PRIDE; Q2NL05; -.
DR GeneID; 768014; -.
DR KEGG; bta:768014; -.
DR CTD; 3796; -.
DR eggNOG; KOG0246; Eukaryota.
DR InParanoid; Q2NL05; -.
DR OrthoDB; 418348at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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; IEA:InterPro.
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 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 Acetylation; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW Microtubule; Mitosis; Motor protein; Neurogenesis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..660
FT /note="Kinesin-like protein KIF2A"
FT /id="PRO_0000253714"
FT DOMAIN 177..507
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..171
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 614..653
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28740"
SQ SEQUENCE 660 AA; 74994 MW; 4D0143CDFF51361E CRC64;
MVTSLNEDNE SVTVEWIENG DTKGKEIDLE SIFSLNPDLV PDEDIEPSPE TPPPPTSSAK
VNKIVKNRRT VASIKNEPPP RDNRVVGSAR ARPSQLPEQS SSAQQNARRK SNCVKEVEKL
QEKREKRRLQ QQELREKRAQ DVDATNPNYE IMCMIRDFRG SLDYRPLTTA DPIDEHRICV
CVRKRPLNKK ETQMKDLDVI TIPSKDVVMV HEPKQKVDLT RYLENQTFRF DYAFDDSAPN
EMVYRFTARP LVETIFERGM ATCFAYGQTG SGKTHTMGGD FSGKNQDCSK GIYALAARDV
FLMLKKPNYK KLELQVNATF FEIYSGKVFD LLNRKTKLRV LEDGKQQVQV VGLQEREVKC
VEDVLKLIDI GNSCRTSGQT SANAHSSRSH AVFQIILRRK GKLHGKFSLI DLAGNERGAD
TSSADRQTRL EGAEINKSLL AHKECIRALG RNKPHTPFRA SKLTQVLRDS FIGENSRTCM
IATISPGMAS CENTLNTLRY ANRVKELTVD PTAAGDVRPI MHHPPNQIDD LEAQWGVGSS
PQRDDLKLLC EQNEEEVSPQ LFTFHEAVSQ MVEMEEQVVE DHRAVFQESI RWLEDEKALL
EMTEEVDYDV DSYATQLEAI LEQKIDILTE LRDKVKSFRA ALQEEEQASK QINPKRPRAL
