KIF2A_PONAB
ID KIF2A_PONAB Reviewed; 744 AA.
AC Q5R9Y9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Kinesin-like protein KIF2A;
GN Name=KIF2A {ECO:0000250|UniProtKB:O00139};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH91421.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAH91421.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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|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 -!- 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; CR859241; CAH91421.1; -; mRNA.
DR RefSeq; NP_001127415.1; NM_001133943.1.
DR AlphaFoldDB; Q5R9Y9; -.
DR SMR; Q5R9Y9; -.
DR STRING; 9601.ENSPPYP00000017314; -.
DR Ensembl; ENSPPYT00000034450; ENSPPYP00000042085; ENSPPYG00000015496.
DR GeneID; 100174485; -.
DR KEGG; pon:100174485; -.
DR CTD; 3796; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000155570; -.
DR InParanoid; Q5R9Y9; -.
DR OrthoDB; 418348at2759; -.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0120103; C:centriolar subdistal appendage; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005876; C:spindle microtubule; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
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..744
FT /note="Kinesin-like protein KIF2A"
FT /id="PRO_0000306272"
FT DOMAIN 223..553
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 66..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 154..187
FT /evidence="ECO:0000255"
FT COILED 698..737
FT /evidence="ECO:0000255"
FT COMPBIAS 120..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313..320
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:0000250|UniProtKB:O00139"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28740"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
SQ SEQUENCE 744 AA; 84099 MW; E4542A52066F7C0F CRC64;
MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF
SLNPDLVPDE EIEPSPETPP PPASSAKVNK IVKNRRTVAS IKNDPPPRDN RVVGSARARP
SQFPEQSSSA QQNGSVSDIS PVQAAKKEFG PPSRRKSNCV KEVEKLQEKR EKRRLQQQEL
REKRAQDVDA TNPNYEIMCM IRDFRGSLDY RPLTTADPID EHRICVCVRK RPLNKKETQM
KDLDVITIPS KDVVMVHEPK QKVDLTRYLE NQTFRFDYAF DDSAPNEMVY RFTARPLVET
IFERGMATCF AYGQTGSGKT HTMGGDFSGK NQDCSKGIYA LAARDVFLML KKPNYKKLEL
QVYATFFEIY SGKVFDLLNR KTKLRVLEDG KQQVQVVGLQ EREVKCVEDV LKLIDIGNSC
RTSGQTSANA HSSRSHAVFQ IILRRKGKLH GKFSLIDLAG NERGADTSSA DRQTRLEGAE
INKSLLALKE CIRALGRNKP HTPFRASKLT QVLRDSFIGE NSRTCMIATI SPGMASCENT
LNTLRYANRV KEFGISPSDI PFSQGSGSRP DLSPSYEYDD FSPSVTRVKE LTVDPTAAGD
VRPIMHHPPN QIDDLETQWG VGSSPQRDDL KLLCEQNEEE VSPQLFTFHE AVSQMVEMEE
QVVEDHRAVF QESIRWLEDE KALLEMTEEV DYDVDSYATQ LEAILEQKID ILTELRDKVK
SFRAALQEEE QASKQINPKR PRAL
