KIF2C_MACFA
ID KIF2C_MACFA Reviewed; 671 AA.
AC Q95LP1;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Kinesin-like protein KIF2C;
DE AltName: Full=Mitotic centromere-associated kinesin;
DE Short=MCAK;
GN Name=KIF2C; ORFNames=QtsA-16015;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
CC -!- FUNCTION: In complex with KIF18B, constitutes the major microtubule
CC plus-end depolymerizing activity in mitotic cells. Regulates the
CC turnover of microtubules at the kinetochore and functions in chromosome
CC segregation during mitosis. Plays a role in chromosome congression and
CC is required for the lateral to end-on conversion of the chromosome-
CC microtubule attachment. {ECO:0000250|UniProtKB:Q99661}.
CC -!- SUBUNIT: Interacts with CENPH. Interacts with MTUS2/TIP150; the
CC interaction is direct. Interacts with MAPRE1; the interaction is
CC direct, regulated by phosphorylation and is probably required for
CC targeting to growing microtubule plus ends. Interacts with KIF18B at
CC microtubule tips; this interaction increases the affinity of both
CC partners for microtubule plus ends and is required for robust
CC microtubule depolymerization. Phosphorylation by AURKA or AURKB
CC strongly reduces KIF18B-binding. {ECO:0000250|UniProtKB:Q99661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q99661}. Nucleus {ECO:0000250|UniProtKB:P70096}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q99661}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q99661}. Note=Associates
CC with the microtubule network at the growing distal tip (the plus-end)
CC of microtubules, probably through interaction with MTUS2/TIP150 and
CC MAPRE1. Association with microtubule plus ends is also mediated by
CC interaction with KIF18B. Centromeric localization requires the presence
CC of BUB1 and SGO2. {ECO:0000250|UniProtKB:P70096,
CC ECO:0000250|UniProtKB:Q99661}.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends. {ECO:0000250|UniProtKB:Q99661}.
CC -!- PTM: Phosphorylation by AURKB, regulates association with centromeres
CC and kinetochores and the microtubule depolymerization activity.
CC {ECO:0000250|UniProtKB:Q99661}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q99661}.
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; AB072747; BAB69716.1; -; mRNA.
DR RefSeq; XP_005543633.1; XM_005543576.2.
DR AlphaFoldDB; Q95LP1; -.
DR SMR; Q95LP1; -.
DR STRING; 9541.XP_005543631.1; -.
DR Ensembl; ENSMFAT00000032667; ENSMFAP00000024527; ENSMFAG00000043842.
DR GeneID; 102134753; -.
DR KEGG; mcf:102134753; -.
DR CTD; 11004; -.
DR VEuPathDB; HostDB:ENSMFAG00000043842; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000154046; -.
DR Proteomes; UP000233100; Chromosome 1.
DR Bgee; ENSMFAG00000043842; Expressed in bone marrow and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007080; P:mitotic metaphase plate congression; 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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Disulfide bond;
KW Kinetochore; Microtubule; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..671
FT /note="Kinesin-like protein KIF2C"
FT /id="PRO_0000125419"
FT DOMAIN 204..534
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..200
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 36..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..184
FT /note="Negative regulator of microtubule-binding"
FT /evidence="ECO:0000250"
FT COILED 564..604
FT /evidence="ECO:0000255"
FT MOTIF 44..47
FT /note="Microtubule tip localization signal"
FT BINDING 294..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 41
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT DISULFID 191..233
FT /evidence="ECO:0000250"
FT DISULFID 290..506
FT /evidence="ECO:0000250"
SQ SEQUENCE 671 AA; 75639 MW; 4EAB399E8B6BBA46 CRC64;
MIDFDDVAAI NPELLQLLPL HPKDNLPLQE NVTIQKQKRR SVNSKIPAPK ESLRTRSTRM
STVSELRVTA QENDMEVELP AAANTRKQFS VPPTHPRPSC PAVAEIPSRM VSEEVEEQVH
SIRGSSSANP VNSVRRKSCI VKEVEKMKNK REEKKAQNSE MRMKRAQEYD SSFPNWEFAR
MIKEFRATLE CHPLTMTDPI EEHRICVCVR KRPLNKQELA KKEIDVISIP SKCLLLVHEP
KLKVDLTKYL ENQAFCFDFA FDETASNEVV YRFTARPLVQ TIFEGGKATC FAYGQTGSGK
THTMGGDLSG KAQNASKGIY AMASRDVFLL KNQPCYRKLG LEVYVTFFEI YNGKLFDLLN
KKAKLRVLED GKQQVQVVGL QEHLVNSADD VIKMIDMGSA CRTSGQTFAN SNSSRSHACF
QILLRAKGRM HGKFSLVDLA GNERGADTSS ADRQTRMEGA EINKSLLALK ECIRALGQNK
AHTPFRESKL TQVLRDSFIG ENSRTCMIAT ISPGISSCEY TLNTLRYADR VKELSPHSGP
SGEQLIQMET EEMEACSNGA LIPGNLSKEE EELSSQMSSF NEAMTQIREL EERAVEELKE
IIQQGPDWLE LSEMTEQPDY DLETFVNKAE FALAQQAKHF SALRDVIKAL RLAMQLEEQA
SRQISSKKRP Q
