KIF2C_RAT
ID KIF2C_RAT Reviewed; 671 AA.
AC Q62909;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Kinesin-like protein KIF2C;
DE AltName: Full=Kinesin-related protein 2;
DE AltName: Full=Mitotic centromere-associated kinesin;
DE Short=MCAK;
GN Name=Kif2c; Synonyms=Krp2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8688559; DOI=10.1091/mbc.7.2.289;
RA Sperry A.O., Zhao L.-P.;
RT "Kinesin-related proteins in the mammalian testes: candidate motors for
RT meiosis and morphogenesis.";
RL Mol. Biol. Cell 7:289-305(1996).
RN [2]
RP SEQUENCE REVISION.
RA Sperry A.O.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: Testis. Localized to the meiotically active cells
CC of the seminiferous epithelia in the testis.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53528.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U44979; AAC53528.1; ALT_FRAME; mRNA.
DR PIR; T10755; T10755.
DR AlphaFoldDB; Q62909; -.
DR SMR; Q62909; -.
DR STRING; 10116.ENSRNOP00000025903; -.
DR iPTMnet; Q62909; -.
DR PhosphoSitePlus; Q62909; -.
DR PaxDb; Q62909; -.
DR PRIDE; Q62909; -.
DR UCSC; RGD:620239; rat.
DR RGD; 620239; Kif2c.
DR eggNOG; KOG0246; Eukaryota.
DR InParanoid; Q62909; -.
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:Q62909; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
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:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; ISO:RGD.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; 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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..671
FT /note="Kinesin-like protein KIF2C"
FT /id="PRO_0000125421"
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 37..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..138
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 REGION 533..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 566..601
FT /evidence="ECO:0000255"
FT MOTIF 44..47
FT /note="Microtubule tip localization signal"
FT COMPBIAS 540..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
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 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
SQ SEQUENCE 671 AA; 75572 MW; D3CE21F711F88506 CRC64;
MIDIDDVAAI NPELVQLLPL RPKDSLPLQE NVTIPKQKRK SVNSKIPGPK EGLRSRSTRI
STVSEVRIPA QENEMEVELP VSTNSRKPFP IHTGHPRPSC STVTELPLLM ISEEAEEQAH
STRSTSSANP GNSVRRKSCI VKEMEKMKNK REEKRAQNSE IRIKRAQEYD NSFPNWEFAR
MIKEFRVTMD CNPLTVTDPI EEHRICVCVR KRPLNKQELA KKEIDVISVP SKCLLLVHEP
KLKVDLTKYL ENQAFCFDFA FDETASNEVV YRFTARPLVQ TIFEGGKATC FAYGQTGSGK
THTMGGDLSG KSQNASKGIY AMASRDVFLL KNQPRYRSLN LEVYVTFFEI YNGKVFELLN
KKAKLRVLED SKQQVQVVGL QEYLVTCADD VIKMINMGSA CRTSGQTFAN SNSSRSHACF
QILLRAKGRL HGKFSLVDLA GNERGADTSS ADRQTRMEGA EINKSLLALK ESIRALGQNK
AHTPFRESKL TQVLRDSFIG ENSRTCMIAM ISPGISSCEY TLNTLRYADR VKELSPHSGP
SGEQAVQMET EEMDASSHGA SLTGNEEEEL SSQMSSFNEA MTQIRELEER AMEELREIIQ
QGPSWLELSE MTDQPDYDLE TFVNKAESAL TQQAKQAKHF SALQEVIKAL RLAMQLEEQA
SKQINSKKRH Q
