KIF2C_XENLA
ID KIF2C_XENLA Reviewed; 730 AA.
AC Q91636; Q5D0B4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Kinesin-like protein KIF2C;
DE AltName: Full=Kinesin central motor 1;
DE Short=xKCM1;
GN Name=kif2c; Synonyms=kcm1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Ovary;
RX PubMed=8548824; DOI=10.1016/s0092-8674(00)80991-5;
RA Walczak C.E., Mitchison T.J., Desai A.;
RT "XKCM1: a Xenopus kinesin-related protein that regulates microtubule
RT dynamics during mitotic spindle assembly.";
RL Cell 84:37-47(1996).
RN [2]
RP SEQUENCE REVISION TO 516.
RA Walczak C.E.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH MTUS1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12919681; DOI=10.1016/s1534-5807(03)00229-6;
RA Ohi R., Coughlin M.L., Lane W.S., Mitchison T.J.;
RT "An inner centromere protein that stimulates the microtubule depolymerizing
RT activity of a KinI kinesin.";
RL Dev. Cell 5:309-321(2003).
CC -!- FUNCTION: Promotes ATP-dependent removal of tubulin dimers from
CC microtubules. Regulates the turnover of microtubules at the kinetochore
CC and functions in chromosome segregation during mitosis
CC (PubMed:8548824). May play a role in chromosome congression and may be
CC required for the lateral to end-on conversion of the chromosome-
CC microtubule attachment (By similarity). {ECO:0000250|UniProtKB:Q99661,
CC ECO:0000269|PubMed:8548824}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q99661}. Nucleus {ECO:0000250|UniProtKB:P70096}.
CC Chromosome, centromere {ECO:0000269|PubMed:12919681,
CC ECO:0000269|PubMed:8548824}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:12919681, ECO:0000269|PubMed:8548824}.
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; U36485; AAC59743.2; -; mRNA.
DR EMBL; BC044976; AAH44976.1; -; mRNA.
DR RefSeq; NP_001080314.1; NM_001086845.1.
DR AlphaFoldDB; Q91636; -.
DR SMR; Q91636; -.
DR BioGRID; 98248; 1.
DR IntAct; Q91636; 2.
DR iPTMnet; Q91636; -.
DR MaxQB; Q91636; -.
DR PRIDE; Q91636; -.
DR DNASU; 380006; -.
DR GeneID; 380006; -.
DR KEGG; xla:380006; -.
DR CTD; 380006; -.
DR Xenbase; XB-GENE-961451; kif2c.S.
DR OrthoDB; 418348at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 380006; Expressed in egg cell and 16 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:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
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 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 ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..730
FT /note="Kinesin-like protein KIF2C"
FT /id="PRO_0000125422"
FT DOMAIN 262..592
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..256
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 79..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..242
FT /note="Negative regulator of microtubule-binding"
FT /evidence="ECO:0000250"
FT COILED 599..730
FT /evidence="ECO:0000255"
FT COMPBIAS 79..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 730 AA; 82586 MW; 25C31C187E491523 CRC64;
MERLVATRLV TGLAVKIMRS NGVIHNANIT SVNMDRSSVN VEWKEGEANK GKEISFADVI
SVNPELLDAV LAPTNVKENM PPQRNVSSQN HKRKTISKIP APKEVAAKNS LLSESGAQSV
LRERSTRMTA IHETLPYENE MEAESTPLPI QQNSVQARSR STKVSIAEEP RLQTRISEIV
EESLPSGRNN QGRRKSNIVK EMEKMKNKRE EQRAQNYERR MKRAQDYDTS VPNWEFGKMI
KEFRATMDCH RISMADPAEE HRICVCVRKR PLNKQELSKK EIDIISVPSK NIVLVHEPKL
KVDLTKYLEN QAFRFDFSFD ETATNEVVYR FTARPLVQSI FEGGKATCFA YGQTGSGKTH
TMGGDFSGKS QNVSKGVYAF ASRDVFLLLD QPRYKHLDLD VFVTFFEIYN GKVFDLLNKK
TKLRVLEDAK QEVQVVGLLE KQVISADDVF KMIEIGSACR TSGQTFANTS SSRSHACLQI
ILRRGSKLHG KFSLVDLAGN ERGVDTASAD RITRMEGAEI NRSLLALKEC IRALGQNKSH
TPFRESKLTQ ILRDSFIGEN SRTCMIAMLS PGFNSCEYTL NTLRYADRVK ELSPQNAETN
DDNLQMEDSG GSHASIEGLQ LQDDFLLKDE ELSTHNSFQD ALNRVGELED KAVDELRELV
QKEPEWTNLL QMTEQPDYDL ENFVMQAEYL IQERSKVLIA LGDSINSLRL ALQVEEQASK
QISKKKRSNK
