KIF4_XENLA
ID KIF4_XENLA Reviewed; 1226 AA.
AC Q91784; Q9PSI0;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chromosome-associated kinesin KIF4;
DE AltName: Full=Chromokinesin;
DE AltName: Full=Chromosome-associated kinesin KLP1;
GN Name=kif4; Synonyms=kif4a, klp1;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Oocyte;
RX PubMed=7720067; DOI=10.1016/0092-8674(95)90376-3;
RA Vernos I., Raats J., Hirano T., Heasman J., Karsenti E., Wylie C.;
RT "Xklp1, a chromosomal Xenopus kinesin-like protein essential for spindle
RT organization and chromosome positioning.";
RL Cell 81:117-127(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-338.
RX PubMed=8482413; DOI=10.1006/dbio.1993.1127;
RA Vernos I., Heasman J., Wylie C.;
RT "Multiple kinesin-like transcripts in Xenopus oocytes.";
RL Dev. Biol. 157:232-239(1993).
CC -!- FUNCTION: Iron-sulfur (Fe-S) cluster binding motor protein that has a
CC role in chromosome segregation during mitosis (By similarity). Required
CC for mitotic chromosomal positioning and bipolar spindle stabilization.
CC {ECO:0000250|UniProtKB:O95239, ECO:0000269|PubMed:7720067}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:O95239};
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:O95239};
CC Note=Binds 1 [4Fe-4S] cluster (By similarity). In the presence of
CC oxygen, the [4Fe-4S] cluster may be converted to [2Fe-2S] (By
CC similarity). {ECO:0000250|UniProtKB:O95239};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7720067}. Chromosome
CC {ECO:0000269|PubMed:7720067}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:7720067}. Note=Associated with mitotic chromosomes.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes, eggs, testes and brain.
CC {ECO:0000269|PubMed:7720067}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Chromokinesin subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; X82012; CAA57539.1; -; mRNA.
DR PIR; I51617; I51617.
DR RefSeq; NP_001081019.1; NM_001087550.1.
DR AlphaFoldDB; Q91784; -.
DR SMR; Q91784; -.
DR BioGRID; 98934; 1.
DR DIP; DIP-48591N; -.
DR IntAct; Q91784; 4.
DR PRIDE; Q91784; -.
DR GeneID; 394332; -.
DR KEGG; xla:394332; -.
DR CTD; 394332; -.
DR Xenbase; XB-GENE-6079277; kif4a.S.
DR OrthoDB; 369179at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 394332; Expressed in egg cell and 18 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 3.40.850.10; -; 1.
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 InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01114; CXC; 1.
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; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding;
KW Iron; Iron-sulfur; Metal-binding; Microtubule; Motor protein;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1226
FT /note="Chromosome-associated kinesin KIF4"
FT /id="PRO_0000125440"
FT DOMAIN 8..337
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 494..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1226
FT /note="Globular"
FT REGION 1052..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 351..1006
FT /evidence="ECO:0000255"
FT COMPBIAS 722..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 163
FT /note="I -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1226 AA; 138924 MW; 7F0275FCF3316697 CRC64;
MGKDEGIPVR VALRCRPLVP KENNEGCKMC LTFVPGEQQV IVGTEKSFTY DYVFDPSAEQ
EEVYNSAVAP LIKGLFKGYN ATVLAYGQTG SGKTYSMGGA YTHNQENEPT VGVIPRTVIA
LFREIHQRPE WEFNLKVSYL EIYNEEILDL LYAARDKTNT ISIREDPKEG IKICGLTERD
VKTALDTLSC LEQGNSSRTV ASTAMNSQSS RSHAIFTISI EQRKEGDKNN SFRSKLHLVD
LAGSERQKKT KAEGDRLKEG ISINRGLLCL GNVISALGDE SKKGGFVPYR DSKLTRLLQD
SLGGNSHTLM IACVSPADSN MEETLNTLRY ADRARKIKNK PIVNTDPQAA ELQRLKLQVQ
ELQVLLLQAH GGTLPVLNSM EPSENLQSLM ERNKNLEKEN GKLSRELGEA AVQTAQFLEK
IIMTEQQNEK LGSKMEELKQ HAACKVNLQR LVETLEDQEL KDNVEVIQNL QQVIVQLQDE
SSGIAGSIEA MDEEAASFPV PEEDSGEKRS SDGFTTNHAL RQAQLSKELI ELNKALVMKE
ALAKKMAQND RQLEPIQSEY LNNIKHLESE VGVLQKEKEE LILALHSAKK DNNQAKLSER
RRKRLQELEG QMTELKKKLG EQSKLLKLRE STEKTVAKMN QEIQGMKMQR VQLMRQMKED
AEKFRTWKQQ KTKEVIQLKE KDRKRQYELL KLERDFQKQA NVLRRKTEEA ASANKRLKEA
LQRQKEAMEK RKDSQSKGME GAASRVKNWL ANEVEVLVST EEAQRHLNDL LEDRKILAQD
IAQLKQKTDA GERIPTKIRR RTYTVAELEN LEEEASVTKQ IESLETEMEL RSAQIADLQQ
KLLDADGEEE MVKRRWETIS NIMEAKCALK YLITELVSSK VAGSKLESSV KQNRAHVADL
QKNIFEERNQ MAEMETEHQS QLMQLEQHHQ EKILYLLSQL QQKQASVPVT IEELPAEEIT
EREKQLMERL KFQDEEIEKM KALCEKNQQL LQENDMYKQK LALLHVASGK KLHNILPAAE
ICSPDSPFDF IPPKPRGKRR TNAKSAAVIL EDLLSESESE EESDDKNWEP GNNSKQSKKL
TSKCSCKARC GNKMCGCRKT KQNCSDDCFC DPSKCRNRDN HMDEGKHEDQ SLESENSKID
YPDVTAGGSF FTPPCVTPTK KVLREISDIG QVLSIKLQRK PSTASASASV MESQENQTSI
LTKKKKVLCN SNTSFFSGCS AITEDE
