KIF4_CHICK
ID KIF4_CHICK Reviewed; 1225 AA.
AC Q90640; Q90608;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Chromosome-associated kinesin KIF4;
DE AltName: Full=Chromokinesin;
GN Name=KIF4; Synonyms=KIF4A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Embryonic retina;
RX PubMed=7876303; DOI=10.1083/jcb.128.5.761;
RA Wang S.Z., Adler R.;
RT "Chromokinesin: a DNA-binding, kinesin-like nuclear protein.";
RL J. Cell Biol. 128:761-768(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 728-1088.
RC STRAIN=White leghorn; TISSUE=Embryonic retina;
RX PubMed=8108415; DOI=10.1073/pnas.91.4.1351;
RA Wang S.Z., Adler R.;
RT "A developmentally regulated basic-leucine zipper-like gene and its
RT expression in embryonic retina and lens.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1351-1355(1994).
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:7876303}.
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:7876303}. Chromosome
CC {ECO:0000269|PubMed:7876303}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:7876303}.
CC -!- TISSUE SPECIFICITY: Expressed in proliferating cells; neuroepithelium
CC of embryos. {ECO:0000269|PubMed:7876303}.
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; U18309; AAC59666.1; -; mRNA.
DR EMBL; U04821; AAA18960.1; -; mRNA.
DR PIR; A56514; A56514.
DR RefSeq; NP_990306.1; NM_204975.1.
DR AlphaFoldDB; Q90640; -.
DR SMR; Q90640; -.
DR STRING; 9031.ENSGALP00000006656; -.
DR PaxDb; Q90640; -.
DR PRIDE; Q90640; -.
DR GeneID; 395823; -.
DR KEGG; gga:395823; -.
DR CTD; 285643; -.
DR VEuPathDB; HostDB:geneid_395823; -.
DR eggNOG; KOG0244; Eukaryota.
DR InParanoid; Q90640; -.
DR OrthoDB; 369179at2759; -.
DR PhylomeDB; Q90640; -.
DR PRO; PR:Q90640; -.
DR Proteomes; UP000000539; Unplaced.
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:0005875; C:microtubule associated complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
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..1225
FT /note="Chromosome-associated kinesin KIF4"
FT /id="PRO_0000125439"
FT DOMAIN 9..338
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 498..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1225
FT /note="Globular"
FT REGION 1006..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..1003
FT /evidence="ECO:0000255"
FT COMPBIAS 717..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 1087..1088
FT /note="KG -> RI (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1225 AA; 138924 MW; FA01ED83425F5875 CRC64;
MVREEEKGIP VRVVRCRPLV PKETSEGCQM CLSFVPGEPQ VIVGSDKAFT YDYVFDPSVE
QEEVFNTAVA PLIRGIFKGY NATVLAYGQT GSGKTYSMGG TYTASQEHDP SMGVIPRVIK
LLFKEKEQRQ DWEFVLKVSY LEIYNEDILD LLCSSRERSS QISIREDPKE GIKIVGLTER
NVASARDTVS CLEQGNNCRT VASTAMNSQS SRSHAIFTIC IDQKKKNDKN SSFHSKLHLV
DLAGSERQKK TKAEGDRLKE GININRGLLC LGNVISALGE ENKKGGFVPY RDSKLTRLLQ
DSLGGNSHTL MIACVSPADS NLEETLNTLR YADRARKIKN KPIVNVDPQA AELNHLKQQV
QQLQVLLLQA HGGTLPVSIN SMAPSENLQS LMEKNQSLME ENEKLSRGLS EAAGQTAQML
ERIIVTEQEN EKMNAKLEQL QQHAVCKLDL QKLLETVEDE ELKENVEVIR NLQQVLAQFQ
SESAAAAEAA TEMANAEQDA AGEAETGQVT KRSSDDFTTQ HALRQAQMSK ELVELNKALA
LKEALAKKMI QNDSQLEPIQ SQYQTNIKDL ELEVSNLQKE KEELILALSM AKKDVNQAKL
SERRRKRLQE LEGQINELKK KLNEQAKLLK LKESTERTVS KLNQEIREMK NQRVQLMRQM
KEDAEKFRQW KQQKDKEVIQ LKERDRKRQY ELLKLERDFQ KQASVLRRKT EEAAAANKRL
KDALQKQREA ADKRKESQNR GMEGVAARVK SWLANEVEVL VSTEEARRHL ADLLEDRKIL
AQELLQLKEK KESGENPPSK LRRRTYSITD LQASEMDLSL SKQIESLETE MELRSAQIAD
LQQKLLDADN GDRVKQRWDN IATILEAKCA LKYLLGELVS SKVQESKLES SLQQSKTNCS
DIQKMLIEER NHATEMEAEF QNQLLLQEQQ HQQEVLYLLS QFQQKEAPGK GVEDSLSEQE
KQMQERLKFQ EKELEKMREI CEKNQELLQE NDVLKQKMLL VQVASGQKLR RDQQVSPESP
DSPFDYIPPK PKTRRQTVAK PRAPTPEMNV EELFSDSEES GEEEDAEWVP VKAAKGTKKS
ATGCFCKGRC GNRQCGCRKQ KVGCTAGCSC DSTKCRNRDP GFQDATVCED QTKDSEGSFK
LEDLRDVTAG ETFFQPVYSP PTMKVLKDIT DQGVFMKKPS TAASLLVRDE ESQENQLPFV
KKKKRMLSSN TSFFSGCTPI KEEID
