KIF4_MOUSE
ID KIF4_MOUSE Reviewed; 1231 AA.
AC P33174; Q80YP3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Chromosome-associated kinesin KIF4;
DE AltName: Full=Chromokinesin;
GN Name=Kif4; Synonyms=Kif4a, Kns4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=7929562; DOI=10.1083/jcb.127.1.187;
RA Sekine Y., Okada Y., Noda Y., Kondo S., Aizawa H., Takemura R.,
RA Hirokawa N.;
RT "A novel microtubule-based motor protein (KIF4) for organelle transports,
RT whose expression is regulated developmentally.";
RL J. Cell Biol. 127:187-201(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 91-240.
RC TISSUE=Brain;
RX PubMed=1447303; DOI=10.1083/jcb.119.5.1287;
RA Aizawa H., Sekine Y., Takemura R., Zhang Z., Nangaku M., Hirokawa N.;
RT "Kinesin family in murine central nervous system.";
RL J. Cell Biol. 119:1287-1296(1992).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-802, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; THR-800; SER-811;
RP SER-816; SER-1224 AND SER-1230, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:7929562}.
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:7929562}. Chromosome
CC {ECO:0000269|PubMed:7929562}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:7929562}.
CC -!- TISSUE SPECIFICITY: Expressed in pyramidal cells in juvenile
CC hippocampus, granular cells in juvenile cerebellar cortex and in adult
CC spleen. {ECO:0000269|PubMed:7929562}.
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; D12646; BAA02167.1; -; mRNA.
DR EMBL; BX005480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX276129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466564; EDL14171.1; -; Genomic_DNA.
DR EMBL; BC050946; AAH50946.1; -; mRNA.
DR CCDS; CCDS30305.1; -.
DR PIR; A54803; A54803.
DR RefSeq; NP_032472.2; NM_008446.2.
DR PDB; 3ZFC; X-ray; 1.80 A; A=1-344.
DR PDB; 3ZFD; X-ray; 1.71 A; A=1-344.
DR PDBsum; 3ZFC; -.
DR PDBsum; 3ZFD; -.
DR AlphaFoldDB; P33174; -.
DR SMR; P33174; -.
DR BioGRID; 200944; 38.
DR IntAct; P33174; 29.
DR STRING; 10090.ENSMUSP00000048383; -.
DR iPTMnet; P33174; -.
DR PhosphoSitePlus; P33174; -.
DR SwissPalm; P33174; -.
DR EPD; P33174; -.
DR jPOST; P33174; -.
DR MaxQB; P33174; -.
DR PaxDb; P33174; -.
DR PeptideAtlas; P33174; -.
DR PRIDE; P33174; -.
DR ProteomicsDB; 263538; -.
DR Antibodypedia; 27394; 228 antibodies from 32 providers.
DR DNASU; 16571; -.
DR Ensembl; ENSMUST00000048962; ENSMUSP00000048383; ENSMUSG00000034311.
DR GeneID; 16571; -.
DR KEGG; mmu:16571; -.
DR UCSC; uc009twh.2; mouse.
DR CTD; 16571; -.
DR MGI; MGI:108389; Kif4.
DR VEuPathDB; HostDB:ENSMUSG00000034311; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000158195; -.
DR HOGENOM; CLU_001485_4_1_1; -.
DR InParanoid; P33174; -.
DR OMA; PAFNKQH; -.
DR OrthoDB; 369179at2759; -.
DR PhylomeDB; P33174; -.
DR TreeFam; TF105224; -.
DR BRENDA; 5.6.1.3; 3474.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16571; 20 hits in 75 CRISPR screens.
DR ChiTaRS; Kif4; mouse.
DR PRO; PR:P33174; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P33174; protein.
DR Bgee; ENSMUSG00000034311; Expressed in animal zygote and 175 other tissues.
DR Genevisible; P33174; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; DNA-binding; Iron; Iron-sulfur; Metal-binding; Microtubule;
KW Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1231
FT /note="Chromosome-associated kinesin KIF4"
FT /id="PRO_0000125438"
FT DOMAIN 9..337
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1001..1231
FT /note="Globular"
FT REGION 1189..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 351..1000
FT /evidence="ECO:0000255"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 800
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 112
FT /note="I -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044..1045
FT /note="EG -> GE (in Ref. 1; BAA02167)"
FT /evidence="ECO:0000305"
FT CONFLICT 1182
FT /note="V -> M (in Ref. 1; BAA02167)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3ZFD"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:3ZFD"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:3ZFD"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 132..144
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3ZFD"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3ZFC"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 213..225
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 228..241
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 255..279
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:3ZFD"
FT TURN 298..303
FT /evidence="ECO:0007829|PDB:3ZFD"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:3ZFD"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:3ZFD"
SQ SEQUENCE 1231 AA; 139519 MW; AA3C5E2E52678DE7 CRC64;
MKEEVKGIPV RVALRCRPLV SKEIKEGCQT CLSFVPGEPQ VVVGNDKSFT YDFVFDPSTE
QEEVFNTAVA PLIKGVFKGY NATVLAYGQT GSGKTYSMGG AYTAEQEHDS AIGVIPRVIQ
LLFKEINKKS DFEFTLKVSY LEIYNEEILD LLCSSREKAT QINIREDPKE GIKIVGLTEK
TVLVASDTVS CLEQGNNSRT VASTAMNSQS SRSHAIFTIS IEQRKKNDKN SSFRSKLHLV
DLAGSERQKK TKAEGDRLRE GININRGLLC LGNVISALGD DKKGNFVPYR DSKLTRLLQD
SLGGNSHTLM IACVSPADSN LEETLNTLRY ADRARKIKNK PIINIDPQAA ELNHLKQQVQ
QLQILLLQAH GGTLPGDINV EPSENLQSLM EKNQSLVEEN EKLSRGLSEA AGQTAQMLER
IILTEQANEK MNAKLEELRR HAACKVDLQK LVETLEDQEL KENIEIICNL QQVIAQLSDE
AAACMTATID TAGEADTQVQ SSPDTSRSSD VFSTQHALRQ AQMSKELIEL NKALALKEAL
AKKMTQNDNQ LQPIQFQYQD NIKNLESEVL SLQREKEELV LELQTAKKDA NQAKLSERRR
KRLQELEGQI ADLKKKLQEQ SKLLKLKEST EHTVSKLNQE IRMMKNQRVQ LMRQMKEDAE
KFRQWKQQKD KEVIQLKERD RKRQYELLKL ERNFQKQSNV LRRKTEEAAA ANKRLKDALQ
KQKEVAEKRK ETQSRGMEST AARMKNWLGN EIEVMVSTEE AKRHLNGLLE ERKILAQDVA
QLKEKRESGE NPPLKLRRRT FSYDEIHGQD SGAEDSIAKQ IESLETELEL RSAQIADLQQ
KLLDAESEDR PKQRWESIAT ILEAKCAIKY LVGELVSSKI LVSKLESSLN QSKASCIDVQ
KMLFEEQNHF AKIETELKEE LVKVEQQHQE KVLYLLSQLQ QSQMTEKQLE ESVSEKEQQL
LSTLKCQEEE LRKMQEVCEQ NQQLLQENSA IKQKLTLLQV ASKQKPHLTR NIFQSPDSSF
EYIPPKPKPC RIKEKCLEQS FAVEGLQYYS EPSVAEQDNE DSDDHADEEW IPTKLVKVSK
KSIQGCSCKG WCGNKQCGCR KQKSDCNVSC SCDPTKCRNR HQNQDNSDAI ELNQDSENSF
KLEDPTEVTS GLSFFHPICA TPSSKILKEM CDADQVQLKQ PVFVSSSDHP ELKSIASESQ
ENKAIGKKKK RALASNTSFF SGCSPIQEES H
