KIF5C_MOUSE
ID KIF5C_MOUSE Reviewed; 956 AA.
AC P28738; Q6NXI9; Q9Z2F8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Kinesin heavy chain isoform 5C;
DE AltName: Full=Kinesin heavy chain neuron-specific 2;
GN Name=Kif5c; Synonyms=Nkhc2;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA Kato K.;
RT "A collection of cDNA clones with specific expression patterns in mouse
RT brain.";
RL Eur. J. Neurosci. 2:704-711(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9782088; DOI=10.1006/geno.1998.5427;
RA Xia C., Rahman A., Yang Z., Goldstein L.S.B.;
RT "Chromosomal localization reveals three kinesin heavy chain genes in
RT mouse.";
RL Genomics 52:209-213(1998).
RN [3]
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 [4]
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 (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 133-142; 242-253; 258-274; 287-297; 546-555 AND
RP 815-830, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP INTERACTION WITH GRIP1.
RX PubMed=11986669; DOI=10.1038/nature743;
RA Setou M., Seog D.-H., Tanaka Y., Kanai Y., Takei Y., Kawagishi M.,
RA Hirokawa N.;
RT "Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to
RT dendrites.";
RL Nature 417:83-87(2002).
RN [8]
RP FUNCTION.
RX PubMed=19608740; DOI=10.1074/jbc.m109.022137;
RA Kindler S., Dieterich D.C., Schutt J., Sahin J., Karpova A., Mikhaylova M.,
RA Schob C., Gundelfinger E.D., Kreienkamp H.J., Kreutz M.R.;
RT "Dendritic mRNA targeting of Jacob and N-methyl-d-aspartate-induced nuclear
RT translocation after calpain-mediated proteolysis.";
RL J. Biol. Chem. 284:25431-25440(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [10]
RP INTERACTION WITH ZFYVE27.
RX PubMed=21976701; DOI=10.1091/mbc.e11-01-0068;
RA Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.;
RT "Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes
RT in vesicular transport during process formation.";
RL Mol. Biol. Cell 22:4602-4620(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 329-334 IN COMPLEXES WITH KIF1A,
RP SUBUNIT, AND INTERACTION WITH MICROTUBULES.
RX PubMed=15286375; DOI=10.1126/science.1096621;
RA Nitta R., Kikkawa M., Okada Y., Hirokawa N.;
RT "KIF1A alternately uses two loops to bind microtubules.";
RL Science 305:678-683(2004).
CC -!- FUNCTION: Involved in synaptic transmission (By similarity). Kinesin is
CC a microtubule-associated force-producing protein that may play a role
CC in organelle transport. Mediates dendritic trafficking of mRNAs
CC (PubMed:19608740). Required for anterograde axonal transportation of
CC MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon
CC elongation (By similarity). {ECO:0000250|UniProtKB:O60282,
CC ECO:0000250|UniProtKB:P56536, ECO:0000269|PubMed:19608740}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains
CC (PubMed:15286375). Interacts with GRIP1 (PubMed:11986669). Interacts
CC with KLC3 and TRAK1 (By similarity). Interacts with ZFYVE27
CC (PubMed:21976701). {ECO:0000250|UniProtKB:O60282,
CC ECO:0000250|UniProtKB:P56536, ECO:0000269|PubMed:11986669,
CC ECO:0000269|PubMed:15286375, ECO:0000269|PubMed:21976701}.
CC -!- INTERACTION:
CC P28738; Q9ESN9: Mapk8ip3; NbExp=8; IntAct=EBI-2506834, EBI-301496;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:O60282}. Note=Abundant in
CC distal regions of dendrites. {ECO:0000250|UniProtKB:O60282}.
CC -!- DOMAIN: Composed of three structural domains: a large globular N-
CC terminal domain which is responsible for the motor activity of kinesin
CC (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC coiled coil domain that mediates the heavy chain dimerization; and a
CC small globular C-terminal domain which interacts with other proteins
CC (such as the kinesin light chains), vesicles and membranous organelles.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43677.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. The C-terminus (up to position 300) corresponds to KIF5C sequence.; Evidence={ECO:0000305};
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DR EMBL; X61435; CAA43677.1; ALT_SEQ; mRNA.
DR EMBL; AF067180; AAC79804.1; -; mRNA.
DR EMBL; AL845332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL26880.1; -; Genomic_DNA.
DR EMBL; BC067051; AAH67051.1; -; mRNA.
DR CCDS; CCDS16024.1; -.
DR PIR; S37711; S37711.
DR RefSeq; NP_032475.2; NM_008449.2.
DR PDB; 1VFV; X-ray; 1.85 A; A=329-334.
DR PDB; 1VFW; X-ray; 2.30 A; A=329-334.
DR PDB; 1VFX; X-ray; 2.55 A; A=329-334.
DR PDB; 1VFZ; X-ray; 2.24 A; A=329-334.
DR PDB; 3J6H; EM; 8.10 A; K=1-345.
DR PDB; 3WRD; X-ray; 2.86 A; A/B=1-334.
DR PDB; 3X2T; X-ray; 2.70 A; A/B=1-334.
DR PDB; 5HLE; X-ray; 2.90 A; A=10-320.
DR PDBsum; 1VFV; -.
DR PDBsum; 1VFW; -.
DR PDBsum; 1VFX; -.
DR PDBsum; 1VFZ; -.
DR PDBsum; 3J6H; -.
DR PDBsum; 3WRD; -.
DR PDBsum; 3X2T; -.
DR PDBsum; 5HLE; -.
DR AlphaFoldDB; P28738; -.
DR SMR; P28738; -.
DR BioGRID; 200947; 23.
DR CORUM; P28738; -.
DR IntAct; P28738; 19.
DR MINT; P28738; -.
DR STRING; 10090.ENSMUSP00000028102; -.
DR iPTMnet; P28738; -.
DR PhosphoSitePlus; P28738; -.
DR EPD; P28738; -.
DR jPOST; P28738; -.
DR MaxQB; P28738; -.
DR PaxDb; P28738; -.
DR PeptideAtlas; P28738; -.
DR PRIDE; P28738; -.
DR ProteomicsDB; 263540; -.
DR Antibodypedia; 33631; 152 antibodies from 22 providers.
DR DNASU; 16574; -.
DR Ensembl; ENSMUST00000028102; ENSMUSP00000028102; ENSMUSG00000026764.
DR GeneID; 16574; -.
DR KEGG; mmu:16574; -.
DR UCSC; uc008jpy.1; mouse.
DR CTD; 3800; -.
DR MGI; MGI:1098269; Kif5c.
DR VEuPathDB; HostDB:ENSMUSG00000026764; -.
DR eggNOG; KOG0240; Eukaryota.
DR GeneTree; ENSGT00940000158539; -.
DR HOGENOM; CLU_001485_11_1_1; -.
DR InParanoid; P28738; -.
DR OMA; AAKQHEM; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; P28738; -.
DR TreeFam; TF105225; -.
DR BioGRID-ORCS; 16574; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Kif5c; mouse.
DR EvolutionaryTrace; P28738; -.
DR PRO; PR:P28738; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P28738; protein.
DR Bgee; ENSMUSG00000026764; Expressed in globus pallidus and 215 other tissues.
DR ExpressionAtlas; P28738; baseline and differential.
DR Genevisible; P28738; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0044295; C:axonal growth cone; IDA:ARUK-UCL.
DR GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0150034; C:distal axon; IDA:ARUK-UCL.
DR GO; GO:0005871; C:kinesin complex; ISS:MGI.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0034190; F:apolipoprotein receptor binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0098963; P:dendritic transport of messenger ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
DR GO; GO:0051028; P:mRNA transport; IMP:UniProtKB.
DR GO; GO:0048489; P:synaptic vesicle transport; 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 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 3D-structure; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..956
FT /note="Kinesin heavy chain isoform 5C"
FT /id="PRO_0000125356"
FT DOMAIN 8..327
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 174..315
FT /note="Microtubule-binding"
FT REGION 859..956
FT /note="Globular"
FT REGION 910..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 406..923
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 403
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 387
FT /note="Q -> H (in Ref. 2; AAC79804)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="R -> I (in Ref. 2; AAC79804)"
FT /evidence="ECO:0000305"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3X2T"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5HLE"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:3X2T"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:3X2T"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 108..122
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 125..139
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5HLE"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 206..216
FT /evidence="ECO:0007829|PDB:3X2T"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3WRD"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:3X2T"
FT TURN 288..293
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 294..304
FT /evidence="ECO:0007829|PDB:3X2T"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3X2T"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:3X2T"
SQ SEQUENCE 956 AA; 109275 MW; A36BC903603D8748 CRC64;
MADPAECSIK VMCRFRPLNE AEILRGDKFI PKFKGEETVV IGQGKPYVFD RVLPPNTTQE
QVYNACAKQI VKDVLEGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIAHDIFDHI
YSMDENLEFH IKVSYFEIYL DKIRDLLDVS KTNLAVHEDK NRVPYVKGCT ERFVSSPEEV
MDVIDEGKAN RHVAVTNMNE HSSRSHSIFL INIKQENVET EKKLSGKLYL VDLAGSEKVS
KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKTHVPYR DSKMTRILQD SLGGNCRTTI
VICCSPSVFN EAETKSTLMF GQRAKTIKNT VSVNLELTAE EWKKKYEKEK EKNKALKSVL
QHLEMELNRW RNGEAVPEDE QISAKDQKSL EPCDNTPIID NITPVVDGIS AEKEKYDEEI
TSLYRQLDDK DDEINQQSQL AEKLKQQMLD QDELLASTRR DYEKIQEELT RLQIENEAAK
DEVKEVLQAL EELAVNYDQK SQEVEDKTRA NEQLTDELAQ KTTTLTTTQR ELSQLQELSN
HQKKRATEIL NLLLKDLGEI GGIIGTNDVK TLADVNGVIE EEFTMARLYI SKMKSEVKSL
VNRSKQLESA QMDSNRKMNA SERELAACQL LISQHEAKIK SLTDYMQNME QKRRQLEESQ
DSLSEELAKL RAQEKMHEVS FQDKEKEHLT RLQDAEEVKK ALEQQMESHR EAHQKQLSRL
RDEIEEKQRI IDEIRDLNQK LQLEQERLSS DYNKLKIEDQ EREVKLEKLL LLNDKREQAR
EDLKGLEETV SRELQTLHNL RKLFVQDLTT RVKKSVELDS DDGGGSAAQK QKISFLENNL
EQLTKVHKQL VRDNADLRCE LPKLEKRLRA TAERVKALES ALKEAKENAM RDRKRYQQEV
DRIKEAVRAK NMARRAHSAQ IAKPIRPGHY PASSPTAVHA VRGGGGGSSN STHYQK
