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   04-NOV-2026, entry version 206.
DE   RecName: Full=Kinesin heavy chain isoform 5C;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P56536};
DE   AltName: Full=Kinesin heavy chain neuron-specific 2;
DE   AltName: Full=Kinesin-1 {ECO:0000250|UniProtKB:P56536};
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 IN COMPLEXES WITH KIF1A, SUBUNIT, AND INTERACTION
RP   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: Microtubule-associated force-producing protein that may play
CC       a role in organelle transport. Has ATPase activity (By similarity).
CC       Involved in synaptic transmission (By similarity). Mediates dendritic
CC       trafficking of mRNAs (PubMed:19608740). Required for anterograde axonal
CC       transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3
CC       function in axon elongation (By similarity).
CC       {ECO:0000250|UniProtKB:O60282, ECO:0000250|UniProtKB:P56536,
CC       ECO:0000269|PubMed:19608740}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P56536};
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_008449.3.
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   AlphaFoldDB; P28738; -.
DR   EMDB; EMD-5916; -.
DR   SMR; P28738; -.
DR   BioGRID; 200947; 26.
DR   CORUM; P28738; -.
DR   FunCoup; P28738; 1211.
DR   IntAct; P28738; 19.
DR   STRING; 10090.ENSMUSP00000028102; -.
DR   GlyGen; P28738; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P28738; -.
DR   PhosphoSitePlus; P28738; -.
DR   SwissPalm; P28738; -.
DR   jPOST; P28738; -.
DR   PaxDb; 10090-ENSMUSP00000028102; -.
DR   PeptideAtlas; P28738; -.
DR   ProteomicsDB; 263540; -.
DR   Antibodypedia; 33631; 165 antibodies from 24 providers.
DR   DNASU; 16574; -.
DR   Ensembl; ENSMPUT00000003598; ENSMPUP00000003531; ENSMPUG00000003561.
DR   Ensembl; ENSMUST00000028102.14; ENSMUSP00000028102.8; ENSMUSG00000026764.16.
DR   GeneID; 16574; -.
DR   KEGG; mmu:16574; -.
DR   UCSC; uc008jpy.1; mouse.
DR   AGR; MGI:1098269; -.
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; AAKHHIC; -.
DR   OrthoDB; 3176171at2759; -.
DR   PhylomeDB; P28738; -.
DR   BRENDA; 3.6.4.B1; 3474.
DR   BioGRID-ORCS; 16574; 1 hit in 79 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   EvolutionaryTrace; P28738; -.
DR   PRO; PR:P28738; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P28738; protein.
DR   Bgee; ENSMUSG00000026764; Expressed in globus pallidus and 218 other cell types or tissues.
DR   ExpressionAtlas; P28738; baseline and differential.
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: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; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; TAS:MGI.
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:0098957; P:anterograde axonal transport of mitochondrion; IBA:GO_Central.
DR   GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; IDA:SynGO.
DR   GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR   GO; GO:0008298; P:intracellular mRNA localization; IEA:Ensembl.
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   GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR   CDD; cd23649; Khc_CBD_cc; 1.
DR   CDD; cd01369; KISc_KHC_KIF5; 1.
DR   FunFam; 3.40.850.10:FF:000009; Kinesin-like protein; 1.
DR   Gene3D; 6.10.250.1590; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR059182; Khc_C.
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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF70; KINESIN HEAVY CHAIN ISOFORM 5C; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Hydrolase; Microtubule;
KW   Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   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         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
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          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          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          205..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
//