KIF5C_RAT
ID KIF5C_RAT Reviewed; 239 AA.
AC P56536;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Kinesin heavy chain isoform 5C;
DE AltName: Full=Kinesin heavy chain neuron-specific 2;
DE Flags: Fragment;
GN Name=Kif5c; Synonyms=Nkhc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP INTERACTION WITH KLC3.
RX PubMed=11319135; DOI=10.1095/biolreprod64.5.1320;
RA Junco A., Bhullar B., Tarnasky H.A., van der Hoorn F.A.;
RT "Kinesin light-chain KLC3 expression in testis is restricted to
RT spermatids.";
RL Biol. Reprod. 64:1320-1330(2001).
RN [2]
RP FUNCTION.
RX PubMed=23576431; DOI=10.1074/jbc.m113.464453;
RA Sun T., Yu N., Zhai L.K., Li N., Zhang C., Zhou L., Huang Z., Jiang X.Y.,
RA Shen Y., Chen Z.Y.;
RT "c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3) regulates
RT neuronal axon elongation in a kinesin- and JNK-dependent manner.";
RL J. Biol. Chem. 288:14531-14543(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY OF 2-239 (1.9 ANGSTROMS).
RC TISSUE=Brain;
RX PubMed=9405049; DOI=10.1021/bi9722498;
RA Sack S., Mueller J., Marx A., Thormaehlen M., Mandelkow E.M., Brady S.T.,
RA Mandelkow E.;
RT "X-ray structure of motor and neck domains from rat brain kinesin.";
RL Biochemistry 36:16155-16165(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY OF 2-239 (3.1 ANGSTROMS).
RX PubMed=9428521; DOI=10.1016/s0092-8674(00)80489-4;
RA Kozielski F., Sack S., Marx A., Thormahlen M., Schonbrunn E., Biou V.,
RA Thompson A., Mandelkow E.M., Mandelkow E.;
RT "The crystal structure of dimeric kinesin and implications for microtubule-
RT dependent motility.";
RL Cell 91:985-994(1997).
CC -!- FUNCTION: Involved in synaptic transmission (By similarity). Mediates
CC dendritic trafficking of mRNAs (By similarity). Kinesin is a
CC microtubule-associated force-producing protein that may play a role in
CC organelle transport (By similarity). Required for anterograde axonal
CC transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3
CC function in axon elongation (PubMed:23576431).
CC {ECO:0000250|UniProtKB:O60282, ECO:0000250|UniProtKB:P28738,
CC ECO:0000269|PubMed:23576431}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC Interacts with GRIP1. Interacts with TRAK1. Interacts with ZFYVE27 (By
CC similarity). Interacts with KLC3 (PubMed:11319135).
CC {ECO:0000250|UniProtKB:O60282, ECO:0000250|UniProtKB:P28738,
CC ECO:0000269|PubMed:11319135}.
CC -!- INTERACTION:
CC P56536; Q8IXI2: RHOT1; Xeno; NbExp=5; IntAct=EBI-994504, EBI-1396430;
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}.
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DR PDB; 2KIN; X-ray; 2.00 A; A=2-239.
DR PDB; 3KIN; X-ray; 3.10 A; A/C=2-239.
DR PDBsum; 2KIN; -.
DR PDBsum; 3KIN; -.
DR AlphaFoldDB; P56536; -.
DR SMR; P56536; -.
DR IntAct; P56536; 8.
DR MINT; P56536; -.
DR STRING; 10116.ENSRNOP00000006341; -.
DR jPOST; P56536; -.
DR PaxDb; P56536; -.
DR PeptideAtlas; P56536; -.
DR PRIDE; P56536; -.
DR UCSC; RGD:1308539; rat.
DR RGD; 1308539; Kif5c.
DR InParanoid; P56536; -.
DR PhylomeDB; P56536; -.
DR EvolutionaryTrace; P56536; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0044295; C:axonal growth cone; ISO:RGD.
DR GO; GO:0035253; C:ciliary rootlet; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0150034; C:distal axon; ISO:RGD.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0034190; F:apolipoprotein receptor binding; IPI:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:RGD.
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; IMP:UniProtKB.
DR GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; IMP:SynGO.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
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; IMP:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; ISO:RGD.
DR GO; GO:0051028; P:mRNA transport; ISS: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; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..>239
FT /note="Kinesin heavy chain isoform 5C"
FT /id="PRO_0000125357"
FT DOMAIN 8..>239
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 174..>239
FT /note="Microtubule-binding"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT NON_TER 239
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2KIN"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:2KIN"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 127..139
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 177..192
FT /evidence="ECO:0007829|PDB:2KIN"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 205..217
FT /evidence="ECO:0007829|PDB:2KIN"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:2KIN"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:2KIN"
SQ SEQUENCE 239 AA; 27165 MW; C96C5FFE4F8E1D7E CRC64;
MADPAECSIK VMCRFRPLNE AEILRGDKFI PKFKGEETVV IGQGKPYVFD RVLPPNTTQE
QVYNACAKQI VKDVLEGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIAHDIFDHI
YSMDENLEFH IKVSYFEIYL DKIRDLLDVS KTNLAVHEDK NRVPYVKGCT ERFVSSPEEV
MDVIDEGKAN RHVAVTNMNE HSSRSHSIFL INIKQENVET EKKLSGKLYL VDLAGSEKV
