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Protein

Kinesin heavy chain isoform 5C

Gene

Kif5c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mediates dendritic trafficking of mRNAs (By similarity). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi86 – 938ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin heavy chain isoform 5C
Alternative name(s):
Kinesin heavy chain neuron-specific 2
Gene namesi
Name:Kif5c
Synonyms:Nkhc2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1308539. Kif5c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›239›239Kinesin heavy chain isoform 5CPRO_0000125357Add
BLAST

Proteomic databases

PeptideAtlasiP56536.
PRIDEiP56536.

Interactioni

Subunit structurei

Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and KLC3. Interacts with TRAK1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
RHOT1Q8IXI25EBI-994504,EBI-1396430From a different organism.

GO - Molecular functioni

  • apolipoprotein receptor binding Source: RGD

Protein-protein interaction databases

IntActiP56536. 7 interactions.
MINTiMINT-1529693.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi10 – 156Combined sources
Helixi20 – 245Combined sources
Beta strandi31 – 344Combined sources
Turni35 – 373Combined sources
Beta strandi38 – 414Combined sources
Beta strandi50 – 534Combined sources
Helixi59 – 668Combined sources
Helixi68 – 758Combined sources
Beta strandi79 – 857Combined sources
Helixi92 – 965Combined sources
Turni103 – 1053Combined sources
Helixi108 – 12114Combined sources
Beta strandi127 – 13913Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi172 – 1743Combined sources
Helixi177 – 19216Combined sources
Helixi198 – 2047Combined sources
Beta strandi205 – 21713Combined sources
Turni218 – 2203Combined sources
Beta strandi223 – 23210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KINX-ray2.00A2-239[»]
3KINX-ray3.10A/C2-239[»]
ProteinModelPortaliP56536.
SMRiP56536. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56536.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – ›239›232Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – ›239›66Microtubule-bindingAdd
BLAST

Domaini

Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000216718.
HOVERGENiHBG103852.
InParanoidiP56536.
PhylomeDBiP56536.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P56536-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPAECSIK VMCRFRPLNE AEILRGDKFI PKFKGEETVV IGQGKPYVFD
60 70 80 90 100
RVLPPNTTQE QVYNACAKQI VKDVLEGYNG TIFAYGQTSS GKTHTMEGKL
110 120 130 140 150
HDPQLMGIIP RIAHDIFDHI YSMDENLEFH IKVSYFEIYL DKIRDLLDVS
160 170 180 190 200
KTNLAVHEDK NRVPYVKGCT ERFVSSPEEV MDVIDEGKAN RHVAVTNMNE
210 220 230
HSSRSHSIFL INIKQENVET EKKLSGKLYL VDLAGSEKV
Length:239
Mass (Da):27,165
Last modified:January 23, 2007 - v2
Checksum:iC96C5FFE4F8E1D7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei239 – 2391

Sequence databases

UniGeneiRn.50843.

Genome annotation databases

UCSCiRGD:1308539. rat.

Cross-referencesi

Sequence databases

UniGeneiRn.50843.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KINX-ray2.00A2-239[»]
3KINX-ray3.10A/C2-239[»]
ProteinModelPortaliP56536.
SMRiP56536. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP56536. 7 interactions.
MINTiMINT-1529693.

Proteomic databases

PeptideAtlasiP56536.
PRIDEiP56536.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:1308539. rat.

Organism-specific databases

RGDi1308539. Kif5c.

Phylogenomic databases

HOGENOMiHOG000216718.
HOVERGENiHBG103852.
InParanoidiP56536.
PhylomeDBiP56536.

Miscellaneous databases

EvolutionaryTraceiP56536.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Kinesin light-chain KLC3 expression in testis is restricted to spermatids."
    Junco A., Bhullar B., Tarnasky H.A., van der Hoorn F.A.
    Biol. Reprod. 64:1320-1330(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLC3.
  2. "X-ray structure of motor and neck domains from rat brain kinesin."
    Sack S., Mueller J., Marx A., Thormaehlen M., Mandelkow E.M., Brady S.T., Mandelkow E.
    Biochemistry 36:16155-16165(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY OF 2-239 (1.9 ANGSTROMS).
    Tissue: Brain.
  3. "The crystal structure of dimeric kinesin and implications for microtubule-dependent motility."
    Kozielski F., Sack S., Marx A., Thormahlen M., Schonbrunn E., Biou V., Thompson A., Mandelkow E.M., Mandelkow E.
    Cell 91:985-994(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY OF 2-239 (3.1 ANGSTROMS).

Entry informationi

Entry nameiKIF5C_RAT
AccessioniPrimary (citable) accession number: P56536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.