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Protein

Kinesin heavy chain isoform 5A

Gene

Kif5a

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

Functioni

Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi86 – 93ATP8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent microtubule motor activity, plus-end-directed Source: GO_Central
  • microtubule binding Source: InterPro
  • microtubule motor activity Source: RGD
  • protein complex binding Source: RGD
  • scaffold protein binding Source: RGD

GO - Biological processi

  • axon guidance Source: GO_Central
  • cellular response to ethanol Source: RGD
  • cellular response to nerve growth factor stimulus Source: RGD
  • cerebral cortex development Source: RGD
  • cytoskeleton-dependent intracellular transport Source: GO_Central
  • hippocampus development Source: RGD
  • microtubule-based movement Source: GO_Central
  • microtubule-based process Source: RGD
  • neuron development Source: RGD
  • protein localization Source: GO_Central
  • response to rotenone Source: RGD
  • thalamus development Source: RGD
  • vesicle-mediated transport Source: UniProtKB

Keywordsi

Molecular functionMotor protein
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin heavy chain isoform 5A
Alternative name(s):
Kinesin heavy chain neuron-specific 1
Neuronal kinesin heavy chain
Short name:
NKHC
Gene namesi
Name:Kif5aImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1303035. Kif5a.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002511432 – 1027Kinesin heavy chain isoform 5AAdd BLAST1026

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei397PhosphothreonineBy similarity1
Modified residuei931PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6QLM7.
PRIDEiQ6QLM7.

Expressioni

Tissue specificityi

Expressed in brain.1 Publication

Interactioni

Subunit structurei

Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1. Interacts with FMR1 (via C-terminus); this interaction is increased in a mGluR-dependent manner. Interacts with BORCS5. Interacts with ZFYVE27. Interacts with VAPA, VAPB, SURF4, RAB11A (GDP-bound form), RAB11B (GDP-bound form) and RTN3 in a ZFYVE27-dependent manner. Interacts with BICD2.By similarity

GO - Molecular functioni

  • microtubule binding Source: InterPro
  • protein complex binding Source: RGD
  • scaffold protein binding Source: RGD

Protein-protein interaction databases

CORUMiQ6QLM7.
DIPiDIP-46364N.
IntActiQ6QLM7. 1 interactor.
STRINGi10116.ENSRNOP00000007721.

Structurei

Secondary structure

11027
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi254 – 256Combined sources3
Helixi257 – 271Combined sources15
Helixi279 – 281Combined sources3
Helixi283 – 287Combined sources5
Helixi289 – 293Combined sources5
Beta strandi294 – 304Combined sources11
Helixi308 – 310Combined sources3
Helixi311 – 325Combined sources15
Beta strandi328 – 331Combined sources4
Beta strandi334 – 336Combined sources3
Helixi339 – 350Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KINX-ray2.00B252-351[»]
3KINX-ray3.10B/D256-372[»]
ProteinModelPortaliQ6QLM7.
SMRiQ6QLM7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6QLM7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 327Kinesin motorPROSITE-ProRule annotationAdd BLAST319

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni174 – 315Microtubule-bindingSequence analysisAdd BLAST142
Regioni271 – 361Necessary for interaction with ZFYVE27By similarityAdd BLAST91
Regioni353 – 1027Interaction with BICD2By similarityAdd BLAST675
Regioni907 – 1027GlobularSequence analysisAdd BLAST121

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili331 – 905Sequence analysisAdd BLAST575

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.Curated

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0240. Eukaryota.
COG5059. LUCA.
HOGENOMiHOG000216718.
HOVERGENiHBG006210.
InParanoidiQ6QLM7.
KOiK10396.
PhylomeDBiQ6QLM7.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiView protein in InterPro
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF00225. Kinesin. 1 hit.
PRINTSiPR00380. KINESINHEAVY.
SMARTiView protein in SMART
SM00129. KISc. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS50067. KINESIN_MOTOR_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6QLM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETNNECSI KVLCRFRPLN QAEILRGDKF IPIFQGDDSV IIGGKPYVFD
60 70 80 90 100
RVFPPNTTQE QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL
110 120 130 140 150
HDPQLMGIIP RIARDIFNHI YSMDENLEFH IKVSYFEIYL DKIRDLLDVT
160 170 180 190 200
KTNLSVHEDK NRVPFVRGCT ERFVSSPEEI LDVIDEGKSN RHVAVTNMNE
210 220 230 240 250
HSSRSHSIFL INIKQENIET EQKLSGKLYL ADLAGSEKVS KTGAEGAVLD
260 270 280 290 300
EAKNINKSLS ALGNVISALA EGTKSYVPYR DSKMTRILQD SLGGNCRTTM
310 320 330 340 350
FICCSPSSYN DAETKSTLMF GQRAKTIKNT ASVNLELTAE QWKKKYEKEK
360 370 380 390 400
EKTKAQKETI AKLEAELSRW RNGENVPETE RLAGEDSALA AEICEETPVN
410 420 430 440 450
DNSSIVVRIA PEERQKYEEE IRRLYKQLDD KDDEINQQSQ LIEKLKQQML
460 470 480 490 500
DQEELLVSTR GDNEKVQREL SHLQSENDAA KEEVKEVLQA LEELAVNYDQ
510 520 530 540 550
KSQEVEEKSQ QNQLLVDELS QKVATMLSLE SEPQRLQEVS GHQRKRIAEV
560 570 580 590 600
LNGLMKDLSE FSVIVGNGEI KLPVEISGAI EEEFTVARLY ISKIKSEVKS
610 620 630 640 650
VVKRCRQLEN LQVECHRKME VTGRELSSCQ LLISQHEAKI RSLTEYMQTV
660 670 680 690 700
ELKKRHLEES YDSLSDELAK LQAQETVHEV ALKDKEPDTQ DAEEVKKALE
710 720 730 740 750
LQMENHREAH HRQLARLRDE INEKQKTIDE LKDLDQKLQL ELEKLQADYE
760 770 780 790 800
RLKNEENEKS AKLQELTFLY ERHEQSKQDL KGLEETVARE LQTLHNLRKL
810 820 830 840 850
FVQDVTTRVK KSAEMEPEDS GGIHSQKQKI SFLENNLEQL TEVHKQLVRD
860 870 880 890 900
NADLRCELPK LEKRLRATAE RVKALEGALK EAKEGAMKDK RRYQQEVDRI
910 920 930 940 950
KEAVRYKSSG KRGHSAQIAK PVRPGHYPAS SPTNPYGTRS PECISYTNNL
960 970 980 990 1000
FQNYQNLHLQ AAPSSTSDVY FASNGATSVA PLASYQKANT DNGNATDIND
1010 1020
NRSDLPCGYE AEDPAKLFPL HQETAAS
Length:1,027
Mass (Da):116,916
Last modified:July 5, 2004 - v1
Checksum:i2068CCC4E05A24CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY535015 mRNA. Translation: AAS45402.1.
RefSeqiNP_997688.1. NM_212523.1.
UniGeneiRn.63144.

Genome annotation databases

GeneIDi314906.
KEGGirno:314906.
UCSCiRGD:1303035. rat.

Similar proteinsi

Entry informationi

Entry nameiKIF5A_RAT
AccessioniPrimary (citable) accession number: Q6QLM7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 5, 2004
Last modified: September 27, 2017
This is version 98 of the entry and version 1 of the sequence. See 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