G5EFQ4
Gene name |
klp-6 (CELE_R144.1, R144.1) |
Protein name |
Kinesin-like protein |
Names |
|
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_R144.1 |
EC number |
|
Protein Class |
STAR-RELATED LIPID TRANSFER PROTEIN 9 (PTHR47117) |

Descriptions
KLP-6's autoinhibition is mediated by a comprehensive interaction between its N-terminal motor domain and multiple coiled-coil domains. This configuration restricts the motor domain's flexibility, hindering its ability to engage with microtubules efficiently. KLP-6 autoinhibition involves a multilevel-lockdown mechanism where internal coiled-coil segments and domains cooperate to lock down the neck and motor domains, consequently blocking nucleotide access and hindering microtubule binding. This intricate process effectively suppresses motor activity.
Autoinhibitory domains (AIDs)
Target domain |
368-394 (Neck coil); 1-357 (Motor domain) |
Relief mechanism |
Partner binding |
Assay |
Structural analysis, Mutagenesis experiment |
Target domain |
1-357 (Motor domain) |
Relief mechanism |
Partner binding |
Assay |
Structural analysis, Mutagenesis experiment |
Accessory elements
No accessory elements
References
- Wang W et al. (2022) "The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition", Nature communications, 13, 4281
- Kita T et al. (2024) "Comparative analysis of two Caenorhabditis elegans kinesins KLP-6 and UNC-104 reveals a common and distinct activation mechanism in kinesin-3", eLife, 12,
Autoinhibited structure
Activated structure

1 structures for G5EFQ4
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
7WRG | X-ray | 316 A | A/B | 1-928 | PDB |
No variants for G5EFQ4
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for G5EFQ4 |
No associated diseases with G5EFQ4
Functions
Description | ||
---|---|---|
EC Number | ||
Subcellular Localization |
|
|
PANTHER Family | PTHR47117 | STAR-RELATED LIPID TRANSFER PROTEIN 9 |
PANTHER Subfamily | PTHR47117:SF3 | KINESIN FAMILY MEMBER 14-LIKE |
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
7 GO annotations of cellular component
Name | Definition |
---|---|
axon | The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter. |
dendrite | A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body. |
kinesin complex | Any complex that includes a dimer of molecules from the kinesin superfamily, a group of related proteins that contain an extended region of predicted alpha-helical coiled coil in the main chain that likely produces dimerization. The native complexes of several kinesin family members have also been shown to contain additional peptides, often designated light chains as all of the noncatalytic subunits that are currently known are smaller than the chain that contains the motor unit. Kinesin complexes generally possess a force-generating enzymatic activity, or motor, which converts the free energy of the gamma phosphate bond of ATP into mechanical work. |
microtubule | Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. |
mitochondrial membrane | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. |
neuronal cell body | The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites. |
non-motile cilium | A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors. |
5 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
ATP hydrolysis activity | Catalysis of the reaction |
microtubule binding | Binding to a microtubule, a filament composed of tubulin monomers. |
microtubule motor activity | A motor activity that generates movement along a microtubule, driven by ATP hydrolysis. |
RNA binding | Binding to an RNA molecule or a portion thereof. |
2 GO annotations of biological process
Name | Definition |
---|---|
cytoskeleton-dependent intracellular transport | The directed movement of substances along cytoskeletal fibers such as microfilaments or microtubules within a cell. |
microtubule-based movement | A microtubule-based process that results in the movement of organelles, other microtubules, or other cellular components. Examples include motor-driven movement along microtubules and movement driven by polymerization or depolymerization of microtubules. |
10 | 20 | 30 | 40 | 50 | 60 |
MGKGDSIIVA | VRVRPFNDRE | KTRNCKLVIE | MPDEETTVIR | DPKTNDEKRF | TYDHSYWSHD |
70 | 80 | 90 | 100 | 110 | 120 |
GFSEKKNGYL | EPTDPHYADQ | RRVFEDLGRG | VLANAWAGYN | CSLFAYGQTG | SGKSYSIVGF |
130 | 140 | 150 | 160 | 170 | 180 |
KNNKGIVPIV | CEELFKQIAD | NKKKNMQFEV | FVSMMEIYCE | KVRDLLSSTP | PPKGGLKVRE |
190 | 200 | 210 | 220 | 230 | 240 |
HPKNGFYVEN | LTTVPVNSFK | EIEAKIEEGT | KSRTIAATQM | NATSSRAHTI | VKITFNQKSS |
250 | 260 | 270 | 280 | 290 | 300 |
KQAGGTSMKK | SEINLVDLAG | SERQSAAGTE | GDRLKEGIVI | NQSLTTLGRV | IKALHDSQKA |
310 | 320 | 330 | 340 | 350 | 360 |
KSGKKTQIPY | RDSVLTCLLK | NALGGNSKTI | MIAAISPADI | NFEETLSTLR | FADRAKSIKT |
370 | 380 | 390 | 400 | 410 | 420 |
NAVVNENQTE | RALRELREEN | LRLQSQIQGG | TAGDASNEEI | EKLRRQLAEN | QKEMEEMEKS |
430 | 440 | 450 | 460 | 470 | 480 |
WQQKIAEEAA | KHASGASEKV | EMEAKKKKMC | HLWNLNEDPA | LTNVIVHFIP | VGESVVGNKP |
490 | 500 | 510 | 520 | 530 | 540 |
TSSGNFIQMS | GLSILPQHVT | LKNDGNNQIH | LSPCSEDLDI | FINGKPVHGE | TQLQQNDRVF |
550 | 560 | 570 | 580 | 590 | 600 |
FGGNHLYVFN | NPTKKGIRTD | ITYENAQAEI | AQNHAAALGN | RGLGGGSKRD | LILEEELMST |
610 | 620 | 630 | 640 | 650 | 660 |
LPLVQRANAM | ATELGRNVKF | EIVLVSPEMR | GLTSGLTEIW | VKVHNISEDT | YFLWEKSRFM |
670 | 680 | 690 | 700 | 710 | 720 |
NRYYGMQEMY | EAKQDGSEDW | NMPKERDPFY | EPPDSPVFIA | SSVVFLQSLA | YLIDVEEQFP |
730 | 740 | 750 | 760 | 770 | 780 |
IVDLSGQEIG | LLTVGLSPCS | TTGKELRGEY | VEDPDQLIGK | NIAFKVKVIS | AVGLPRRILK |
790 | 800 | 810 | 820 | 830 | 840 |
SNCKYRFFGS | KKMTTTATVS | GNTPAYGHEE | TFQFKPVTKE | VADYLANSNL | YITFWGTQRP |
850 | 860 | 870 | 880 | 890 | 900 |
RGASSRKNSI | STIGSNEARE | GPNKAKRVER | LVHQAKTSEN | RNISVKALET | VLKGVDDNEN |
910 | 920 | ||||
RKTRKQSMKK | AGSTTIKSRS | GSKKPKAK |