Descriptions
The Kinesin-1 light chains (KLCs) exhibit autoinhibition through an intramolecular interaction between the TPR domain and a highly conserved peptide motif within an unstructured region, occluding a key cargo binding site. Cargo binding displaces this interaction, leading to a global conformational change in the KLCs, resulting in a more extended conformation which is essential for the regulation of the motor activity.
Autoinhibitory domains (AIDs)
Target domain |
210-496 (Cargo binding site on the TPR domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
3 structures for O88447
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6FUZ | X-ray | 270 A | A | 199-495 | PDB |
| 6FV0 | X-ray | 229 A | A | 204-495 | PDB |
| AF-O88447-F1 | Predicted | AlphaFoldDB |
No variants for O88447
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O88447 | |||||
No associated diseases with O88447
6 regional properties for O88447
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Tetratricopeptide repeat | 211 - 244 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 253 - 286 | IPR019734-2 |
| repeat | Tetratricopeptide repeat | 295 - 328 | IPR019734-3 |
| repeat | Tetratricopeptide repeat | 337 - 370 | IPR019734-4 |
| repeat | Tetratricopeptide repeat | 380 - 413 | IPR019734-5 |
| repeat | Tetratricopeptide repeat | 463 - 496 | IPR019734-6 |
13 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. |
| ciliary rootlet | A cytoskeleton-like structure, originating from the basal body at the proximal end of a cilium, and extending proximally toward the cell nucleus. Rootlets are typically 80-100 nm in diameter and contain cross striae distributed at regular intervals of approximately 55-70 nm. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoplasmic vesicle | A vesicle found in the cytoplasm of a cell. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| growth cone | The migrating motile tip of a growing neuron projection, where actin accumulates, and the actin cytoskeleton is the most dynamic. |
| 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. |
| membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
| 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. |
| neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
| neuronal cell body | The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites. |
| vesicle | Any small, fluid-filled, spherical organelle enclosed by membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| kinesin binding | Interacting selectively and non-covalently and stoichiometrically with kinesin, a member of a superfamily of microtubule-based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation. |
| tubulin binding | Binding to monomeric or multimeric forms of tubulin, including microtubules. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| axo-dendritic transport | The directed movement of organelles or molecules along microtubules in neuron projections. |
| cell adhesion | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. |
| intracellular protein transport | The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic 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. |
| protein localization to synapse | Any process in which a protein is transported to, and/or maintained at the synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell. |
| stress granule disassembly | The disaggregation of a stress granule into its constituent protein and RNA parts. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q2HJJ0 | KLC4 | Kinesin light chain 4 | Bos taurus (Bovine) | SS |
| Q2TBQ9 | KLC3 | Kinesin light chain 3 | Bos taurus (Bovine) | SS |
| P46824 | Klc | Kinesin light chain | Drosophila melanogaster (Fruit fly) | SS |
| Q9NSK0 | KLC4 | Kinesin light chain 4 | Homo sapiens (Human) | SS |
| Q6P597 | KLC3 | Kinesin light chain 3 | Homo sapiens (Human) | SS |
| Q9H0B6 | KLC2 | Kinesin light chain 2 | Homo sapiens (Human) | SS |
| Q07866 | KLC1 | Kinesin light chain 1 | Homo sapiens (Human) | SS |
| O88448 | Klc2 | Kinesin light chain 2 | Mus musculus (Mouse) | EV |
| Q91W40 | Klc3 | Kinesin light chain 3 | Mus musculus (Mouse) | SS |
| Q9DBS5 | Klc4 | Kinesin light chain 4 | Mus musculus (Mouse) | SS |
| Q5PQM2 | Klc4 | Kinesin light chain 4 | Rattus norvegicus (Rat) | SS |
| Q68G30 | Klc3 | Kinesin light chain 3 | Rattus norvegicus (Rat) | SS |
| P37285 | Klc1 | Kinesin light chain 1 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MYDNMSTMVY | IKEEKLENVT | QDEIISKTKQ | VIQGLEALKN | EHNSILQSLL | ETLKCLKKDD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ESNLVEEKSS | MIRKSLEMLE | LGLSEAQVMM | ALSNHLNAVE | SEKQNVRAQV | RRLCQENQWL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RDELANTQQK | LQKSEQSVAQ | LEEEKKHLEF | MNQLKKYDDD | ISPSEDKDSD | SSKEPLDDLF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PNDEDEPGQG | IQHSDSSAAA | ARQGYEIPAR | LRTLHNLVIQ | YASQGRYEVA | VPSCKQALED |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LEKTSGHDHP | DVATMLNILA | LVYRDQNKYK | DAANLLNDAL | AIREKTLGRD | HPAVAATLNN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LAVLYGKRGK | YKEAEPLCKR | ALEIREKVLG | KDHPDVAKQL | NNLALLCQNQ | GKYEEVEYYY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QRALGIYQTK | LGPDRTPNVA | KTKNNLASCY | LKQGKFKQAE | TLYKEILTRA | HEAEFGSVDD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ENKPIWMHAE | EREECKGKQK | DGSAFGEYGG | WYKACKVDSP | TVTTTLKNLG | ALYRRQGKFE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AAETLEEAAM | RSRKQGLDNV | HKQRVAEVLN | DPESMEKRRS | RESLNMDVVK | YESGPDGGEE |
| A |