O88448
Gene name |
Klc2 |
Protein name |
Kinesin light chain 2 |
Names |
KLC 2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
|
EC number |
|
Protein Class |
KINESIN LIGHT CHAIN (PTHR45783) |
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 |
196-480 (Cargo binding site on the TPR domain) |
Relief mechanism |
Partner binding |
Assay |
Mutagenesis experiment, Split protein assay, Structural analysis |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
4 structures for O88448
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3ZFW | X-ray | 290 A | A/B | 217-478 | PDB |
| 5FJY | X-ray | 400 A | A/B/C | 160-478 | PDB |
| 6EJN | X-ray | 320 A | A/B | 190-477 | PDB |
| AF-O88448-F1 | Predicted | AlphaFoldDB |
No variants for O88448
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O88448 | |||||
No associated diseases with O88448
5 regional properties for O88448
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Kinesin light chain repeat | 264 - 305 | IPR015792 |
| repeat | Tetratricopeptide repeat | 239 - 272 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 281 - 314 | IPR019734-2 |
| repeat | Tetratricopeptide repeat | 323 - 356 | IPR019734-3 |
| repeat | Tetratricopeptide repeat | 365 - 398 | IPR019734-4 |
Functions
| Description | ||
|---|---|---|
| EC Number | ||
| Subcellular Localization |
|
|
| PANTHER Family | PTHR45783 | KINESIN LIGHT CHAIN |
| PANTHER Subfamily | PTHR45783:SF2 | KINESIN LIGHT CHAIN 2 |
| PANTHER Protein Class |
cytoskeletal protein
microtubule binding motor protein microtubule or microtubule-binding cytoskeletal protein |
|
| PANTHER Pathway Category |
Alzheimer disease-amyloid secretase pathway kinesin |
|
11 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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. |
| lysosomal membrane | The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm. |
| 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. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
1 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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| axo-dendritic transport | The directed movement of organelles or molecules along microtubules in neuron projections. |
| lysosome localization | Any process in which a lysosome is transported to, and/or maintained in, a specific location. |
| 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. |
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 |
| Q07866 | KLC1 | Kinesin light chain 1 | Homo sapiens (Human) | SS |
| Q9H0B6 | KLC2 | Kinesin light chain 2 | Homo sapiens (Human) | SS |
| O88447 | Klc1 | Kinesin light chain 1 | Mus musculus (Mouse) | SS |
| Q91W40 | Klc3 | Kinesin light chain 3 | Mus musculus (Mouse) | SS |
| Q9DBS5 | Klc4 | Kinesin light chain 4 | Mus musculus (Mouse) | SS |
| P37285 | Klc1 | Kinesin light chain 1 | Rattus norvegicus (Rat) | SS |
| Q5PQM2 | Klc4 | Kinesin light chain 4 | Rattus norvegicus (Rat) | SS |
| Q68G30 | Klc3 | Kinesin light chain 3 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATMVLPREE | KLSQDEIVLG | TKAVIQGLET | LRGEHRALLA | PLASHEAGEA | EPGSQERCLL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LRRSLEAIEL | GLGEAQVILA | LSSHLGAVES | EKQKLRAQVR | RLVQENQWLR | EELAGTQQKL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QRSEQAVAQL | EEEKQHLLFM | SQIRKLDEML | PQEEKGDVPK | DSLDDLFPNE | DEQSPAPSPG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GGDVAAQHGG | YEIPARLRTL | HNLVIQYASQ | GRYEVAVPLC | KQALEDLEKT | SGHDHPDVAT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MLNILALVYR | DQNKYKDAAH | LLNDALAIRE | KTLGKDHPAV | AATLNNLAVL | YGKRGKYKEA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EPLCKRALEI | REKVLGKFHP | DVAKQLSNLA | LLCQNQGKAE | EVEYYYRRAL | EIYATRLGPD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DPNVAKTKNN | LASCYLKQGK | YQDAETLYKE | ILTRAHEKEF | GSVNGENKPI | WMHAEEREES |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KDKRRDRRPM | EYGSWYKACK | VDSPTVNTTL | RTLGALYRPE | GKLEAAHTLE | DCASRSRKQG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LDPASQTKVV | ELLKDGSGRG | HRRGSRDVAG | PQSESDLEES | GPAAEWSGDG | SGSLRRSGSF |
| 550 | 560 | 570 | 580 | 590 | |
| GKLRDALRRS | SEMLVRKLQG | GGPQEPNSRM | KRASSLNFLN | KSVEEPVQPG | GRVFLTAAL |