Q2TBQ9
SS
Gene name |
KLC3 |
Protein name |
Kinesin light chain 3 |
Names |
|
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:517633 |
EC number |
|
Protein Class |
|
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 |
206-438 (Cargo binding site on the TPR domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q2TBQ9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2TBQ9-F1 | Predicted | AlphaFoldDB |
No variants for Q2TBQ9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2TBQ9 | |||||
No associated diseases with Q2TBQ9
4 regional properties for Q2TBQ9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Tetratricopeptide repeat | 249 - 282 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 291 - 324 | IPR019734-2 |
| repeat | Tetratricopeptide repeat | 333 - 366 | IPR019734-3 |
| repeat | Tetratricopeptide repeat | 375 - 408 | IPR019734-4 |
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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. |
| 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. |
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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| sperm mitochondrial sheath assembly | The assembly and organization of the sperm mitochondrial sheath, the tightly packed helical sheath of ATP-producing mitochondria restricted to the midpiece of the sperm flagellum. |
| spermatid development | The process whose specific outcome is the progression of a spermatid over time, from its formation to the mature structure. |
| spermatogenesis | The developmental process by which male germ line stem cells self renew or give rise to successive cell types resulting in the development of a spermatozoa. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q2HJJ0 | KLC4 | Kinesin light chain 4 | Bos taurus (Bovine) | SS |
| P46824 | Klc | Kinesin light chain | Drosophila melanogaster (Fruit fly) | SS |
| Q9NSK0 | KLC4 | Kinesin light chain 4 | Homo sapiens (Human) | SS |
| Q9H0B6 | KLC2 | Kinesin light chain 2 | Homo sapiens (Human) | SS |
| Q07866 | KLC1 | Kinesin light chain 1 | Homo sapiens (Human) | SS |
| Q6P597 | KLC3 | Kinesin light chain 3 | Homo sapiens (Human) | SS |
| Q9DBS5 | Klc4 | Kinesin light chain 4 | Mus musculus (Mouse) | SS |
| O88447 | Klc1 | Kinesin light chain 1 | Mus musculus (Mouse) | SS |
| O88448 | Klc2 | Kinesin light chain 2 | Mus musculus (Mouse) | EV |
| Q91W40 | Klc3 | Kinesin light chain 3 | 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 |
| MSVQVAAPGG | LGLGLERPSP | EELVRQTRQV | VKGLEALRAE | HRGLAGHLAE | ALAAQGPAAG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LELLEEKQQV | VSHSLEAIEL | GLGEAQVLLA | LSAHVGALEA | EKQRLRAQAR | RLAQENAWLR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EELEETQRRL | RASEEAVAQL | EEEKSHLEFL | GQLRQYDPPA | ESQQPESPPR | RDSLASLFPS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EEEERRGPEA | VGAAAAQQGG | YEIPARLRTL | HNLVIQYAGQ | GRYEVAVPLC | RQALEDLERS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SGHCHPDVAT | MLNILALVYR | DQNKYKEATD | LLHDALQIRE | QTLGPEHPAV | AATLNNLAVL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YGKRGRYREA | EPLCQRALEI | REKVLGADHP | DVAKQLNNLA | LLCQNQGKFE | EVERHYARAL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SIYEALGGPH | DPNVAKTKNN | LASAYLKQNK | YQQAEELYKE | ILHREALPAP | LGAPNTGTTS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DTQQQTLSRS | SSFSKLRESI | RRGSEKLVSR | LRGEGAAGAA | GMKRAMSLSM | LNTDGSRAPE |
| 490 | 500 | ||||
| NQFPRQHLSE | ASRTLSTSTQ | DLGPR |