Q9DBS5
SS
Gene name |
Klc4 (Knsl8) |
Protein name |
Kinesin light chain 4 |
Names |
KLC 4 , Kinesin-like protein 8 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:74764 |
EC number |
|
Protein Class |
|
Descriptions
Engulfment and cell motility (ELMO) proteins bind a subset of DOCK members and act as critical regulators of Rac signaling. Although formation of a DOCK180/ELMO complex is not essential for Rac1 activation, ELMO mutants deficient in binding to DOCK180 are unable to promote cytoskeleton remodeling. ELMO facilitates the co-localization of DOCK180 and Rac at the membrane and therefore indirectly endorses the Rac GEF activity of this complex. ELMO is autoinhibited via an intramolecular interaction between the N-terminal Armadillo repeats (ARMs, renamed ELMO Inhibitory Domain (EID)) and the C-terminal region termed the ELMO Autoregulatory Domain (EAD). Relief of ELMO autoinhibition occurs through cell stimulation and ELMO Ras-binding domain (RBD) engagement (via a GTPase or other unknown binding partner). Cell stimulation leads to ELMO conformational changes that facilitate DOCK180/ELMO interactions, which in turn enhances the Rac GEF activity in DOCK180.
Autoinhibitory domains (AIDs)
Target domain |
210-497 (Cargo binding site on the TPR domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9DBS5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9DBS5-F1 | Predicted | AlphaFoldDB |
32 variants for Q9DBS5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389466913 | 69 | R>W | No | EVA | |
| rs3389467566 | 73 | R>P | No | EVA | |
| rs3389467541 | 108 | Q>* | No | EVA | |
| rs3389477724 | 110 | R>W | No | EVA | |
| rs3389466890 | 138 | A>T | No | EVA | |
| rs3389380158 | 153 | L>P | No | EVA | |
| rs3389426362 | 164 | E>* | No | EVA | |
| rs3389416045 | 165 | E>V | No | EVA | |
| rs3389470900 | 167 | E>G | No | EVA | |
| rs3389462762 | 182 | E>D | No | EVA | |
| rs3389484650 | 193 | R>H | No | EVA | |
| rs3389457715 | 260 | A>D | No | EVA | |
| rs3389457782 | 267 | N>I | No | EVA | |
| rs3389416069 | 273 | A>D | No | EVA | |
| rs3407812349 | 280 | L>H | No | EVA | |
| rs3407674018 | 280 | L>V | No | EVA | |
| rs3389467231 | 286 | T>P | No | EVA | |
| rs3389467522 | 295 | A>V | No | EVA | |
| rs3389446981 | 302 | A>T | No | EVA | |
| rs3389470894 | 304 | L>R | No | EVA | |
| rs3389380153 | 309 | G>C | No | EVA | |
| rs864278905 | 336 | V>E | No | EVA | |
| rs3389484661 | 363 | A>V | No | EVA | |
| rs3389484686 | 379 | A>D | No | EVA | |
| rs3389446979 | 393 | G>D | No | EVA | |
| rs3389475786 | 437 | S>R | No | EVA | |
| rs3389416029 | 438 | R>W | No | EVA | |
| rs3389457692 | 440 | R>H | No | EVA | |
| rs3389470921 | 460 | S>N | No | EVA | |
| rs3389462827 | 571 | R>M | No | EVA | |
| rs49199340 | 588 | A>S | No | EVA | |
| rs3389466837 | 619 | S>G | No | EVA |
No associated diseases with Q9DBS5
3 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. |
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. |
1 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. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q2TBQ9 | KLC3 | Kinesin light chain 3 | Bos taurus (Bovine) | SS |
| Q2HJJ0 | KLC4 | Kinesin light chain 4 | Bos taurus (Bovine) | SS |
| P46824 | Klc | Kinesin light chain | Drosophila melanogaster (Fruit fly) | 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 |
| Q9NSK0 | KLC4 | Kinesin light chain 4 | Homo sapiens (Human) | SS |
| Q91W40 | Klc3 | Kinesin light chain 3 | Mus musculus (Mouse) | SS |
| O88447 | Klc1 | Kinesin light chain 1 | Mus musculus (Mouse) | SS |
| O88448 | Klc2 | Kinesin light chain 2 | Mus musculus (Mouse) | EV |
| P37285 | Klc1 | Kinesin light chain 1 | Rattus norvegicus (Rat) | SS |
| Q68G30 | Klc3 | Kinesin light chain 3 | Rattus norvegicus (Rat) | SS |
| Q5PQM2 | Klc4 | Kinesin light chain 4 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPPPSDIVKV | AIEWPGAYPK | LMEIDQKKPL | SAIIKEVCDG | WSLANHEYFA | LQHADSSNFY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ITEKNRNEIK | NGTILRLTTS | PAQNAQQLHE | RIQSSSMDAK | LEALKDLASL | SRDVTFAQEF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| INLDGISLLT | QMVESGTERY | QKLQKIMKPC | FGDMLSFTLT | AFVELMDHGI | VSWDTFSVAF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IKKIASFVNK | SAIDISILQR | SLAILESMVL | NSHDLYQKVA | QEITIGQLIP | HLQGTDQEIQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TYTIAVINAL | FLKAPDERRQ | EMANILAQKQ | LRYIILTHVI | RAQRAINNEM | AHQLYVLQVL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TFNLLEDRMM | TKMDPQDQAQ | RDIIFELRRI | AFDAESEPNN | SSGSMEKRKS | MYTRDYKKLG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FINHVNPAMD | FTQTPPGMLA | LDNMLYFAKH | HQDAYIRIVL | ENSSREDKHE | CPFGRSSIEL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TKMLCEILKV | GELPSETCND | FHPMFFTHDR | SFEEFFCICI | QLLNKTWKEM | RATSEDFNKV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| MQVVKEQVMR | ALTTKPSSLD | QFKSKLQNLS | YTEILKIRQS | ERMNQEDFQS | RPILELKEKI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QPEILELIKQ | QRLNRLVEGT | CFRKLNARRR | QDKFWYCRLS | PNHKVLHYGD | LEESPQGEVP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| HDSLQDKLPV | ADIKAVVTGK | DCPHMKEKGA | LKQNKEVLEL | AFSILYDSNC | QLNFIAPDKH |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EYCIWTDGLN | ALLGKDMMSD | LTRNDLDTLL | SMEIKLRLLD | LENIQIPDAP | PPIPKEPSNY |
| DFVYDCN |