Descriptions
Kinesin (KIF) motor proteins play a major role in the transport of intracellular cargo and in the regulation of microtubule (MT) organization and dynamics in an ATP-dependent fashion. A prototypic kinesin includes a conserved globular N-terminal motor domain, which binds to MTs, hydrolyses ATP and converts its chemical energy to mechanical work. The kinesin motor domain is typically followed by a stalk domain often consisting of α-helical coiled-coil regions that are important for dimerization and a tail domain containing the binding sites for cargo or kinesin-regulatory proteins.
In human KIF21A, the intramolecular antiparallel coiled coil in the stalk domain autoinhibits the kinesin motor domain, preventing its interaction with microtubules (MTs) and ATP hydrolysis, thus regulating intracellular transport and MT dynamics. Interaction of the KIF21A regulatory domain with the KIF21B motor domain and sequence similarities to KIF7 and KIF27 strongly suggest a conservation of this regulatory mechanism in other kinesin-4 family members.
Autoinhibitory domains (AIDs)
Target domain |
3-379 (Kinesin motor domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
0 structures for A0A8M3AWT6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for A0A8M3AWT6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A0A8M3AWT6 | |||||
No associated diseases with A0A8M3AWT6
9 regional properties for A0A8M3AWT6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | WD40 repeat | 1256 - 1334 | IPR001680-1 |
| repeat | WD40 repeat | 1358 - 1396 | IPR001680-2 |
| repeat | WD40 repeat | 1399 - 1441 | IPR001680-3 |
| repeat | WD40 repeat | 1449 - 1487 | IPR001680-4 |
| repeat | WD40 repeat | 1490 - 1530 | IPR001680-5 |
| repeat | WD40 repeat | 1533 - 1570 | IPR001680-6 |
| domain | Kinesin motor domain | 3 - 379 | IPR001752 |
| conserved_site | WD40 repeat, conserved site | 1280 - 1294 | IPR019775 |
| conserved_site | Kinesin motor domain, conserved site | 268 - 279 | IPR019821 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
4 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. |
2 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. |
| system development | The process whose specific outcome is the progression of an organismal system over time, from its formation to the mature structure. A system is a regularly interacting or interdependent group of organs or tissues that work together to carry out a given biological process. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDDSTVRVAL | RIRPQLAKEK | IEGCHICTFV | MPDEPQVVLG | KDKAFTYDYV | FDMDSTQDNI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YSNCTEKLIE | GCFEGYNATI | FAYGQTGSGK | TYTMGTGFDV | AIPDEDLGII | PRAVTHLFKG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IEQRRQQAAE | QSRPVPEFKI | SAQFLELYNE | EVLDLFDTTR | DMESRKQKSH | IKIHEDASGG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IYTVGVTTRN | VSSEAEMMQC | LKLGALSRTT | ASTQMNVQSS | RSHAIFTIHI | CQIRVCAPAD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SPPEQDNETD | NRLAGSSSEM | EEFETLTAKF | HFVDLAGSER | LKRTGATGER | AKEGISINCG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLALGNVISA | LGDRSKRSTH | VPYRDSKLTR | LLQDSLGGNS | RTVMIACISP | SDQDFMETLN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TLKYANRARN | IKNKVMVNQD | RASQQISALR | TEIARLQMEL | MEYRTGKRMV | GEDGLESIND |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MFHENSMLQV | ENNNLRMRVK | AMQEAIDAQG | ARLTQLLSQQ | ANQLLARAGE | GSEEIGNMIQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NYIKEIEDLR | AKLLESEAVN | ENLRRNLTRA | SSRPQFYGAS | GSFSTALLGP | DPSQETSDII |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EIAKKDLEKL | KRREKKKKKR | LQQLLADKRD | EDEDEEEEVE | EDSANKDETQ | EDGEQKTEKE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| QSESTNQEPE | MEASDREEGD | GEEDEEDVEE | EEMEAEESSE | ETDSELDEKE | DFQADLANIT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| CEIAIKQKLI | DELENSQRRL | HTLKQQYEHK | LMMLQSKIRD | TQLERDRVLH | SMGSVESCSE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DKTKRIKAEY | EKKLSVMNKE | LQKLQAAQKE | HARLLKNQSQ | YEKQLKKLQL | DLTEMKKTKV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| RLMKQMKEQQ | EKSRMAESRR | NREIATLKKD | QRKQEHQLKL | LEAQKRQQEL | ILRRKTEEVT |
| 850 | 860 | 870 | 880 | 890 | 900 |
| ALRRQVRPIS | GKVTRKANLS | EPNFDLSHRP | PAGRTYGSGA | PNGTRLYHRR | AAGIYSTRVA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| RGKWQSLERR | ISDIIMQRMT | ISNMEADMNR | LLKQREELTR | RRDKISRKRE | RLLADDPEVE |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| KHLQPVNEEL | ESLLANIDYI | NDSISDCQAN | IMQMEEAKEE | GDAVDVSAVI | SSCTLAEARF |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| LLDHFMSMAL | NKGLQAAQKE | SQIKVMEGRL | KQTEINSATQ | NQLLFHMLKE | KAEFNPELDA |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| LLGNALQENG | DDSSSDESTP | SPAVEGNTLA | SDLMKLCGET | KSRTKARRRT | TTQMELLYVD |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| SGQDAATKDF | TIPLHPMAET | SEGSGELESA | GNTVRDRDYM | PSPAGLTSRM | GGISSSGNRF |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| PAGGQKRLPE | PSPLSRRKTY | DKGQAQADKA | KSKEILQGII | NPVPVWKSAR | GGGGGTLQCV |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| HVAEGHSKAV | LCVESTDDLM | FTGSKDRTCK | VWNLVTGQEI | MSLGGHPNNV | VSVRYSSSLV |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| FTVSTSYIKV | WDIRDSAKCI | RTLTSSGLVN | TGDMCAASTN | RTVTIPAGEN | QINQIYLNPS |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| GTVLYAAAGN | SVRVWDLRRF | VCTGKLTGHL | GPVMCLTVDQ | TGNGQDLVIT | GSKDHYIKMF |
| 1450 | 1460 | 1470 | 1480 | 1490 | 1500 |
| DVTEGAMGSI | SPTHNFEPPH | YDGIESLVVQ | GDCLFSGSRD | NGIKKWDLTR | KDLLQQVPNA |
| 1510 | 1520 | 1530 | 1540 | 1550 | 1560 |
| HRDWVCALGV | VPASAILLSG | CRAGVLKLWH | TDTLSPLGEI | RGHESPINSI | STNSTHLFTA |
| 1570 | 1580 | 1590 | |||
| ADDRTVKIWR | ARGSLDGSAD | VGDTMEEGVS | N |