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

185-470 (Cargo binding site on the TPR domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P46824

Entry ID Method Resolution Chain Position Source
AF-P46824-F1 Predicted AlphaFoldDB

No variants for P46824

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P46824

No associated diseases with P46824

6 regional properties for P46824

Type Name Position InterPro Accession
repeat Kinesin light chain repeat 337 - 378 IPR015792
repeat Tetratricopeptide repeat 228 - 261 IPR019734-1
repeat Tetratricopeptide repeat 270 - 303 IPR019734-2
repeat Tetratricopeptide repeat 312 - 345 IPR019734-3
repeat Tetratricopeptide repeat 354 - 387 IPR019734-4
repeat Tetratricopeptide repeat 437 - 470 IPR019734-5

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

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.

2 GO annotations of biological process

Name Definition
dorsal appendage formation Establishment of the dorsal filaments, elaborate specializations of the chorion that protrude from the anterior end of the egg and facilitate embryonic respiration.
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
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
Q91W40 Klc3 Kinesin light chain 3 Mus musculus (Mouse) 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
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
MTQMSQDEII TNTKTVLQGL EALRVEHVSI MNGIAEVQKD NEKSDMLRKN IENIELGLSE
70 80 90 100 110 120
AQVMMALTSH LQNIEAEKHK LKTQVRRLHQ ENAWLRDELA NTQQKFQASE QLVAQLEEEK
130 140 150 160 170 180
KHLEFMASVK KYDENQEQDD ACDKSRTDPV VELFPDEENE DRHNMSPTPP SQFANQTSGY
190 200 210 220 230 240
EIPARLRTLH NLVIQYASQG RYEVAVPLCK QALEDLERTS GHDHPDVATM LNILALVYRD
250 260 270 280 290 300
QNKYKEAANL LNDALSIRGK TLGENHPAVA ATLNNLAVLY GKRGKYKDAE PLCKRALEIR
310 320 330 340 350 360
EKVLGKDHPD VAKQLNNLAL LCQNQGKYDE VEKYYQRALD IYESKLGPDD PNVAKTKNNL
370 380 390 400 410 420
AGCYLKQGRY TEAEILYKQV LTRAHEREFG AIDSKNKPIW QVAEEREEHK FDNRENTPYG
430 440 450 460 470 480
EYGGWHKAAK VDSPTVTTTL KNLGALYRRQ GMFEAAETLE DCAMRSKKEA YDLAKQTKLS
490 500
QLLTSNEKRR SKAIKEDLDF SEEKNAKP