Q05090 · KLC_STRPU
- ProteinKinesin light chain
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids686 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | kinesin complex | |
Cellular Component | microtubule | |
Molecular Function | kinesin binding | |
Biological Process | microtubule-based movement |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameKinesin light chain
- Short namesKLC
Organism names
- Taxonomic lineageEukaryota > Metazoa > Echinodermata > Eleutherozoa > Echinozoa > Echinoidea > Euechinoidea > Echinacea > Camarodonta > Echinidea > Strongylocentrotidae > Strongylocentrotus
Accessions
- Primary accessionQ05090
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000215100 | 1-686 | Kinesin light chain | |||
Sequence: MSGSKLSTPNNSGGGQGNLSQEQIITGTREVIKGLEQLKNEHNDILNSLYQSLKMLKKDTPGDSNLVEEKTDIIEKSLESLELGLGEAKVMMALGHHLNMVEAEKQKLRAQVRRLVQENTWLRDELAATQQKLQTSEQNLADLEVKYKHLEYMNSIKKYDEDRTPDEEASSSDPLDLGFPEDDDGGQADESYPQPQTGSGSVSAAAGGYEIPARLRTLHNLVIQYASQSRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAGNLLHDALAIREKTLGPDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEWYYQRALEIYEKKLGPDDPNVAKTKNNLAAAYLKQGKYKAAETLYKQVLTRAHEREFGLSADDKDNKPIWMQAEEREEKGKFKDNAPYGDYGGWHKAAKVDSRSRSSPTVTTTLKNLGALYRRQGKYDAAEILEECAMKSRRNALDMVRETKVRELLGQDLSTDVPRSEAMAKERHHRRSSGTPRHGSTESVSYEKTDGSEEVSIGVAWKAKRKAKDRSRSIPAGYVEIPRSPPHVLVENGDGKLRRSGSLSKLRASVRRSSTKLLNKLKGRESDDDGGMKRASSMSVLPSRGNDESTPAPIQLSQRGRVGSHDNLSSRRQSGNF |
Post-translational modification
Phosphorylation may modulate the process of mechanochemical coupling.
Keywords
- PTM
Interaction
Subunit
Oligomeric complex composed of two heavy chains and two light chains.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, coiled coil, repeat, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MSGSKLSTPNNSGGGQGNLSQEQ | ||||||
Coiled coil | 20-160 | |||||
Sequence: SQEQIITGTREVIKGLEQLKNEHNDILNSLYQSLKMLKKDTPGDSNLVEEKTDIIEKSLESLELGLGEAKVMMALGHHLNMVEAEKQKLRAQVRRLVQENTWLRDELAATQQKLQTSEQNLADLEVKYKHLEYMNSIKKYD | ||||||
Region | 158-204 | Disordered | ||||
Sequence: KYDEDRTPDEEASSSDPLDLGFPEDDDGGQADESYPQPQTGSGSVSA | ||||||
Repeat | 215-248 | TPR 1 | ||||
Sequence: LRTLHNLVIQYASQSRYEVAVPLCKQALEDLEKT | ||||||
Repeat | 257-290 | TPR 2 | ||||
Sequence: ATMLNILALVYRDQNKYKEAGNLLHDALAIREKT | ||||||
Repeat | 299-332 | TPR 3 | ||||
Sequence: AATLNNLAVLYGKRGKYKEAEPLCKRALEIREKV | ||||||
Repeat | 341-374 | TPR 4 | ||||
Sequence: AKQLNNLALLCQNQGKYEEVEWYYQRALEIYEKK | ||||||
Repeat | 383-416 | TPR 5 | ||||
Sequence: AKTKNNLAAAYLKQGKYKAAETLYKQVLTRAHER | ||||||
Repeat | 472-505 | TPR 6 | ||||
Sequence: TTTLKNLGALYRRQGKYDAAEILEECAMKSRRNA | ||||||
Region | 520-558 | Disordered | ||||
Sequence: QDLSTDVPRSEAMAKERHHRRSSGTPRHGSTESVSYEKT | ||||||
Region | 586-686 | Disordered | ||||
Sequence: GYVEIPRSPPHVLVENGDGKLRRSGSLSKLRASVRRSSTKLLNKLKGRESDDDGGMKRASSMSVLPSRGNDESTPAPIQLSQRGRVGSHDNLSSRRQSGNF | ||||||
Compositional bias | 627-641 | Basic and acidic residues | ||||
Sequence: LNKLKGRESDDDGGM | ||||||
Compositional bias | 648-686 | Polar residues | ||||
Sequence: SVLPSRGNDESTPAPIQLSQRGRVGSHDNLSSRRQSGNF |
Domain
The light chain is composed of three structural domains: a large globular N-terminal domain which may be involved in binding to kinesin heavy chains, a central alpha-helical coiled-coil domain that mediates the light chain dimerization; and a small globular C-terminal which may play a role in regulating mechanochemical activity or attachment of kinesin to membrane-bound organelles.
Sequence similarities
Belongs to the kinesin light chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q05090-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameKLC-3
- Length686
- Mass (Da)76,517
- Last updated1994-06-01 v1
- Checksum603D71186CC0364B
Q05090-2
- NameKLC-1
- Differences from canonical
- 564-600: Missing
Q05090-3
- NameKLC-2
- Differences from canonical
- 564-572: Missing
Q05090-4
- NameKLC-4
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7M7T5H3 | A0A7M7T5H3_STRPU | 678 | |||
A0A7M7T4W8 | A0A7M7T4W8_STRPU | 691 | |||
A0A7M7PRB3 | A0A7M7PRB3_STRPU | 676 | |||
A0A7M7PRF1 | A0A7M7PRF1_STRPU | 672 | |||
A0A7M7PPL7 | A0A7M7PPL7_STRPU | 663 | |||
A0A7M7PTH0 | A0A7M7PTH0_STRPU | 666 | |||
A0A7M7PTB3 | A0A7M7PTB3_STRPU | 567 | |||
A0A7M7PT11 | A0A7M7PT11_STRPU | 565 | |||
A0A7M7PSA8 | A0A7M7PSA8_STRPU | 604 | |||
A0A7M7PRV8 | A0A7M7PRV8_STRPU | 576 | |||
A0A7M7PMZ9 | A0A7M7PMZ9_STRPU | 620 | |||
A0A7M7PNM2 | A0A7M7PNM2_STRPU | 700 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002879 | 441-451 | in isoform KLC-4 | |||
Sequence: GKFKDNAPYGD → VKKRKPKPAKS | ||||||
Alternative sequence | VSP_002880 | 452-686 | in isoform KLC-4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002877 | 564-572 | in isoform KLC-2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002878 | 564-600 | in isoform KLC-1 | |||
Sequence: Missing | ||||||
Compositional bias | 627-641 | Basic and acidic residues | ||||
Sequence: LNKLKGRESDDDGGM | ||||||
Compositional bias | 648-686 | Polar residues | ||||
Sequence: SVLPSRGNDESTPAPIQLSQRGRVGSHDNLSSRRQSGNF |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L10235 EMBL· GenBank· DDBJ | AAA03059.1 EMBL· GenBank· DDBJ | mRNA | ||
L10234 EMBL· GenBank· DDBJ | AAA03058.1 EMBL· GenBank· DDBJ | mRNA | ||
L10233 EMBL· GenBank· DDBJ | AAA03057.1 EMBL· GenBank· DDBJ | mRNA | ||
L08258 EMBL· GenBank· DDBJ | AAA03060.1 EMBL· GenBank· DDBJ | mRNA |