P12637 · CASQ2_CANLF
- ProteinCalsequestrin-2
- GeneCASQ2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids410 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle (PubMed:3427023).
Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca2+ ions. Regulates the release of lumenal Ca2+ via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca2+ ions. Regulates the release of lumenal Ca2+ via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
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 | sarcoplasmic reticulum | |
Cellular Component | sarcoplasmic reticulum lumen | |
Cellular Component | Z disc | |
Molecular Function | calcium ion binding | |
Biological Process | negative regulation of ryanodine-sensitive calcium-release channel activity | |
Biological Process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion | |
Biological Process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCalsequestrin-2
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionP12637
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 206 | Creates an additional N-glycosylation site. Decreases calcium binding and increases the rate of spontaneous Ca2+ release from myocytes. | ||||
Sequence: K → N |
PTM/Processing
Features
Showing features for signal, chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MKRTHLFIAGLYLLASCRA | ||||||
Chain | PRO_0000004217 | 20-410 | Calsequestrin-2 | |||
Sequence: EEGLNFPTYDGKDRVVSLTEKNFKQVLKKYDVLCLYYHESVSSDKVAQKQFQLKEIVLELVAQVLEHKDIGFVMVDAKKEAKLAKKLGFDEEGSLYVLKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIINSKLEVQAFERIEDQIKLIGFFKSEESEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPDKPYTEEELVEFVKEHQRPTLRRLRPEDMFETWEDDLNGIHIVAFAERSDPDGYEFLEILKQVARDNTDNPDLSIVWIDPDDFPLLVAYWEKTFKIDLFKPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDNEEGDDGDDDEDDDDDDGNNSDEESNDDSDDDDE | ||||||
Modified residue | 282 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 335 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 395 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 397 | Phosphoserine; by CK2 | ||||
Sequence: S | ||||||
Modified residue | 401 | Phosphoserine; by CK2 | ||||
Sequence: S | ||||||
Modified residue | 405 | Phosphoserine; by CK2 | ||||
Sequence: S |
Post-translational modification
Phosphorylation in the C-terminus, probably by CK2, moderately increases calcium buffering capacity.
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in heart muscle (at protein level).
Interaction
Subunit
Interacts with ASPH (By similarity).
Monomer, homodimer and homooligomer. Mostly monomeric in the absence of calcium. Forms higher oligomers in a calcium-dependent manner. Dimers associate to form tetramers, that then form linear homomer chains. Interacts with TRDN
Monomer, homodimer and homooligomer. Mostly monomeric in the absence of calcium. Forms higher oligomers in a calcium-dependent manner. Dimers associate to form tetramers, that then form linear homomer chains. Interacts with TRDN
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 221-242 | Calcium regulated hydrophobic site | ||||
Sequence: MDEPIAIPDKPYTEEELVEFVK | ||||||
Region | 364-410 | Disordered | ||||
Sequence: DVLSGKINTEDDDNEEGDDGDDDEDDDDDDGNNSDEESNDDSDDDDE | ||||||
Compositional bias | 374-410 | Acidic residues | ||||
Sequence: DDDNEEGDDGDDDEDDDDDDGNNSDEESNDDSDDDDE |
Sequence similarities
Belongs to the calsequestrin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length410
- Mass (Da)47,417
- Last updated1989-10-01 v1
- ChecksumFCA99A8D7E7ABB82
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 71 | in Ref. 2; AA sequence | ||||
Sequence: Q → E | ||||||
Compositional bias | 374-410 | Acidic residues | ||||
Sequence: DDDNEEGDDGDDDEDDDDDDGNNSDEESNDDSDDDDE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J03766 EMBL· GenBank· DDBJ | AAA30833.1 EMBL· GenBank· DDBJ | mRNA |