P31231 (CASQ1_RANES) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 66.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Calsequestrin-1 Alternative name(s): Calsequestrin, skeletal muscle isoform |
| Organism | Rana esculenta (Edible frog) (Pelophylax esculentus) |
| Taxonomic identifier | 8401 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Pelophylax![]() |
Protein attributes
| Sequence length | 420 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. The skeletal muscle CASQ1) binds around 80 Ca2+ ions, while the cardiac CASQ2) binds approximately 60 Ca2+ ions By similarity. |
| Subcellular location | Sarcoplasmic reticulum lumen. Note: This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells. |
| Sequence similarities | Belongs to the calsequestrin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Sarcoplasmic reticulum |
| Domain | Signal |
| Ligand | Calcium |
| Molecular function | Muscle protein |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular_component | sarcoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | calcium ion binding Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Molecular cloning, functional expression and tissue distribution of the cDNA encoding frog skeletal muscle calsequestrin." Treves S., Vilsen B., Chiozzi P., Andersen J.P., Zorzato F. Biochem. J. 283:767-772(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle. |
| [2] | "Frog brain expresses a 60 KDa Ca2+ binding protein similar to mammalian calreticulin." Treveso S., Zorzato F., Chiozzi P., Melandri P., Volpe P., Pozzan T. Biochem. Biophys. Res. Commun. 175:444-450(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-57. Tissue: Skeletal muscle. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X64324 mRNA. Translation: CAA45609.1. |
| PIR | S22418. |
3D structure databases | |
| ProteinModelPortal | P31231. |
| SMR | P31231. Positions 25-369. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG050805. |
Family and domain databases | |
| Gene3D | 3.40.30.10. 3 hits. |
| InterPro | IPR001393. Calsequestrin. IPR018233. Calsequestrin_CS. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| PANTHER | PTHR10033. PTHR10033. 1 hit. |
| Pfam | PF01216. Calsequestrin. 1 hit. [Graphical view] |
| PRINTS | PR00312. CALSEQUESTRN. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 3 hits. |
| PROSITE | PS00863. CALSEQUESTRIN_1. 1 hit. PS00864. CALSEQUESTRIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CASQ1_RANES | ||||||||
| Accession | Primary (citable) accession number: P31231 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
