Calsequestrin-1

Details

Name
Calsequestrin-1
Synonyms
  • Calmitine
  • Calsequestrin, skeletal muscle isoform
  • CASQ
Gene Name
CASQ1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049492|Calsequestrin-1
MSATDRMGPRAVPGLRLALLLLLVLGTPKSGVQGQEGLDFPEYDGVDRVINVNAKNYKNV
FKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKK
LGLTEVDSMYVFKGDEVIEYDGEFSADTIVEFLLDVLEDPVELIEGERELQAFENIEDEI
KLIGYFKSKDSEHYKAFEDAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPV
TIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGFEFL
ETLKAVAQDNTENPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWME
MDDEEDLPSAEELEDWLEDVLEGEINTEDDDDDDDD
Number of residues
396
Molecular Weight
45159.635
Theoretical pI
Not Available
GO Classification
Functions
calcium ion binding
Processes
endoplasmic reticulum organization / ion transmembrane transport / protein polymerization / regulation of cardiac conduction / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / response to denervation involved in regulation of muscle adaptation / response to heat / response to organic substance / sarcomere organization / skeletal muscle tissue development
Components
endoplasmic reticulum / Golgi apparatus / I band / mitochondrial matrix / mitochondrion / sarcoplasmic reticulum / sarcoplasmic reticulum lumen / sarcoplasmic reticulum membrane / smooth endoplasmic reticulum / T-tubule / terminal cisterna lumen
General Function
Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction.
Specific Function
Calcium ion binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Sarcoplasmic reticulum
Gene sequence
>lcl|BSEQ0049493|Calsequestrin-1 (CASQ1)
ATGAGTGCTACAGACAGGATGGGGCCCAGAGCTGTGCCGGGTCTGCGGCTGGCACTGCTG
TTGCTGCTGGTGCTAGGGACACCCAAGTCAGGGGTACAGGGGCAGGAAGGGCTGGACTTC
CCTGAGTACGATGGTGTGGACCGTGTGATCAATGTCAATGCAAAGAACTACAAGAATGTG
TTCAAGAAGTATGAGGTGCTGGCACTCCTCTACCATGAACCCCCCGAGGATGACAAGGCC
TCACAAAGACAATTTGAGATGGAGGAGCTGATCCTGGAGTTAGCAGCCCAAGTCCTAGAA
GACAAGGGTGTTGGCTTCGGGCTGGTAGACTCTGAGAAGGATGCAGCTGTGGCCAAGAAA
CTAGGCCTAACTGAAGTGGACAGCATGTATGTATTCAAGGGAGATGAAGTCATTGAGTAC
GATGGCGAGTTTTCTGCTGACACCATCGTGGAGTTTCTGCTTGATGTCCTAGAGGACCCT
GTGGAATTGATTGAAGGTGAACGAGAGCTGCAGGCGTTTGAGAATATTGAGGATGAGATC
AAACTCATTGGCTACTTCAAGAGCAAAGACTCAGAGCATTACAAAGCCTTCGAGGATGCA
GCTGAGGAGTTTCATCCCTACATCCCCTTCTTCGCCACCTTCGACAGCAAGGTGGCAAAG
AAGCTGACCCTGAAGCTGAATGAGATTGATTTCTACGAGGCCTTCATGGAAGAGCCTGTG
ACCATCCCAGACAAGCCCAATAGCGAAGAGGAGATTGTCAACTTCGTGGAGGAGCACAGG
AGATCAACCCTGAGGAAACTGAAGCCGGAGAGTATGTATGAGACCTGGGAGGATGATATG
GATGGAATCCACATTGTGGCCTTCGCAGAGGAAGCTGATCCTGATGGTTTCGAGTTCTTA
GAGACTCTCAAGGCTGTGGCCCAAGATAACACTGAAAACCCAGATCTTAGCATCATCTGG
ATTGACCCTGATGACTTCCCCCTGCTGGTCCCATACTGGGAGAAGACGTTTGACATCGAC
TTGTCAGCCCCACAAATAGGAGTCGTCAATGTTACTGATGCGGATAGCGTATGGATGGAA
ATGGACGATGAGGAGGACCTGCCTTCTGCTGAGGAGCTGGAGGACTGGCTGGAGGATGTC
CTGGAGGGCGAGATCAACACAGAGGACGATGACGATGATGATGATGACTAG
Chromosome Location
1
Locus
1q23.2
External Identifiers
ResourceLink
UniProtKB IDP31415
UniProtKB Entry NameCASQ1_HUMAN
HGNC IDHGNC:1512
General References
  1. Fujii J, Willard HF, MacLennan DH: Characterization and localization to human chromosome 1 of human fast-twitch skeletal muscle calsequestrin gene. Somat Cell Mol Genet. 1990 Mar;16(2):185-9. [Article]
  2. Bataille N, Schmitt N, Aumercier-Maes P, Ollivier B, Lucas-Heron B, Lestienne P: Molecular cloning of human calmitine, a mitochondrial calcium binding protein, reveals identity with calsequestrine. Biochem Biophys Res Commun. 1994 Sep 30;203(3):1477-82. [Article]
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  6. Sanchez EJ, Lewis KM, Danna BR, Kang C: High-capacity Ca2+ binding of human skeletal calsequestrin. J Biol Chem. 2012 Mar 30;287(14):11592-601. doi: 10.1074/jbc.M111.335075. Epub 2012 Feb 15. [Article]
  7. Rossi D, Vezzani B, Galli L, Paolini C, Toniolo L, Pierantozzi E, Spinozzi S, Barone V, Pegoraro E, Bello L, Cenacchi G, Vattemi G, Tomelleri G, Ricci G, Siciliano G, Protasi F, Reggiani C, Sorrentino V: A mutation in the CASQ1 gene causes a vacuolar myopathy with accumulation of sarcoplasmic reticulum protein aggregates. Hum Mutat. 2014 Oct;35(10):1163-70. doi: 10.1002/humu.22631. Epub 2014 Sep 10. [Article]
  8. D'Adamo MC, Sforna L, Visentin S, Grottesi A, Servettini L, Guglielmi L, Macchioni L, Saredi S, Curcio M, De Nuccio C, Hasan S, Corazzi L, Franciolini F, Mora M, Catacuzzeno L, Pessia M: A Calsequestrin-1 Mutation Associated with a Skeletal Muscle Disease Alters Sarcoplasmic Ca2+ Release. PLoS One. 2016 May 19;11(5):e0155516. doi: 10.1371/journal.pone.0155516. eCollection 2016. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB11093Calcium citrateapproved, investigationalnoligandDetails
DB11348Calcium PhosphateapprovednoligandDetails
DB13800Calcium levulinateapproved, experimentalunknownagonistDetails
DB14481Calcium phosphate dihydrateapprovednoDetails