Calsequestrin-2

Details

Name
Calsequestrin-2
Synonyms
  • Calsequestrin, cardiac muscle isoform
Gene Name
CASQ2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049484|Calsequestrin-2
MKRTHLFIVGIYFLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPV
SSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGD
RTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYK
AFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEF
VKEHQRPTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPD
LSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADSVWMEIPDDDDLPTAEELED
WIEDVLSGKINTEDDDEDDDDDDNSDEEDNDDSDDDDDE
Number of residues
399
Molecular Weight
46435.28
Theoretical pI
Not Available
GO Classification
Functions
calcium ion binding / calcium-dependent protein binding / protein homodimerization activity
Processes
cardiac muscle contraction / cellular response to caffeine / detection of calcium ion / ion transmembrane transport / negative regulation of potassium ion transmembrane transporter activity / negative regulation of potassium ion transport / negative regulation of ryanodine-sensitive calcium-release channel activity / protein polymerization / Purkinje myocyte to ventricular cardiac muscle cell signaling / regulation of cardiac conduction / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of cell communication by electrical coupling / regulation of heart rate / regulation of membrane repolarization / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / sarcomere organization / sequestering of calcium ion / striated muscle contraction
Components
calcium channel complex / cytoplasm / intracellular / junctional membrane complex / junctional sarcoplasmic reticulum membrane / sarcoplasmic reticulum / sarcoplasmic reticulum lumen / sarcoplasmic reticulum membrane / Z disc
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, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) 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.
Specific Function
Calcium ion binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Sarcoplasmic reticulum lumen
Gene sequence
>lcl|BSEQ0049485|Calsequestrin-2 (CASQ2)
ATGAAGAGAACTCACTTGTTTATTGTGGGGATTTATTTTCTGTCCTCTTGCAGGGCAGAA
GAGGGGCTTAATTTCCCCACATATGATGGGAAGGACCGAGTGGTAAGTCTTTCCGAGAAG
AACTTCAAGCAGGTTTTAAAGAAATATGACTTGCTTTGCCTCTACTACCATGAGCCGGTG
TCTTCAGATAAGGTCACGCAAAAACAGTTCCAACTGAAAGAAATCGTGCTTGAGCTTGTG
GCCCAGGTCCTTGAACATAAAGCTATAGGCTTTGTGATGGTGGATGCCAAGAAAGAAGCC
AAGCTTGCCAAGAAACTGGGTTTTGATGAAGAAGGAAGCCTGTATATTCTTAAGGGTGAT
CGCACAATAGAGTTTGATGGCGAGTTTGCAGCTGATGTCTTGGTGGAGTTCCTCTTGGAT
CTAATTGAAGACCCAGTGGAGATCATCAGCAGCAAACTGGAAGTCCAAGCCTTCGAACGC
ATTGAAGACTACATCAAACTCATTGGCTTTTTCAAGAGTGAGGACTCAGAATACTACAAG
GCTTTTGAAGAAGCAGCTGAACACTTCCAGCCTTACATCAAATTCTTTGCCACCTTTGAC
AAAGGGGTTGCAAAGAAATTATCTTTGAAGATGAATGAGGTTGACTTCTATGAGCCATTT
ATGGATGAGCCCATTGCCATCCCCAACAAACCTTACACAGAAGAGGAGCTGGTGGAGTTT
GTGAAGGAACACCAAAGACCCACTCTACGTCGCCTGCGCCCAGAAGAAATGTTTGAAACA
TGGGAAGATGATTTGAATGGGATCCACATTGTGGCCTTTGCAGAGAAGAGTGATCCAGAT
GGCTACGAATTCCTGGAGATCCTGAAACAGGTTGCCCGGGACAATACTGACAACCCCGAT
CTGAGCATCCTGTGGATCGACCCGGACGACTTTCCTCTGCTCGTTGCCTACTGGGAGAAG
ACTTTCAAGATTGACCTATTCAGGCCACAGATTGGGGTGGTGAATGTCACAGATGCTGAC
AGTGTCTGGATGGAGATTCCAGATGATGACGATCTTCCAACTGCTGAGGAGCTGGAGGAC
TGGATTGAGGATGTGCTTTCTGGAAAGATAAACACTGAAGATGATGATGAAGATGATGAT
GATGATGATAATTCTGATGAAGAGGATAATGATGACAGTGATGACGATGATGATGAATAG
Chromosome Location
1
Locus
1p13.1
External Identifiers
ResourceLink
UniProtKB IDO14958
UniProtKB Entry NameCASQ2_HUMAN
HGNC IDHGNC:1513
General References
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  5. Sanchez EJ, Munske GR, Criswell A, Milting H, Dunker AK, Kang C: Phosphorylation of human calsequestrin: implications for calcium regulation. Mol Cell Biochem. 2011 Jul;353(1-2):195-204. doi: 10.1007/s11010-011-0787-4. Epub 2011 Mar 17. [Article]
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  7. Lahat H, Pras E, Olender T, Avidan N, Ben-Asher E, Man O, Levy-Nissenbaum E, Khoury A, Lorber A, Goldman B, Lancet D, Eldar M: A missense mutation in a highly conserved region of CASQ2 is associated with autosomal recessive catecholamine-induced polymorphic ventricular tachycardia in Bedouin families from Israel. Am J Hum Genet. 2001 Dec;69(6):1378-84. Epub 2001 Oct 25. [Article]
  8. Laitinen PJ, Swan H, Kontula K: Molecular genetics of exercise-induced polymorphic ventricular tachycardia: identification of three novel cardiac ryanodine receptor mutations and two common calsequestrin 2 amino-acid polymorphisms. Eur J Hum Genet. 2003 Nov;11(11):888-91. [Article]
  9. Houle TD, Ram ML, Cala SE: Calsequestrin mutant D307H exhibits depressed binding to its protein targets and a depressed response to calcium. Cardiovasc Res. 2004 Nov 1;64(2):227-33. [Article]
  10. di Barletta MR, Viatchenko-Karpinski S, Nori A, Memmi M, Terentyev D, Turcato F, Valle G, Rizzi N, Napolitano C, Gyorke S, Volpe P, Priori SG: Clinical phenotype and functional characterization of CASQ2 mutations associated with catecholaminergic polymorphic ventricular tachycardia. Circulation. 2006 Sep 5;114(10):1012-9. Epub 2006 Aug 14. [Article]
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Drug Relations

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