Hmdb loader
Identification
HMDB Protein ID HMDBP07556
Secondary Accession Numbers
  • 13264
Name Calsequestrin-2
Synonyms
  1. Calsequestrin, cardiac muscle isoform
Gene Name CASQ2
Protein Type Unknown
Biological Properties
General Function Involved in calcium ion binding
Specific 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. Binds 40 to 50 moles of calcium
Pathways Not Available
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
binding
calcium ion binding
Cellular Location
  1. Sarcoplasmic reticulum lumen
Gene Properties
Chromosome Location Chromosome:1
Locus 1p13.3-p11
SNPs CASQ2
Gene Sequence
>1200 bp
ATGAAGAGAACTCACTTGTTTATTGTGGGGATTTATTTTCTGTCCTCTTGCAGGGCAGAA
GAGGGGCTTAATTTCCCCACATATGATGGGAAGGACCGAGTGGTAAGTCTTTCCGAGAAG
AACTTCAAGCAGGTTTTAAAGAAATATGACTTGCTTTGCCTCTACTACCATGAGCCGGTG
TCTTCAGATAAGGTCACGCAAAAACAGTTCCAACTGAAAGAAATCGTGCTTGAGCTTGTG
GCCCAGGTCCTTGAACATAAAGCTATAGGCTTTGTGATGGTGGATGCCAAGAAAGAAGCC
AAGCTTGCCAAGAAACTGGGTTTTGATGAAGAAGGAAGCCTGTATATTCTTAAGGGTGAT
CGCACAATAGAGTTTGATGGCGAGTTTGCAGCTGATGTCTTGGTGGAGTTCCTCTTGGAT
CTAATTGAAGACCCAGTGGAGATCATCAGCAGCAAACTGGAAGTCCAAGCCTTCGAACGC
ATTGAAGACTACATCAAACTCATTGGCTTTTTCAAGAGTGAGGACTCAGAATACTACAAG
GCTTTTGAAGAAGCAGCTGAACACTTCCAGCCTTACATCAAATTCTTTGCCACCTTTGAC
AAAGGGGTTGCAAAGAAATTATCTTTGAAGATGAATGAGGTTGACTTCTATGAGCCATTT
ATGGATGAGCCCATTGCCATCCCCAACAAACCTTACACAGAAGAGGAGCTGGTGGAGTTT
GTGAAGGAACACCAAAGACCCACTCTACGTCGCCTGCGCCCAGAAGAAATGTTTGAAACA
TGGGAAGATGATTTGAATGGGATCCACATTGTGGCCTTTGCAGAGAAGAGTGATCCAGAT
GGCTACGAATTCCTGGAGATCCTGAAACAGGTTGCCCGGGACAATACTGACAACCCCGAT
CTGAGCATCCTGTGGATCGACCCGGACGACTTTCCTCTGCTCGTTGCCTACTGGGAGAAG
ACTTTCAAGATTGACCTATTCAGGCCACAGATTGGGGTGGTGAATGTCACAGATGCTGAC
AGTGTCTGGATGGAGATTCCAGATGATGACGATCTTCCAACTGCTGAGGAGCTGGAGGAC
TGGATTGAGGATGTGCTTTCTGGAAAGATAAACACTGAAGATGATGATGAAGATGATGAT
GATGATGATAATTCTGATGAAGAGGATAATGATGACAGTGATGACGATGATGATGAATAG
Protein Properties
Number of Residues 399
Molecular Weight 46435.3
Theoretical pI 3.97
Pfam Domain Function
Signals
  • 1-19
Transmembrane Regions
  • None
Protein Sequence
>Calsequestrin-2
MKRTHLFIVGIYFLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPV
SSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGD
RTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYK
AFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEF
VKEHQRPTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPD
LSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADSVWMEIPDDDDLPTAEELED
WIEDVLSGKINTEDDDEDDDDDDNSDEEDNDDSDDDDDE
GenBank ID Protein 119395727
UniProtKB/Swiss-Prot ID O14958
UniProtKB/Swiss-Prot Entry Name CASQ2_HUMAN
PDB IDs
GenBank Gene ID NM_001232
GeneCard ID CASQ2
GenAtlas ID CASQ2
HGNC ID HGNC:1513
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
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  3. Kim E, Youn B, Kemper L, Campbell C, Milting H, Varsanyi M, Kang C: Characterization of human cardiac calsequestrin and its deleterious mutants. J Mol Biol. 2007 Nov 2;373(4):1047-57. Epub 2007 Aug 29. [PubMed:17881003 ]
  4. 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. [PubMed:11704930 ]
  5. 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. [PubMed:14571276 ]
  6. 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. [PubMed:15485681 ]
  7. 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. [PubMed:16908766 ]
  8. Valle G, Galla D, Nori A, Priori SG, Gyorke S, de Filippis V, Volpe P: Catecholaminergic polymorphic ventricular tachycardia-related mutations R33Q and L167H alter calcium sensitivity of human cardiac calsequestrin. Biochem J. 2008 Jul 15;413(2):291-303. doi: 10.1042/BJ20080163. [PubMed:18399795 ]