InterPro : IPR018233

Name  Calsequestrin, conserved site Short Name  Calsequestrin_CS
Type  Conserved_site Description  Calsequestrin is the principal calcium-binding protein present in thesarcoplasmic reticulum of cardiac and skeletal muscle []. It is a highly acidic protein that is able to bind over 40 calcium ions and acts as an internalcalcium store in muscle. Sequence analysis has suggested that calcium isnot bound in distinct pockets via EF-hand motifs, but rather via presentation of a charged protein surface. Two forms of calsequestrinhave been identified. The cardiac form is present in cardiac and slowskeletal muscle and the fast skeletal form is found in fast skeletal muscle.The release of calsequestrin-bound calcium (through a a calciumrelease channel) triggers muscle contraction.The active protein is not highly structured, more than 50% ofit adopting a random coil conformation []. When calcium binds there is a structural change wherebythe alpha-helical content of the proteinincreases from 3 to 11% [].Both forms of calsequestrin are phosphorylated by casein kinase II, butthe cardiac form is phosphorylated more rapidly and to a higher degree [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

2 Found In

Id Name Short Name Type
IPR012336 Thioredoxin-like fold Thioredoxin-like_fold Domain
IPR001393 Calsequestrin Calsequestrin Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Slupsky JR Characterization of cardiac calsequestrin. 1987 Biochemistry 26 6539-44
Scott BT Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning. 1988 J Biol Chem 263 8958-64
Cala SE Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. Demonstration of a cluster of unique rapidly phosphorylated sites in cardiac calsequestrin. 1991 J Biol Chem 266 391-8

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)