It also helps the sarcoplasmic reticulum store an extraordinarily high amount of calcium ions.

[1] Sequence analysis has suggested that calcium is not bound in distinct pockets via EF-hand motifs, but rather via presentation of a charged protein surface.

[5] Furthermore, CASQ2 modulates the CICR mechanism by lengthening to process to functionally recharge the sarcoplasmic reticulum's calcium ion stores.

[6] A mutation can have a significant effect if it disrupts the linear polymerization ability of CASQ2, which directly accounts for its high-capacity to bind Ca2+.

[6] In addition, the hydrophobic core of domain II appears to be necessary for CASQ2's function, because a single amino acid mutation that disrupts this hydrophobic core directly leads to molecular aggregates, which are unable to respond to calcium ions.