STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane

By Shenyuan L. Zhang, Ying Yu, J. Roos, J. A. Kozak, Thomas J. Deerinck, Mark Ellisman, K. Stauderman, M. Cahalan. Nature, 2005

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Handbook of ion channels (2015, background): “EF-hand STIM1 mutants with impaired Ca2+ binding form puncta and activate CRAC channels independently of ER Ca2+ store depletion [33,34]; the absence of Ca2+ binding in these mutants essentially tricks the molecules into responding as if stores are depleted.”
Dual functions for the endoplasmic reticulum calcium sensors STIM1 and STIM2 in T cell activation and tolerance (2008, background): “STIM proteins with EF-hand alterations that impair Ca 2+ binding are constitutively present in puncta, even in resting cells with full Ca 2+ store”
Store-Operated Calcium Channels. (2015, neutral): “Overexpression of STIM1 proteins with EF hand mutations designed [and later confirmed (155)] to reduce Ca(2) affinity (D76A, D76A/D78A, E87A) triggered constitutive formation of puncta as well as activation of SOCE and ICRAC in unstimulated cells (199, 239, 362, 443), essentially mimicking the effec”
Molecular Basis of Calcium Signaling in Lymphocytes: STIM and ORAI (2010, background): “Moreover, the same substitutions lead to constitutive activation of store-operated Ca2+ entry and CRAC current (19, 31, 106), demonstrating that disruption of Ca2+ binding to EF-hand 1 is functionally equivalent to dissociation of Ca2+ upon store depletion.”