Anti-stromal interaction molecule 2

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STIM (stromal interaction molecule) proteins are conserved single-pass transmembrane protein. The three STIM proteins, STIM1, STIM2 and D-Stim, are ubiquitously expressed proteins composed of a single SAM (sterile α-motif) domain and an unpaired EF hand within the highly conserved extracellular region and coiled-coil domains that are conserved in structure and position within the cytoplasmic region. Significant divergence between these proteins was found only at the extreme C-termini. STIM proteins are modified by phosphorylation and N-linked glycosylation.

STIM (stromal interaction molecule) required for the regulation of store-operated Ca2+ influx. Store-operated calcium entry is mediated by Ca2+ release-activated Ca2+ (CRAC) channels, following Ca2+ depletion from the endoplasmic reticulum (ER) stores. This process is crucial for gene transcription, proliferation and cytokine release. STIM2 is an inhibitor of STIM1-mediated store-operated Ca2+ entry. STIM2 co-localizes with STIM1 in punctae upon store depletion, and coprecipitates with STIM1 from cell lysates, suggesting that they may play a coordinated role in controlling Ca2+ entry.