STIM1

Stromal interaction molecule 1
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsSTIM1 ; D11S4896E; GOK; IMD10; STRMK; TAM; TAM1
External IDsOMIM: 605921 MGI: 107476 HomoloGene: 20681 GeneCards: STIM1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez678620866
EnsemblENSG00000167323ENSMUSG00000030987
UniProtQ13586P70302
RefSeq (mRNA)NM_001277961NM_009287
RefSeq (protein)NP_001264890NP_033313
Location (UCSC)Chr 11:
3.88 – 4.11 Mb		Chr 7:
102.27 – 102.44 Mb
PubMed search

Stromal interaction molecule 1 is a protein that in humans is encoded by the STIM1 gene.[1][2][3] STIM1 has a single transmembrane domain, and is localized to the endoplasmic reticulum, and to a lesser extent to the plasma membrane.[4]

Even though the protein has been identified earlier, its function was unknown until recently. In 2005, it was discovered that STIM1 functions as a calcium sensor in the endoplasmic reticulum.<ref name=pmid"15866891">Roos J, DiGregorio PJ, Yeromin AV, Ohlsen K, Lioudyno M, Zhang S, Safrina O, Kozak JA, Wagner SL, Cahalan MD, Veliçelebi G, Stauderman KA. (2005). "STIM1, an essential and conserved component of store-operated Ca2+ channel function". J.Cell.Biol. 169 (3): 435–45. doi:10.1083/jcb.200502019. PMC 2171946. PMID 15866891.</ref>[5] Upon activation of the IP3 receptor, the calcium concentration in the endoplasmic reticulum decreases, which is sensed by STIM1, via its EF hand domain. STIM1 activates the "store-operated" ORAI1 calcium ion channels in the plasma membrane, via intracellular STIM1 movement, clustering under plasma membrane and protein protein interaction with ORAI isoforms.[6] 2-Aminoethoxydiphenyl borate (2-APB) and 4-chloro-3-ethylphenol (4-CEP) cause STIM1 clustering in a cell and prevent STIM1 moving toward plasma membrane.[7]

Interactions

STIM1 has been shown to interact with STIM2.[2]

References

  1. ↑ Parker NJ, Begley CG, Smith PJ, Fox RM (Feb 1997). "Molecular cloning of a novel human gene (D11S4896E) at chromosomal region 11p15.5". Genomics 37 (2): 253–6. doi:10.1006/geno.1996.0553. PMID 8921403.
  2. ↑ 2.0 2.1 Williams RT, Manji SS, Parker NJ, Hancock MS, Van Stekelenburg L, Eid JP, Senior PV, Kazenwadel JS, Shandala T, Saint R, Smith PJ, Dziadek MA (Jul 2001). "Identification and characterization of the STIM (stromal interaction molecule) gene family: coding for a novel class of transmembrane proteins". Biochem J 357 (Pt 3): 673–85. doi:10.1042/0264-6021:3570673. PMC 1221997. PMID 11463338.
  3. ↑ Williams RT, Senior PV, Van Stekelenburg L, Layton JE, Smith PJ, Dziadek MA (May 2002). "Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation". Biochim Biophys Acta 1596 (1): 131–7. doi:10.1016/S0167-4838(02)00211-X. PMID 11983428.
  4. ↑ Soboloff, Jonathan; Rothberg, B. S.; Madesh, M.; Gill, D. L. (September 2012). "STIM proteins: dynamic calcium signal transducers". Nat Rev Mol Cell Biol 13 (9): 549–65. doi:10.1038/nrm3414. PMC 3458427. PMID 22914293.
  5. ↑ Liou J, Kim ML, Heo WD, Jones JT, Myers JW, Ferrell JE Jr, Meyer T. (2005). "STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx". Curr. Biol. 15 (13): 1235–41. doi:10.1016/j.cub.2005.05.055. PMC 3186072. PMID 16005298.
  6. ↑ Putney JW (2009). "Capacitative calcium entry: from concept to molecules.". Immunol Rev 231 (1): 10–22. doi:10.1111/j.1600-065X.2009.00810.x. PMID 19754887.
  7. ↑ Zeng B, Chen, GL, Xu, SZ (2012). "Store-independent pathways for cytosolic STIM1 clustering in the regulation of store-operated Ca(2+) influx.". Biochem Pharmacol 84 (8): 1024–35. doi:10.1016/j.bcp.2012.07.013.x. PMID 22842488.