S100 Calcium Binding Protein A11 (S100A11), also known as calgizzarin, is a member of the S100 family of proteins. These proteins are characterized by their ability to bind calcium ions through EF-hand motifs, which are helix-loop-helix structures . The S100 family consists of 21 known members in humans, each with a molecular weight between 10 and 14 kDa .
The S100 proteins were first discovered in 1965 by American scientist Blake W. Moore, who identified a unique protein in the brain tissue of cattle that could be dissolved in a saturated ammonium sulfate solution . This protein was named S100 due to its solubility properties. S100 proteins are predominantly found in vertebrates and play crucial roles both inside and outside cells as calcium sensors and binding proteins .
S100A11 is a protein coding gene that facilitates the differentiation and cornification of keratinocytes . It is widely expressed in various tissues and has been implicated in several cellular processes, including cell cycle progression, differentiation, motility, invasion, and tubulin polymerization . The protein encoded by the S100A11 gene has a length of 105 amino acids and a mass of approximately 11.7 kDa .
S100A11 mediates signal transduction in response to internal or external stimuli and plays various roles in different diseases such as cancers, metabolic diseases, neurological diseases, and vascular calcification . It can also function as a chemotactic agent in inflammatory diseases . Altered expression and chromosomal rearrangements of the S100A11 gene have been implicated in tumor metastasis .