S100A11 Human

S100 Calcium Binding Protein A11, also known as S100A11 or calgizzarin, is a member of the S100 family of proteins. This family is characterized by the presence of two EF-hand calcium-binding motifs, which are helix-loop-helix structural domains capable of binding calcium ions. S100A11 is a small acidic protein with a molecular weight of approximately 13 kDa .

The S100 protein family was 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 . S100A11 itself was first isolated from chicken gizzard muscles in 1989 and later cloned and purified in 1991 . The protein contains two EF-hand domains that undergo conformational changes upon binding calcium ions .

The gene encoding S100A11 is located on chromosome 1q21, where it is clustered with other members of the S100 family . S100A11 is primarily localized in the cytoplasm and/or nucleus of a wide range of cells . It is involved in the regulation of various cellular processes, including cell cycle progression and differentiation .

S100A11 plays a crucial role in several cellular functions:

• Cell Motility and Invasion: S100A11 is involved in cell motility and invasion, which are critical processes in cancer metastasis .
• Tubulin Polymerization: The protein also plays a role in the polymerization of tubulin, a key component of the cytoskeleton .
• Signal Transduction: S100A11 mediates signal transduction in response to internal or external stimuli, functioning as a calcium sensor and binding protein .

S100A11 has been implicated in various diseases, including:

• Cancer: Altered expression and chromosomal rearrangements of the S100A11 gene have been linked to tumor metastasis .
• Inflammatory Diseases: S100A11 can function as a chemotactic agent in inflammatory diseases .
• Metabolic and Neurological Diseases: The protein also plays roles in metabolic and neurological diseases .