Many different calcium-binding proteins exist, with different cellular and tissue distribution and involvement in specific functions. Calcium binding proteins also serve an important physiological role for cells. The most ubiquitous Ca2+-sensing protein, found in all
eukaryotic organisms including
yeasts, is
calmodulin. Intracellular storage and release of Ca2+ from the
sarcoplasmic reticulum is associated with the high-capacity, low-affinity calcium-binding protein
calsequestrin.
Calretinin is another type of Calcium binding protein weighing 29kD. It is involved in cell signaling and shown to exist in neurons. This type of protein is also found in large quantities in malignant mesothelial cells, which can be easily differentiated from
carcinomas. This differentiation is later applied for a diagnosis on ovarian stromal tumors. Also, another member of the EF-hand superfamily is the S100B protein, which regulates p53. P53 is known as a tumor suppressor protein and in this case acts as a transcriptional activator or repressor of numerous genes. S100B proteins are abundantly found in cancerous
tumor cells causing them to be overexpressed, therefore making these proteins useful for classifying tumors. In addition, this explains why this protein can easily interact with p53 when
transcriptional regulation takes place. Calcium-binding proteins can be either intracellular and extracellular. Those that are intracellular can contain or lack a structural EF-hand domain. Extracellular calcium-binding proteins are classified into six groups. ==Functions==