| Type: | Family | Name: | Senescence marker protein-30 (SMP-30) |
| Description: | Regucalcin, also known as senesence marker protein-30 (SMP30), was discovered in 1978 as a Ca2+binding protein that does not contain EF-hand motifs, suggesting a novel class of Ca2+binding protein. It is primarily localised to the liver and kidney cortex of animals. Expression of its mRNA in the liver and renal cortex of rats is stimulated by an increase in cellular Ca2+levels [, ]. Regucalin, as a regulatory protein of Ca2+, has a pivotal role in the control of many cell functions. The protein has a reversible effect onCa2+-induced activation and inhibition of many enzymes in both the liver and renal cortex cells []. It has also been shown to inhibit various proteinkinases (including Ca2+/calmodulin-dependent protein kinase [], proteinkinase C [] and tyrosine kinase) and protein phosphatases, indicating aregulatory role in signal transduction within the cell. In addition, regucalcin regulates intracellular Ca2+homeostasis by enhancing Ca2+- pumping activity in the plasma membrane through activation of the pumpenzymes []. Moreover, it can inhibit RNA synthesis in the nuclei of normal and regenerating rat livers in vitro [].Hydropathy profiles indicate hydrophobic domains in both N- and C-terminal regions of the regucalcin molecule; the protein also exhibits hydrophilic characteristics. Human and rodent regucalcins share 89% sequence identity, the high degree of conservation between species suggesting that the complete structure is required for physiological function. | Short Name: | SMP-30 |
