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Description

Calponin-1 (UniProt: P51911, also known as Basic calponin, Calponin H1 smooth muscle) is encoded by the CNN1 gene (Gene ID:1264) in human. Calponin is an actin filament-associated regulatory protein that is expressed in smooth muscle and non-muscle cells of vertebrates. Three isoforms of Calponin have been reported that inhibit actin-activated myosin ATPase activity and stabilize the actin cytoskeleton. Calponin 1 is specifically expressed in smooth muscle cells is involved in fine-tuning of smooth muscle contractility. Calponin-2 is found in multiple cell types, including developing smooth muscles and Calponin-3 is found in the neurons, astrocytes and glial cells. Calponin-1 can bind to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 (and other calponins) has a calponin homology (CH) domain at its N-terminal (aa 28-131) that can function either as a part of actin-binding site or serve as a regulatory structure for actin-binding activity. It also has three calponin-like domains (aa 164-189, 204-229, and 243-268) next to the C-terminal region that are conserved in all calponins. The C-terminal segment varies among different calponins and has differentiated effects on weakening the binding of calponin to F-actin. Deletion of the C-terminal tail segment is shown to enhance the actin-binding and bundling activities of calponins. (Ref.: Liu, R., and Jin, J-P (2016). Gene 585(1), 143-153).