Caldesmon Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration. Belongs to the caldesmon family. High-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular-weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart. 6 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Actin-binding
Cellular Component:  cell; cytoskeleton; myofibril
Molecular Function:  actin binding; calmodulin binding; myosin II binding; S100 protein binding
Biological Process:  muscle contraction; negative regulation of calcium-dependent ATPase activity
Reference #:  P12957 (UniProtKB)
Alt. Names/Synonyms: CAD; CALD1; Caldesmon; caldesmon 1; CDM; L-caldesmon; Non-muscle caldesmon
Gene Symbols: CALD1
Molecular weight: 88,747 Da
Basal Isoelectric point: 5.56  Predict pI for various phosphorylation states
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Caldesmon

Protein Structure Not Found.

Cross-references to other databases:  STRING  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene