calmodulinlike

Calmodulinlike refers to proteins that resemble calmodulin in sequence and function. They are members of the EF-hand calcium-binding protein family and typically act as calcium sensors that transduce Ca2+ signals to cellular responses. The term is often used for a broad set of calmodulin-like proteins found across eukaryotes, including plants, fungi, and animals.

Most calmodulin-like proteins contain one or more EF-hand motifs—helix-loop-helix domains that bind calcium. Calmodulin itself has four EF-hands arranged in two globular domains; calmodulin-like proteins show variation in the number of EF-hands, overall length, and terminal extensions, resulting in diverse calcium-binding properties and target interactions. In plants, for example, the calmodulin-like (CML) gene family comprises many members with tissue-specific expression and distinct response profiles to developmental cues and environmental stimuli.

Functionally, calmodulin-like proteins bind Ca2+ and undergo conformational changes that enable them to interact with and regulate a variety of target enzymes and other proteins, including kinases, phosphatases, and transcriptional regulators. Through these interactions, they participate in processes such as growth, development, stress responses, and metabolism. They can provide specificity in calcium signaling due to differences in expression patterns and target compatibility among family members.

Distribution and significance vary by organism but broadly include a wide range of eukaryotes, from yeast to plants and animals. Differences from the archetypal calmodulin lie mainly in sequence divergence and functional specialization among family members, contributing to organism- and tissue-specific calcium signaling networks. Calmodulin-like proteins are active areas of research for understanding Ca2+-dependent regulation and for potential agricultural and biomedical applications.