CALML1

CALML1, or calmodulin-like protein 1, is a human protein encoded by the CALML1 gene. It belongs to the EF-hand calcium-binding protein family and is structurally similar to calmodulin, containing motifs that bind calcium ions. As a result, CALML1 functions as an intracellular calcium sensor and contributes to calcium signaling in various cellular contexts.

Functionally, CALML1 participates in translating changes in intracellular calcium levels into regulatory signals. In its calcium-bound form, it can interact with a range of target proteins to modulate enzyme activity, ion channel function, and other signaling processes. The exact targets and outcomes of CALML1-mediated regulation can be tissue- and context-dependent, reflecting the diverse roles of calcium signaling in cells.

Expression of CALML1 is broad, with detected mRNA and protein in many tissues. It is commonly described as cytosolic, though its localization can vary with calcium status and cellular environment. As with other calmodulin-like proteins, CALML1 likely participates in complex signaling networks and may influence neuronal signaling and muscle-related processes, among other functions.

Evolutionarily, CALML1 is conserved across vertebrates, underscoring a preserved role in calcium-mediated regulation. It forms part of a family of calmodulin-like proteins that expand the repertoire of intracellular calcium sensors beyond canonical calmodulin.

Clinical significance regarding CALML1 is not dominated by a single disease association; research generally emphasizes its function as a modulator of calcium signaling and its potential roles in cellular processes across tissues. Further studies are ongoing to clarify its specific targets and physiological impact.