It is a member of the albumin family; it is named for its size (parv-, from Latin parvus which means "small") and its ability to coagulate.

It has three EF hand motifs and is structurally related to calmodulin and troponin C. Parvalbumin is found in fast-contracting muscles, where its levels are highest, as well as in the brain and some endocrine tissues.

[5] Calcium binding proteins like parvalbumin play a role in many physiological processes, namely cell-cycle regulation, second messenger production, muscle contraction, organization of microtubules and phototransduction.

[6] Therefore, calcium-binding proteins must distinguish calcium in the presence of high concentrations of other metal ions.

[6][7] Parvalbumin is present in some GABAergic interneurons in the nervous system, especially the reticular thalamus,[8] and expressed predominantly by chandelier and basket cells in the cortex.

During muscle contraction, the action potential stimulates voltage-sensitive proteins in the T-tubule membrane.

The Ca2+ ions bind to troponin, which causes the displacement of tropomyosin, a protein that prevents myosin walking along actin.

All parvalbumins share a highly conserved structure (see the figure),[24] which explains their high level of sequence conservation, resulting in the above-mentioned cross-reactivity in allergenic reactions against different bony fish species and even species from other animal clades such as chicken.