In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. Highly thermostable. Not degraded by heating at 140 degrees Celsius for 20 min. Expressed in both white and dark muscles (at protein level). About eight and a half times lower expression in the dark muscle than in the white muscle (at protein level). The N-terminus is blocked. Causes an allergic reaction in human (PubMed:12842183, PubMed:16436146, Ref.4, Ref.5, Ref.6, PubMed:27041301). Binds to IgE in patients allergic to fish parvalbumin (PubMed:16436146, PubMed:27041301, Ref.4, Ref.6). Binds to IgE in 80% of 5 fish-allergic patients tested (PubMed:12842183). IgE reactivity linearly decreases with the increase in heating temperature (from 40 to 140 degrees Celsius). More than 50% reduction of allergenicity by heating at 80 degrees Celsius and almost complete loss of allergenicity by heating at 140 degrees Celsius (PubMed:27041301). IgE reactivity of 12 fish-allergic patients tested is significantly reduced (60-100% reduction) in the presence of EGTA as a result of Ca(2+) depletion (Ref.5). Belongs to the parvalbumin family.