Intrinsically disordered proteins (IDPs) undergo functional liquid-liquid phase separation in living cells. A random-phase-approximation (RPA) theory for sequence-specific electrostatics in IDP phase separation is presented. RPA is applied to study binodal and spinodal phase behaviors of neutral polyampholytes and the RNA helicase Ddx4. Various phase separation theories are compared with one another as well as Ddx4 phase separation experiments. A concentration-dependent permittivity in protein solution is explored as a cooperative effect in favor of phase separation.