CRYZ (crystallin zeta) encodes a multifunctional protein with both structural and enzymatic roles. As an enzyme, CRYZ functions as an NADPH-dependent quinone oxidoreductase involved in xenobiotic detoxification 1. The protein demonstrates tissue-specific expression patterns, being highly expressed in the lens of certain mammals (camelids and hystricomorph rodents like guinea pigs) where it serves as a structural crystallin protein, comprising up to 10% of total soluble lens protein 12. In humans, CRYZ is located on chromosome 1-p31 and shows different evolutionary recruitment patterns compared to other species 32. The gene spans approximately 20 kb with nine exons and lacks typical TATA and CAAT promoter boxes 1. Recent studies suggest broader biological roles beyond the lens, with genetic variants near CRYZ being associated with circulating resistin levels, which may influence cardiovascular disease risk 4. Additionally, CRYZ has been implicated in neuropsychiatric disorders through epigenetic mechanisms, with methylation patterns associated with tic spectrum disorders and birth-weight discordance potentially affecting metabolic pathways 56. The protein's dual crystallin-enzyme function represents an example of evolutionary recruitment of metabolic enzymes for structural roles in specific tissues.