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SERPINA2 encodes a member of the serpin family—a group of serine protease inhibitors. It is an intracellular glycoprotein localized to the endoplasmic reticulum, and shares substantial homology with the alpha-1-antitrypsin gene (SERPINA1). Most contemporary human populations carry inactive or deleted alleles, and there is no evidence for a functional extracellular protein in circulation. Phylogenetic analysis suggests SERPINA2 diverged from SERPINA1 in primates and has undergone positive selection, possibly linked to alternative cellular functions in the ER, such as chymotrypsin-like activity or interaction with ER chaperones. SERPINA2 is not associated with known diseases and is not considered a pharmacological target, receptor, or enzyme for drug development. It is sometimes erroneously listed as a functional protein due to its close similarity with alpha-1-antitrypsin, but current evidence places it predominantly as a polymorphic pseudogene with possible intracellular functions.
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