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Poly(A)-specific ribonuclease subunit PAN3 (**PAN3**) is a conserved eukaryotic protein that serves as a regulatory/adaptor subunit within the PAN2–PAN3 deadenylation complex, which is responsible for shortening the 3′ poly(A) tails of cytoplasmic mRNAs—a key step controlling both general and microRNA-mediated mRNA decay[1][2][3][4]. The PAN3 protein contains a pseudokinase domain, a coiled-coil region, and a C-terminal knob domain, forming a homodimer that binds one PAN2 subunit to produce the functional deadenylase complex[1][2][3][4]. PAN3 binds RNA directly through multiple mechanisms (notably, zinc finger and PAM2 motifs), supplying substrate poly(A) RNA to the PAN2 deadenylase and mediating recruitment of the complex to specific mRNA targets via interactions with poly(A)-binding proteins (PABP) and GW182/TNRC6 proteins[1][2][4]. While PAN3 itself is not catalytically active as a kinase, it binds ATP, and this binding is thought to regulate conformational changes in the complex required for mRNA degradation[3][4]. PAN3's activity strongly influences the fate of mRNAs and thereby cell cycle progression, cell proliferation, and possibly disease states including cancer[1][2][3][4].
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