Ecto-ADP-ribosyltransferase 3 (ART3)

Ecto-ADP-ribosyltransferase 3 (ART3) is an arginine-specific mono(ADP-ribosyl)transferase enzyme found primarily at the cell surface or secreted, encoded by the ART3 gene in humans[3][5][2]. It catalyzes the transfer of ADP-ribose from NAD^+ onto protein arginine residues, a reversible posttranslational modification that can modulate the function of target proteins[2][5][1]. While biochemical activity has been demonstrated, the full physiological substrates and functions of ART3 remain incompletely understood. ART3 is part of the extracellular branch of the ADP-ribosyltransferase family and is mainly characterized by its MARylation (mono-ADP-ribosylation) activity rather than generating poly-ADP-ribose[1]. It has been investigated as a possible biomarker in the context of male fertility and some cancers, but has not been established as a therapeutic target, nor are there approved drugs targeting it[2]. There are no major safety concerns currently described for ART3-specific modulation. Key points: - ART3 is a member of the ART family, involved in mono-ADP-ribosylation, primarily targeting protein arginine residues. - Biological roles include protein modification, immune signaling, and potentially regulation of cellular interactions through the cell surface. - There are no established drugs or targeted therapies involving ART3, though research into ADP-ribosyltransferases as a class is ongoing. - Some data link ART3 to diseases like cancer and developmental disorders, but its precise pathological roles remain to be fully defined[2].

Other names

ART3TMARTARTC3ADP-ribosyltransferase C2 and C3 toxin-like 3Mono(ADP-ribosyl)transferase 3NAD(P)(+)--arginine ADP-ribosyltransferase 3mono-ADP-ribosyltransferase 3

Not applicable/none yet demonstrated, as ART3 is not a validated therapeutic drug target; in theory, inhibition or modulation of enzymatic activity would affect ADP-ribosylation status of proteins