Angiotensinogen (1-14), human, also known as angiotensin precursor, is a serum globulin synthesized by the liver that is hydrolyzed by renin to form angiotensin I,

Angiotensinogen (1-14), human (AGT), the common precursor of the angiotensin peptide family, consists of 485 amino acids in humans, with the N-terminal 33 amino acids serving as a signal peptide. Renin specifically cleaves amino acids 34-43 (the 10th residue after the signal peptide is removed) to release angiotensin I (AngI), which then generates a variety of bioactive peptides through a cascade reaction. Notably, this enzymatic cleavage mechanism is conserved across species—most mammalian AGTs can be recognized and cleaved by human renin, and synthetic peptides containing only the N-terminal sequence can mimic the function of the natural substrate. This property suggests that the N-terminal domain of AGT plays a crucial role in renin recognition. [1-2]