Neurexophilin 2 (NXPH2)

Comparison of the amino acid sequences of human, rat, mouse, and bovine neurexophilins revealed that neurexophilins share a common predicted structure composed of 5 domains: an N-terminal signal peptide, a variable N-terminal domain, a highly conserved central domain that is N-glycosylated, a short linker region, and a conserved C-terminal domain that is cysteine-rich. Northern blot analysis of a variety of human tissues detected NXPH2 expression in brain and kidney. Missler and Sudhof (1998) concluded that neurexophilins form a family of related glycoproteins that are proteolytically processed after synthesis. They suggested that neurexophilins are signaling molecules that resemble neuropeptides and that act by binding to alpha-neurexins and possibly other receptors.