This is then followed by a nucleophilic attack by a hydroxide ligand on the bound phosphorus atom, resulting in cleavage of the phosphate ester bond and production of an alcohol.

[9][10] In newborn rats, TRAP is also detectable in the spleen, thymus, liver, kidneys, skin, lung, and heart at low levels.

Transcribed from this gene is a 1.5kb mRNA with an open reading frame (ORF) of 969-975 bp encoding a 323-325 amino acid protein.

These result in thickening and shortening of the cortices, formation of club-like deformities in the distal femur, and widened epiphyseal growth plates with delayed mineralization of cartilage, all of which increase with age.

[15] In TRAP overexpressing transgenic mice, mild osteoporosis occurs along with increased osteoblast activity and bone synthesis.

[16] Proposed functions of TRAP include osteopontin /bone sialoprotein dephosphorylation, the generation of reactive oxygen species (ROS), iron transport, and as a cell growth and differentiation factor.

Genetic deficiency of TRAP, determined by biallelic recessive mutations in the ACP5 gene, are the basis of the human disorder spondylenchondrodysplasia.

TRAP, containing a redox active iron, catalyzes the generation of ROS through Fenton chemistry:[21] producing hydroxyl radicals, hydrogen peroxide, and singlet oxygen.

[22] Due to the unique anatomy of the porcine uterus, and the specific, progesterone-induced expression of TRAP; it is hypothesized that uteroferrin acts as an iron transport protein.