This gene encodes a G protein-coupled receptor cell surface protein that binds and is activated by N-Formylmethionine-containing oligopeptides, particularly N-Formylmethionine-leucyl-phenylalanine (FMLP).

Two receptors where thereafter discovered and named FPR2 and FPR3 based on the similarity of their genes' predicted amino acid sequence to that of FPR1 rather than on any ability to bind or be activated by the formyl oligopeptides.

[16] The studies indicated that FPR1 is a G protein-coupled receptor that activates cells though a linkage to the pertussis toxin-sensitive Gαi subclass of G proteins, that FPR1 is located on chromosome 19q.13.3, and that this gene consists of two exons, the first of which encodes a 66 base pair 5'-untranslated sequence, the second of which has an intronless open reading frame coding for a protein containing ~354 amino acids; the studies also indicated that cells express multiple formyl peptide receptor mRNA transcripts due to Allelic heterogeneity, alternate Polyadenylation sites, and possibly products of other genes with homology to FPR1.

Since ψFpr-rs2 transcripts are expressed and inducible in multiple mouse tissues and since gene knockout studies ascribe functionality to it, ψFpr-rs2 may not a true pseudogene and, it is suggested, should be renamed Fpr-rs8.

[26] Fpr-rs1, Fpr-rs3, Fpr-rs4, Fpr-rs6, and Fpr-rs7 receptors are expressed in the olfactory bulb sensory neurons of the Vomeronasal organ where they have been shown to respond to their known ligands, FMLP and lipoxin A4.

These results suggest that the cited receptors function to allow the olfactory-based detection of various contaminated compounds such as spoiled food and/or their many inflammation-regulating and other agonists in bodily secretions.

[29] The effect of these gene knockouts appeared due to faulty leukocyte function and other causes leading to a breakdown in the innate immune response.