The human FPR1 gene encodes the N-formyl peptide receptor, a G protein
-coupled receptor (GPCR) that mediates the activation of mature myeloi
d cells by bacterial N-formyl oligopeptides. To investigate the molecu
lar basis for myeloid-specific production of this receptor, we have cl
oned and sequenced FPR1. The gene is organized into three exons and tw
o introns that span 6 kb. The coding block lacks introns. Yet, the tra
nscription start point (tsp) is separated from the start codon by 4902
bp consisting of three exons and two large introns. Two mRNAs are pro
duced by alternative splicing of exon 2 in HL-60 neutrophils and norma
l blood monocytes. The region 5' to the tsp contains three pyrimidine-
rich segments, a feature that has been observed in other myeloid-speci
fic genes. One complete Alu repeat is found in each intron and in the
3'-flanking region 317 bp downstream of the polyadenylation signal. Th
us, FPR1 is a small myeloid-specific gene that is expressed as two alt
ernatively spliced mRNAs encoding the same protein.