Chicken annexin V (anchorin CII) is a collagen binding, membrane-associated molecule with Ca2+ channel activity. Here we report on the coding sequences, promoter region, size and distribution of exons, and exon-intron junctions of the chicken annexin V gene. It is about 25 kb long and codes for 13 short exons between 50 and 581 bp length. Exon sizes and locations of splice sites are almost completely homologous to those of the human and mouse annexin II or pigeon annexin I genes, although there is only 50-60% homology in the sequence of the corresponding proteins. The four repeat structure and symmetry of the annexin V as evident from sequence and X-ray analysis studies is only partially reflected in this highly conserved exon distribution. In the first two repeats of chicken annexin V the exons correlate with protein domains containing one, two, or three alpha-helices, while in the repeats 3 and 4 exon junctions and alpha-helical domains do not correlate. The analysis of the promoter structure revealed the absence of a typical TATA-box, but a GC-rich region which may possibly promote transcription from several start sites.