Annexin V is a phospholipase A2 and protein kinase C inhibitory protei
n with calcium channel activity and an undefined role in cellular sign
al transduction, inflammation, growth and differentiation. Three genom
ic clones for human annexin V (ANX5) were characterized by restriction
analysis, Southern blotting and sequencing. ANX5 spans al least 29 kb
of the human genome and contains 13 exons ranging in length from 44 t
o 513 bp and 12 introns from 232 bp to 8 kb. The absence of a typical
TATA box and the presence of high GS C content and Spl-binding sites i
n its promoter characterize it as a 'housekeeping' gene and account fo
r its broad pattern of expression. Potential binding sites for cis-reg
ulatory elements identified in the 5'-upstream region of annexin V are
consistent with its known regulation by oncogenic and growth-related
stimuli. ANX5, like its chick homologue, differs from the genes encodi
ng annexins I, II and III in features of its promoter and in the size
of its exons 1, 2 and 3 in ways that may impart individuality to its r
egulation and function.