A. Shirvan et al., DIVERGENT STRUCTURE OF THE HUMAN SYNEXIN (ANNEXIN-VII) GENE AND ASSIGNMENT TO CHROMOSOME-10, Biochemistry, 33(22), 1994, pp. 6888-6901
The human synexin (annexin VII) gene occurs as a single copy at chromo
some 10q21.1-21.2 and substantially deviates in size and in the locati
on of splice junctions from the other two well-characterized members o
f the annexin gene family, lipocortin I (annexin I) and calpactin I (a
nnexin II). The synexin gene contains 14 exons, including an alternati
vely spliced cassette exon, and spans approximately 34 kb of DNA. Only
five of the fourteen splice junctions are conserved compared to other
annexins, and the differences are particularly pronounced in the exon
s that encode the C-terminal third and fourth conserved repeats in the
gene product. Although parallels between exons and protein domains we
re not apparent, we did observe clustering of splice junctions corresp
onding to either the unique N-terminal domain or the conserved C-termi
nal tetrad repeat domain, which is common to all annexins. Furthermore
, a complete analysis of the 5' flanking region of the annexin VII gen
e revealed an entirely different set of cis-acting and enhancer elemen
ts compared to other annexin genes. We conclude that the annexin VII g
ene may have arisen by a divergence from the evolutionary pathway take
n by both annexins I and II.