In this paper we show the organisation of the Drosophila gene encoding a Go
lgi alpha-mannosidase II. We demonstrate that it encodes a functional homol
ogue of the mouse Golgi a-mannosidase II. The Drosophila and mouse cDNA seq
uences translate into amino acid sequences which show 41% identity and 61%
similarity. Expression of the Drosophila GMII sequence in CHOP cells produc
es an enzyme which has mannosidase activity and is inhibited by swainsonine
and by CuSO4. In cultured Drosophila cells and in Drosophila embryos, anti
bodies raised against a C-terminal peptide localise this product mainly to
the Golgi apparatus as identified by cryo-immuno electron microscopy studie
s and by antibodies raised against known mammalian Golgi proteins. We discu
ss these results in terms of the possible use of dGMII as a Drosophila Golg
i marker.