|
Resolution: standard / high Figure 1.
Schematic representation of the primary structure of several members of the ACE protein
family. The locations of the active-site zinc-binding motifs are indicated by HEXXH;
transmembrane domains are in black. The sequence of gACE is identical to that of the
C domain of sACE, except for its first 36 residues. Human gACE and sACE have the same
carboxy-terminal transmembrane and cytosolic sequences, whereas ACE2 has a distinct
transmembrane and cytosolic sequence. Neither of the Drosophila ACEs, AnCE and Acer, has a membrane-anchoring sequence. Dimensions are not to scale.
N, amino terminus; C, carboxyl terminus. The single lines are regions of sequence
with no similarity to other proteins. The carboxyl end of ACE2 is homologous to collectin,
a non-enzymatic protein associated with renal injury [18].
Riordan Genome Biology 2003 4:225 doi:10.1186/gb-2003-4-8-225 |