Figure 1 of Han, Mol Vis 2011; 17:1381-1396.


Figure 1. Alignment of the predicted protein sequences of three X. laevis prominin homologs, showing characteristic features of prominins, including the pentaspan transmembrane topology, a conserved cysteine rich domain, conserved leucine residues and N-glycosylation sites. We designated the three X. laevis prominin homologs as xlProminin-1, 2, and 3, respectively. Identical and conserved residues are indicated by differentially shaded boxes. Predicted transmembrane domains are marked with M#. The predicted signal peptides of xlProminin-1 and 2 are boxed. No signal peptide was predicted for xlProminin-3. Positions of alternatively spliced exons are indicated by arrows and the sequences of the alternatively spliced exons are given. Note that the N- and C-termini of the three X. laevis prominin homologs are less conserved than other regions. Cysteine residues at the junction of M1 and the first intracellular domain (I1) are marked with yellow. Conserved leucine residues of the three xlProminin homologs are marked with red. Conserved glycosylation sites are marked with green.