Collagen Type XXVI (COL26)

Sato et al. (2002) cloned mouse Emid2, which they called Col26a1, by yeast 2-hybrid analysis using Hsp47 as bait. The deduced 438-amino acid protein contains an N-terminal signal sequence, followed by 3 noncollagenous domains separated by 2 collagenous domains. Emid2 has 13 cysteine residues in the N-terminal portion of the first noncollagenous region and 2 clusters of gly-X-Y collagen-like repeats. Sato et al. (2002) determined that mouse Emid2 shows collagen-like characteristics, including hydroxylation and N-glycosylation. The N-glycans were found to be modified to more complex forms in the Golgi apparatus before secretion. In addition, Emid2 formed trimers that were secreted into the culture medium of transfected human embryonic kidney cells.