The carbohydrate recognition domain (CRD) of the following proteins shares a striking structural similarity with calcium-dependent L-type (leguminous) lectins:

• Yeast proteins EMP46 and EMP47, type I membrane proteins, which cycle between the endoplasmic reticulum (ER) and the Golgi apparatus by vesicles coated with coat protein complexes I and II (COPI and COPII). They are considered to function as cargo reveptors for exporting N-linked glycoproteins from the ER.
• Animal p58/ERGIC-53, a calcium-dependent lectin that cycles between the endoplasmic reticulum (ER) and the Golgi complex and appears to act as a cargo receptor for a subset of soluble glycoproteins exported from the ER.
• Mammalian vesicular-integral protein of 36 kDa (VIP36), a transport lectin for trafficking certain high-mannose type glycoproteins in the early secretory pathway.

The L-type lectin-like domain has an overall globular shape composed of a β-sandwich of two major twisted antiparallel β-sheets (see <PDB:1GV9>). The β-sandwich comprises a major concave β-sheet and a minor convex β-sheet, in a variation of the jelly roll fold [1,2,3,4].

The profile we developed covers the entire L-type lectin-like domain.