PROSITE documentation PDOC51328
L-type lectin-like (leguminous) domain profile


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.

Last update:

August 2007 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

L_LECTIN_LIKE, PS51328; L-type lectin-like (leguminous) domain profile  (MATRIX)


1AuthorsVelloso L.M. Svensson K. Schneider G. Pettersson R.F. Lindqvist Y.
TitleCrystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum.
SourceJ. Biol. Chem. 277:15979-15984(2002).
PubMed ID11850423

2AuthorsVelloso L.M. Svensson K. Pettersson R.F. Lindqvist Y.
TitleThe crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding.
SourceJ. Mol. Biol. 334:845-851(2003).
PubMed ID14643651

3AuthorsSatoh T. Sato K. Kanoh A. Yamashita K. Yamada Y. Igarashi N. Kato R. Nakano A. Wakatsuki S.
TitleStructures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p.
SourceJ. Biol. Chem. 281:10410-10419(2006).
PubMed ID16439369

4AuthorsSatoh T. Cowieson N.P. Hakamata W. Ideo H. Fukushima K. Kurihara M. Kato R. Yamashita K. Wakatsuki S.
TitleStructural basis for recognition of high-mannose type glycoproteins by mammalian transport lectin VIP36.
SourceJ. Biol. Chem. 0:0-0(2007).
PubMed ID17652092

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)