{PDOC51328}
{PS51328; L_LECTIN_LIKE}
{BEGIN}
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* L-type lectin-like (leguminous) domain profile *
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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
beta-sandwich of  two major twisted antiparallel beta-sheets (see <PDB:1GV9>).
The beta-sandwich  comprises  a  major  concave  beta-sheet and a minor convex
beta-sheet, in a variation of the jelly roll fold [1-4].

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

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2007 / First entry.

[ 1] Velloso L.M., Svensson K., Schneider G., Pettersson R.F.,
     Lindqvist Y.
     "Crystal structure of the carbohydrate recognition domain of
     p58/ERGIC-53, a protein involved in glycoprotein export from the
     endoplasmic reticulum."
     J. Biol. Chem. 277:15979-15984(2002).
     PubMed=11850423; DOI=10.1074/jbc.M112098200
[ 2] Velloso L.M., Svensson K., Pettersson R.F., Lindqvist Y.
     "The 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."
     J. Mol. Biol. 334:845-851(2003).
     PubMed=14643651
[ 3] Satoh T., Sato K., Kanoh A., Yamashita K., Yamada Y., Igarashi N.,
     Kato R., Nakano A., Wakatsuki S.
     "Structures of the carbohydrate recognition domain of Ca2+-independent
     cargo receptors Emp46p and Emp47p."
     J. Biol. Chem. 281:10410-10419(2006).
     PubMed=16439369; DOI=10.1074/jbc.M512258200
[ 4] Satoh T., Cowieson N.P., Hakamata W., Ideo H., Fukushima K.,
     Kurihara M., Kato R., Yamashita K., Wakatsuki S.
     "Structural basis for recognition of high-mannose type glycoproteins
     by mammalian transport lectin VIP36."
     J. Biol. Chem. 0:0-0(2007).
     PubMed=17652092; DOI=10.1074/jbc.M703064200

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