PS50228

SUEL-type lectin domain profile

PROSITE profiles entry
Member databasePROSITE profiles
PROSITE profiles typedomain
Short nameSUEL_LECTIN

Description

Lectins bind to specific carbohydrate residues of glycoproteins and glycolipids present at the cell surface. This allow them to agglutinate a variety of cellular types. On the basis of sequence similarity and common characteristics such as sugar binding specificity, conserved carbohydrate recognition domains, and ion requirement the different lectins can be grouped in different categories, like C-type, I-type, galectins, pentraxins and P-type lectin. The sea urchin (Anthocidaris crassispina) egg lectin (SUEL) forms a new class of lectins. Altough SUEL was first isolated as a D-galactoside binding lectin it was latter shown that it bind to L-rhamnose preferentially
[5]
[4]
. L- rhamnose and D-galactose share the same hydroxyl group orientation at C2 and C4 of the pyranose ring structure. SUEL is a lectin that exist as a disulfide linked homodimer. The dimeric form is essential for hemagglutination activity but the monomeric form retains carbohydrate binding capacity
[5]
. Based on primary structure analysis, a cysteine-rich domain homologous to the SUEL protein has been identified in the following proteins
[1]
[2]
[3]
: - Plant beta-galactosidases (EC 3.2.1.23) (lactases). They constitute a widespread family of enzymes characterized by their ability to hydrolyse terminal, non-reducing beta D-galactosyl residues from beta-D-galactosides. - Mammalian latrophilin, the calcium independent receptor of alpha- latrotoxin (CIRL). It belongs to the secretin family of G-protein coupled receptors. The lectin domain is not required for alpha-latratoxin binding
[3]
. - Human lectomedin-1. - Rhamnose-binding lectin (SAL) from catfish (Parasilurus asotus) eggs. This protein is composed of three tandem repeat domains homologous to the SUEL lectin domain. All cysteine positions of each domain are completely conserved
[4]
. - Caenorhabditis elegans hypothetical proteins B0457.1, F32A7.3A and F32A7.3B. - Human hypothetical protein KIAA0821.

References

1.Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors. Lelianova VG, Davletov BA, Sterling A, Rahman MA, Grishin EV, Totty NF, Ushkaryov YA. J. Biol. Chem. 272, 21504-8, (1997). View articlePMID: 9261169

2.Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily. Tateno H, Saneyoshi A, Ogawa T, Muramoto K, Kamiya H, Saneyoshi M. J. Biol. Chem. 273, 19190-7, (1998). View articlePMID: 9668106

3.Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants. Krasnoperov V, Bittner MA, Holz RW, Chepurny O, Petrenko AG. J. Biol. Chem. 274, 3590-6, (1999). View articlePMID: 9920906

4.Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs. Hosono M, Ishikawa K, Mineki R, Murayama K, Numata C, Ogawa Y, Takayanagi Y, Nitta K. Biochim. Biophys. Acta 1472, 668-75, (1999). View articlePMID: 10564781

5.Amino acid sequence and molecular characterization of a D-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs. Ozeki Y, Matsui T, Suzuki M, Titani K. Biochemistry 30, 2391-4, (1991). View articlePMID: 2001368

Integrated to
External Links
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.