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InterPro: IPR000922 D-galactoside/L-rhamnose binding SUEL lectin

Protein matchesHelp
UniProtKB
Matches:
554 proteins
AccessionHelp IPR000922 Lectin_gal_bd
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR003924 GPCR, family 2, latrophilin
GO Term annotationHelp
Function GO:0005529 sugar binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The D-galactoside binding lectin purified from sea urchin (Anthocidaris crassispina) eggs exists as a disulphide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity [1]. The sea urchin egg lectin (SUEL) forms a new class of lectins. Although SUEL was first isolated as a D-galactoside binding lectin, it was latter shown that it bind to L-rhamnose preferentially [1, 2]. L-rhamnose and D-galactose share the same hydroxyl group orientation at C2 and C4 of the pyranose ring structure.

A cysteine-rich domain homologous to the SUEL protein has been identified in the following proteins [3, 4, 5]:

  • Plant beta-galactosidases (EC:3.2.1.23) (lactases).
  • Mammalian latrophilin, the calcium independent receptor of alpha-latrotoxin (CIRL). The galactose-binding lectin domain is not required for alpha-latratoxin binding [5].
  • Human lectomedin-1.
  • Rhamnose-binding lectin (SAL) from catfish (Silurus asotus, Namazu) 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 [2].
  • The hypothetical B0457.1, F32A7.3A and F32A7.3B proteins from Caenorhabditis elegans.
  • The human KIAA0821 protein.

Database linksHelp
PROSITE doc: PDOC50228
PANDIT: PF02140
Blocks: IPB000922

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000922 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O94910 Latrophilin-1

P86179 L-rhamnose-binding lectin CSL3

Q0INM3 Beta-galactosidase 15

Q80TR1 Latrophilin-1

Q8GX69 Beta-galactosidase 16

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017983 GPCR, family 2, secretin-like, conserved site
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR003112 Olfactomedin-like
IPR000832 GPCR, family 2, secretin-like
IPR017981 GPCR, family 2-like
IPR000203 GPS domain
IPR001944 Glycoside hydrolase, family 35
IPR008979 Galactose-binding domain-like
IPR003334 GPCR, family 2, latrophilin, C-terminal
IPR000922 D-galactoside/L-rhamnose binding SUEL lectin
IPR017853 Glycoside hydrolase, catalytic core
IPR003924 GPCR, family 2, latrophilin
IPR019801 Glycoside hydrolase, family 35, conserved site
IPR001879 GPCR, family 2, extracellular hormone receptor domain
PDB Chain
ModBase
SWISS-MODEL

PublicationsHelp
1. Ozeki Y, Matsui T, Suzuki M, Titani K.
Amino acid sequence and molecular characterization of a D-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs.
Biochemistry 30 2391-4 1991 [PubMed: 2001368]
http://dx.doi.org/10.1021/bi00223a014
2. Hosono M, Ishikawa K, Mineki R, Murayama K, Numata C, Ogawa Y, Takayanagi Y, Nitta K.
Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs.
Biochim. Biophys. Acta 1472 668-75 1999 [PubMed: 10564781]
http://dx.doi.org/10.1016/S0304-4165(99)00185-3
3. Lelianova VG, Davletov BA, Sterling A, Rahman MA, Grishin EV, Totty NF, Ushkaryov YA.
Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors.
J. Biol. Chem. 272 21504-8 1997 [PubMed: 9261169]
http://dx.doi.org/10.1074/jbc.272.34.21504
4. Tateno H, Saneyoshi A, Ogawa T, Muramoto K, Kamiya H, Saneyoshi M.
Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily.
J. Biol. Chem. 273 19190-7 1998 [PubMed: 9668106]
http://dx.doi.org/10.1074/jbc.273.30.19190
5. Krasnoperov V, Bittner MA, Holz RW, Chepurny O, Petrenko AG.
Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants.
J. Biol. Chem. 274 3590-6 1999 [PubMed: 9920906]
http://dx.doi.org/10.1074/jbc.274.6.3590

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InterPro 23.1