AMINO-ACID-SEQUENCE OF A C-TYPE LECTIN CEL-IV FROM THE MARINE INVERTEBRATE CUCUMARIA-ECHINATA

The complete amino acid sequence of a Ca2+-dependent lectin, GEL-IV, f rom the marine invertebrate Cucumaria echinata was analyzed, The estab lished sequence showed that GEL-IV comprises 157 amino acid residues w ith a molecular mass of 17,098 Da (without disulfide bonds), From comp arison with other proteins, GEL-IV was apparently homologous with the C-type lectin family, The identity was relatively high with a sea cucu mber (Stichopus japonicus) lectin SJL-I (40.0%) and a sea urchin (Anth ocidaris is crassispina) lectin echinoidin (32.6%), In GEL-IV, one int erchain and two intrachain disulfide bonds were identified, Interestin gly, one of the two intrachain disulfide bonds that were highly conser ved among the other C-type lectins was missing, suggesting that this m ight he a characteristic feature of C-type lectins in the Holothuroide a,