Yuasa H J, Furuta E, Nakamura A, Takagi T
Graduate School of Science, Tohoku University, Sendai, Japan.
Comp Biochem Physiol B Biochem Mol Biol. 1998 Mar;119(3):479-84. doi: 10.1016/s0305-0491(98)00008-x.
Three C-type lectins of 15 kDa were isolated from the water-soluble fraction (WSF) of the body surface mucus of the land slug, Incilaria fruhstorferi. Based on their partial amino acid sequences, the nucleotide sequences of cDNAs encoding these lectins, named incilarin A, B and C, were determined. cDNAs of incilarin A, B and C consisted of 673, 663 and 715 bp, and deduced amino acids were 150, 149 and 156 residues, respectively. All three lectins had signal peptides of 17 amino acid residues at their N-termini. They showed 44-55% amino acid sequence identity with each other, and lower but significant homology with the other animal C-type lectins and antifreeze protein. Incilarin A and B seem to possess two intramolecular disulfide bonds in the carbohydrate-binding domain (CRD) conserved among the animal C-type lectins, however, one of these bonds is absent in incilarin C.
从陆地蛞蝓Incilaria fruhstorferi体表黏液的水溶性部分（WSF）中分离出三种15 kDa的C型凝集素。根据它们的部分氨基酸序列，确定了编码这些凝集素（分别命名为incilarin A、B和C）的cDNA的核苷酸序列。incilarin A、B和C的cDNA分别由673、663和715 bp组成，推导的氨基酸分别为150、149和156个残基。所有这三种凝集素在其N端都有17个氨基酸残基的信号肽。它们彼此之间的氨基酸序列同一性为44-55%，与其他动物C型凝集素和抗冻蛋白有较低但显著的同源性。Incilarin A和B似乎在动物C型凝集素保守的碳水化合物结合结构域（CRD）中具有两个分子内二硫键，然而，incilarin C中缺少其中一个键。
