Amino acid sequence of a C-type lectin CEL-IV from the marine invertebrate Cucumaria echinata.
The complete amino acid sequence of a Ca(2+)-dependent lectin, CEL-IV, from the marine invertebrate Cucumaria echinata was analyzed. The established sequence showed that CEL-IV comprises 157 amino acid residues with a molecular mass of 17,098 Da (without disulfide bonds). From comparison with other proteins, CEL-IV was apparently homologous with the C-type lectin family. The identity was relatively high with a sea cucumber (Stichopus japonicus) lectin SJL-I (40.0%) and a sea urchin (Anthocidaris crassispina) lectin echinoidin (32.6%). In CEL-IV, one interchain and two intrachain disulfide bonds were identified. Interestingly, one of the two intrachain disulfide bonds that were highly conserved among the other C-type lectins was missing, suggesting that this might be a characteristic feature of C-type lectins in the Holothuroidea.
Hatakeyama
T
T
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Ohuchi
K
K
Kuroki
M
M
Yamasaki
N
N
D000595:Amino Acid Sequence; D000818:Animals; D003063:Cnidaria / Q000737:chemistry; D003488:Cyanogen Bromide; D003545:Cysteine / Q000032:analysis; D004220:Disulfides / Q000032:analysis; D010450:Endopeptidases; D006868:Hydrolysis; D037102:Lectins / Q000032:analysis*; D037181:Lectins, C-Type; D008969:Molecular Sequence Data; D012616:Sea Cucumbers / Q000737:chemistry*; D012617:Sea Urchins / Q000737:chemistry
C095642:CEL-IV, Cucumaria echinata; D004220:Disulfides; D037102:Lectins; D037181:Lectins, C-Type; D010450:Endopeptidases; D003545:Cysteine; D003488:Cyanogen Bromide