Protein: Galactose/N-acetylgalactosamine-binding lectin CEL-III (Gal/GalNAc-binding lectin CEL-III) (CEL-III) (Hemolytic lectin CEL-III) (Lectin CEL-III) (Q868M7)
Organism: Pseudocnus echinatus (Sea cucumber) (Cucumaria echinata)
Function: Galactose/N-acetylgalactosamine (Gal/GalNAc)-binding lectin with hemolytic activity. Favors saccharides that have a beta-1,4 linkage at the non-reducing end rather than saccharides having alpha-1,6 or alpha-1,4 linkages. Binds lactose, lactulose, GalNAc, galactosamine, methyl alpha-galactopyranoside, methyl beta-galactopyranoside, N-acetyllactosamine, p-nitrophenyl beta-D-galactopyranoside (pNP-Gal), p-nitrophenyl N-acetyl-beta-D-galactosaminide (pNP-GalNAc), asialofetuin, and human erythrocyte membrane lipids lactosyl ceramide (LacCer) and globoside globotetraosylceramide (Gb4Cer). Binds moderately to galactose, melibiose, raffinose, fucose, methyl alpha-galactoside and methyl beta-galactoside. Binds weakly to glucose, mannose and N-acetylglucosamine (GlcNAc). Has hemolytic activity towards human (A, B and O-type), rabbit and rat erythrocytes, but not towards mouse, chicken or horse erythrocytes. Forms ion-permeable transmembrane pores in the erythrocyte membrane as well as in artificial liposomes containing human erythrocyte membrane lipids LacCer, Gb4Cer and galactosyl ceramide (GalCer) leading to destruction of the membrane. Has hemagglutinating activity towards rabbit, human and rat erythrocytes, and at relatively high concentrations towards chicken and horse erythrocytes, but not towards mouse erythrocytes. Has dose-dependent cytotoxic effect on Madin-Darby canine kidney (MDCK), African green monkey kidney (Vero) and human epithelia carcinoma (HeLa) cell lines, but Chinese hamster ovary (CHO), rat sarcoma (XC) and potoroo rat kangaroo kidney (PtK1) cells are highly resistant to the cytotoxic effect of this protein. Impairs malaria parasite development in malaria parasite infected transgenic A.stephensi mosquitoes expressing this protein specifically in their midguts. Binds to ookinetes and leads to strong dose-dependent inhibition of ookinete formation in vitro. Leads to severely impaired oocyst formation and significantly reduced sporozoite production of rodent malaria parasite P.berghei in the salivary glands of the transgenic mosquitoes. The parasite transmission to uninfected mice (vectorial competence) of these mosquitoes is significantly impaired. Leads also to severely impaired oocyst formation of human malaria parasite P.falciparum in transgenic mosquitoes fed on mature P.falciparum gametocyte cultures. May be involved in defense mechanisms acting as a toxic protein to foreign microorganisms. May act in defense against predators.
Subcellular location: Secreted {ECO:0000269|PubMed:10101284, ECO:0000269|PubMed:10478454, ECO:0000269|PubMed:11471734, ECO:0000269|PubMed:14561725, ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:18159942, ECO:0000269|PubMed:22313748, ECO:0000269|PubMed:24652284, ECO:0000269|PubMed:7876091, ECO:0000269|PubMed:8663224, ECO:0000269|PubMed:9058193, ECO:0000269|PubMed:9133626, ECO:0000269|PubMed:9305736}.
Interaction partners:
Sequence:
MVSLVPCGFAQVLCTNPLDIGELRNYKSKQCVDIVGNQGSGNIATHDCDGLSDQQIIMCGDGTIRNEARNYCFTPDGSGNANVMSSPCTLYPEIPSSQRWRLGRKKAFTDNGGIEQVATEIINLASGKCLDVEGSDGTGDIGVYDCQNLDDQYFYIRSRGPELFYGRLRNEKSDLCLDVEGSEGKGNVLMYSCEDNLDQWFRYYENGEIVNAKQGMCLDVEGSDGSGNVGIYRCDDLRDQMWSRPNAYCNGDYCSFLNKESNKCLDVSGDQGTGDVGTWQCDGLPDQRFKWVFDDWEVPTATWNMVGCDQNGKVSQQISNTISFSSTVTAGVAVEVSSTIEKGVIFAKASVSVKVTASLSKAWTNSQSGTTAITYTCDNYDSDEEFTRGCMWQLAIETTEVKSGDLLVWNPQIIKCTRSNTAPGCAPFTKCANEDCTFCTDI