[3][4] Even though intelectins contain fibrinogen-like domain found in the ficolins family of immune lectins, there is significant structural divergence.

[12] In addition, X. laevis embryos secrete Xenopus embryonic epidermal lectin into the environmental water, presumably to bind microbes.

[18] Several lines of evidence suggest that intelectins recognize microbes and may function as an innate immune defense protein.

[20][21] In zebrafish and rainbow trout, intelectin expression is stimulated upon microbial exposure.

[22][23][24] Mammals such as sheep and mice also upregulate intelectin expression upon parasitic infection.

Although intelectins require calcium ion for function, the sequences bear no resemblance to C-type lectins.

[3] In addition, merely around 50 amino acids (the fibronogen-like domain) align with any known protein, specifically the ficolin family.

In intelectin homologs where the N-terminal cysteines are absent, the CRD itself may still capable of forming non-covalent oligomer in solution.