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C-type lectin domain family 18 member C (CLEC18C) is a protein encoded in humans by the CLEC18C gene on chromosome 16q22. It is one of three closely related proteins in the CLEC18 family and is primarily found in the Golgi apparatus, endoplasmic reticulum, and endosome within cells[1][2][3][6]. CLEC18C is a secreted glycoprotein with a C-type lectin-like domain (CTLD) and a SCP/TAPS/CAP domain, both of which mediate interactions with carbohydrates and possibly glycolipids. CLEC18C specifically binds polysaccharides—including fucoidan, beta-glucans, and galactans—in a calcium-independent fashion[1][2][7]. It is abundantly expressed in human peripheral blood leukocytes, with expression upregulated during differentiation to macrophages and dendritic cells. While evidence suggests a potential role in modulating immune responses and glycolipid metabolism, direct roles in human disease or as a drug target have not yet been established[1].
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