SIGNR1 is a type II transmembrane C-type lectin that was identified in a search for mouse homologues of human DC-SIGN. It is expressed at high levels in splenic marginal zone macrophages and lymph node medullary macrophages, where it functions to uptake dextran polysaccharides, including the capsular polysaccharide of Streptococcus pneumoniae. It has also been demonstrated that SIGNR1 physically associates with TLR4/MD2, and it has been suggested that this association plays a role in recognition of LPS. Furthermore, recently it has been shown that SIGNR1 deficient mice have a defect in catabolism of the complement component C3, and that SIGNR1 binds directly to the complement C1 subcomponent, C1q to assemble a non-conventional C3 convertase.
CD209; CD209 antigen-like protein B; CDSIGN; CIRE; DC-SIGN-related protein 1; DC-SIGNR1; Dcsign; MGC130443; OtB7; SIGN-R1; SIGNR5
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