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Dcar (dendritic cell immuno-activating receptor) is a type II calcium-dependent (C-type) lectin localized in the natural killer (NK) gene complex in the telomeric region of murine chromosome 6. It is a 209 amino acid-long membrane glycoprotein with a single C-terminal carbohydrate recognition domain (CRD) and no immunoreceptor typrosine-based inhibitory motif (ITIM) in the N-terminal cytoplasmic tail. A positively-charged arginine residue is present in the transmembrane domain, which may explain the association between Dcar and the Fc receptor g chain and its stable expression on the cell surface.
Based on the genomic structure and the predicted functional domains, a targeting vector was designed where the first two exons were floxed by cre-recombinase recognition sites, removing the cytoplasmic, trans-membrane and neck domains.
