The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-12A (C-type lectin domain family 12, member A), also known as CLL1, MICL, CLL-1 or DCAL-2, is a 275 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Existing as multiple alternatively spliced isoforms that are expressed in neutrophils, eosinophils, monocytes and dendritic cells, CLEC-12A functions as a cell surface receptor that acts as a negative regulator of granulocyte and monocyte function and, via this activity, modulates signaling cascades. CLEC-12A is highly subject to post-translational glycosylation at its N-terminus and may also exist as a homodimer.