CLEC1A Gene - C-Type Lectin Domain Family 1 Member A | NCBI, UniProt, OMIM

CLEC1A (C-type lectin domain family 1 member A) encodes a type II transmembrane glycoprotein belonging to the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. The protein, also known as DCIR (dendritic cell immunoreceptor), is primarily expressed on dendritic cells, monocytes, macrophages, and NK cells. It functions as an inhibitory receptor via an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic tail, modulating immune responses by suppressing activation signals. CLEC1A is involved in antigen uptake, endocytosis, and regulation of inflammatory cytokine production. Genetic variants and altered expression have been linked to autoimmune diseases such as rheumatoid arthritis and systemic lupus erythematosus, as well as to certain cancers.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• KEGG: hsa04650 - Natural killer cell mediated cytotoxicity

• Reactome: R-HSA-168249 - Innate Immune System

• Reactome: R-HSA-6798695 - Neutrophil degranulation

CLEC1A encodes DCIR, a 237-amino-acid type II transmembrane protein with a single C-type lectin-like domain (CTLD) in the extracellular region and an ITIM motif in the cytoplasmic tail. The protein forms homodimers and recognizes carbohydrate ligands (e.g., mannose, fucose) on pathogens and self-glycoproteins. Upon ligand binding, DCIR recruits phosphatases such as SHP-1 and SHP-2 to attenuate activation signals, thereby limiting pro-inflammatory cytokine release. DCIR also mediates antigen internalization and presentation. Alternative splicing generates multiple isoforms, with the full-length isoform being the most abundant. Post-translational modifications include N-glycosylation at Asn-150, which is essential for ligand binding.