CLEC2D

CLEC2D
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	4QKG, 4QKH, 4QKI, 4QKJ, 4WCO
Identifiers
Aliases	CLEC2D, CLAX, LLT1, OCIL, C-type lectin domain family 2 member D
External IDs	OMIM: 605659; HomoloGene: 137257; GeneCards: CLEC2D; OMA:CLEC2D - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	9,699,553 bp
RNA expression pattern
	Top expressed in
	granulocyte; ; Achilles tendon; ; spleen; ; lymph node; ; blood; ; appendix; ; right uterine tube; ; epithelium of colon; ; monocyte; ; bone marrow cells;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	transmembrane signaling receptor activity; carbohydrate binding; protein binding;
Cellular component	plasma membrane; membrane; integral component of membrane; endoplasmic reticulum; integral component of plasma membrane; cell surface;
Biological process	regulation of immune response; cell surface receptor signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	29121
	n/a
	ENSG00000069493
	n/a
	Q9UHP7
	n/a
NM_001004419; NM_001004420; NM_001197317; NM_001197318; NM_001197319;
	NM_013269
	n/a
	NP_001004419; NP_001184246; NP_001184247; NP_001184248; NP_037401
	n/a
	Wikidata
View/Edit Human

C-type lectin domain family 2 member D is a protein that in humans is encoded by the CLEC2D gene.

This gene encodes a member of the natural killer cell receptor C-type lectin family. The encoded protein inhibits osteoclast formation and contains a transmembrane domain near the N-terminus as well as the C-type lectin-like extracellular domain. Several alternatively spliced transcript variants have been identified, but the full-length nature of every transcript has not been defined. CLEC2D encodes the gene for the Lectin Like Transcript-1 (LLT1) protein which is a functional ligand for the human NKR-P1A receptor, encoded by the KLRB1 gene. In mice, there are many orthologs of the CLEC2D gene, and the presumed homolog is Clr-b/Ocil (Clec2d). Clr-b has been implicated in missing-self recognition by natural killer cells through engagement of the NKR-P1B receptor.