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Available structures
PDBHuman UniProt search: PDBe RCSB
AliasesKLRC2, CD159c, NKG2-C, NKG2C, killer cell lectin like receptor C2
External IDsOMIM: 602891 HomoloGene: 135919 GeneCards: KLRC2
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 12: 10.43 – 10.44 Mbn/a
PubMed search[2]n/a
View/Edit Human

NKG2-C type II integral membrane protein or NKG2C is a protein that in humans is encoded by the KLRC2 gene.[3][4] It is also known as or cluster of differentiation 159c (CD159c).


Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. NK cells preferentially express several calcium-dependent (C-type) lectins, which have been implicated in the regulation of NK cell function. The group, designated KLRC (NKG2) are expressed primarily in natural killer (NK) cells and encodes a family of transmembrane proteins characterized by a type II membrane orientation (extracellular C terminus) and the presence of a C-type lectin domain. The KLRC (NKG2) gene family is located within the NK complex, a region that contains several C-type lectin genes preferentially expressed on NK cells. KLRC2 alternative splice variants have been described but their full-length nature has not been determined.[4]


KLRC2 has been shown to interact and form dimers with CD94.[5][6] The CD94/NKG2C heterodimer can bind to HLA-E [7][8] and this binding leads to NK cells activation.

During infection with human cytomegalovirus, peptides derived from the virus are presented on HLA-E and natural killer cells that express the CD94/NKG2C receptor can specifically recognise the virus peptides. This recognition leads to activation, expansion, and differentiation of adaptive NK cells.[9]

See also[edit]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000205809 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ Plougastel B, Trowsdale J (Apr 1998). "Sequence analysis of a 62-kb region overlapping the human KLRC cluster of genes". Genomics. 49 (2): 193–9. doi:10.1006/geno.1997.5197. PMID 9598306.
  4. ^ a b "Entrez Gene: KLRC2 killer cell lectin-like receptor subfamily C, member 2".
  5. ^ Lazetic S, Chang C, Houchins JP, Lanier LL, Phillips JH (Dec 1996). "Human natural killer cell receptors involved in MHC class I recognition are disulfide-linked heterodimers of CD94 and NKG2 subunits". Journal of Immunology. 157 (11): 4741–5. PMID 8943374.
  6. ^ Ding Y, Sumitran S, Holgersson J (May 1999). "Direct binding of purified HLA class I antigens by soluble NKG2/CD94 C-type lectins from natural killer cells". Scandinavian Journal of Immunology. 49 (5): 459–65. doi:10.1046/j.1365-3083.1999.00566.x. PMID 10320637. S2CID 28500838.
  7. ^ Braud VM, Allan DS, O'Callaghan CA, Söderström K, D'Andrea A, Ogg GS, Lazetic S, Young NT, Bell JI, Phillips JH, Lanier LL, McMichael AJ (Feb 1998). "HLA-E binds to natural killer cell receptors CD94/NKG2A, B and C.". Nature. 391 (6669): 795–9. Bibcode:1998Natur.391..795B. doi:10.1038/35869. PMID 9486650. S2CID 4379457.
  8. ^ Lee N, Llano M, Carretero M, Ishitani A, Navarro F, López-Botet M, Geraghty DE (Apr 1998). "HLA-E is a major ligand for the natural killer inhibitory receptor CD94/NKG2A". PNAS. 95 (9): 5199–204. Bibcode:1998PNAS...95.5199L. doi:10.1073/pnas.95.9.5199. PMC 20238. PMID 9560253.
  9. ^ Hammer Q, Rückert T, Borst EM, Dunst J, Haubner A, Durek P, Heinrich F, Gasparoni G, Babic M, Tomic A, Pietra G, Nienen M, Blau IW, Hofmann J, Na IK, Prinz I, Koenecke C, Hemmati P, Babel N, Arnold R, Walter J, Thurley K, Mashreghi MF, Messerle M, Romagnani C (May 2018). "Peptide-specific recognition of human cytomegalovirus strains controls adaptive natural killer cells". Nature Immunology. 19 (5): 453–463. doi:10.1038/s41590-018-0082-6. PMID 29632329. S2CID 4718187.

Further reading[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.