CLEC2D
C-type lectin domain family 2 member D is a protein that in humans is encoded by the CLEC2D gene.[3]
CLEC2D | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | CLEC2D, CLAX, LLT1, OCIL, C-type lectin domain family 2 member D | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 605659 HomoloGene: 137257 GeneCards: CLEC2D | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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.[3] 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.
References
- GRCh38: Ensembl release 89: ENSG00000069493 - Ensembl, May 2017
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Entrez Gene: CLEC2D C-type lectin domain family 2, member D".
Further reading
- Boles KS, Barten R, Kumaresan PR, et al. (1999). "Cloning of a new lectin-like receptor expressed on human NK cells". Immunogenetics. 50 (1–2): 1–7. doi:10.1007/s002510050679. PMID 10541800. S2CID 30994521.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Iizuka K, Naidenko OV, Plougastel BF, et al. (2003). "Genetically linked C-type lectin-related ligands for the NKRP1 family of natural killer cell receptors". Nat. Immunol. 4 (8): 801–7. doi:10.1038/ni954. PMID 12858173. S2CID 23775959.
- Hu YS, Zhou H, Myers D, et al. (2004). "Isolation of a human homolog of osteoclast inhibitory lectin that inhibits the formation and function of osteoclasts". J. Bone Miner. Res. 19 (1): 89–99. doi:10.1359/JBMR.0301215. PMID 14753741. S2CID 28328386.
- Carlyle JR, Jamieson AM, Gasser S, et al. (2004). "Missing self-recognition of Ocil/Clr-b by inhibitory NKR-P1 natural killer cell receptors". Proc. Natl. Acad. Sci. U.S.A. 101 (10): 3527–32. Bibcode:2004PNAS..101.3527C. doi:10.1073/pnas.0308304101. PMC 373496. PMID 14990792.
- Mathew PA, Chuang SS, Vaidya SV, et al. (2004). "The LLT1 receptor induces IFN-gamma production by human natural killer cells". Mol. Immunol. 40 (16): 1157–63. doi:10.1016/j.molimm.2003.11.024. PMID 15104121.
- Gange CT, Quinn JM, Zhou H, et al. (2004). "Characterization of sugar binding by osteoclast inhibitory lectin". J. Biol. Chem. 279 (28): 29043–9. doi:10.1074/jbc.M312518200. PMID 15123656.
- Aldemir H, Prod'homme V, Dumaurier MJ, et al. (2006). "Cutting edge: lectin-like transcript 1 is a ligand for the CD161 receptor". J. Immunol. 175 (12): 7791–5. doi:10.4049/jimmunol.175.12.7791. PMID 16339512.
- Rosen DB, Bettadapura J, Alsharifi M, et al. (2006). "Cutting edge: lectin-like transcript-1 is a ligand for the inhibitory human NKR-P1A receptor". J. Immunol. 175 (12): 7796–9. doi:10.4049/jimmunol.175.12.7796. PMID 16339513.
- Rosen DB, Cao W, et al. (2008). "Functional Consequences of Interactions between Human NKR-P1A and Its Ligand LLT1 Expressed on Activated Dendritic Cells and B Cells". J. Immunol. 180 (10): 6508–6517. doi:10.4049/jimmunol.180.10.6508. PMC 2577150. PMID 18453569.