ULBP3

UL16 binding protein 3
PDB rendering based on 1kcg.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1KCG​
Identifiers
Symbols	ULBP3 ; RAET1N
External IDs	OMIM: 605699 HomoloGene: 129737 GeneCards: ULBP3 Gene
Gene ontology Molecular function • natural killer cell lectin-like receptor binding Cellular component • plasma membrane • anchored component of plasma membrane Biological process • viral process • antigen processing and presentation • natural killer cell activation • natural killer cell mediated cytotoxicity • regulation of immune response Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	79465	n/a
Ensembl	ENSG00000131019	n/a
UniProt	Q9BZM4	n/a
RefSeq (mRNA)	NM_024518	n/a
RefSeq (protein)	NP_078794	n/a
Location (UCSC)	Chr 6: 150.06 – 150.07 Mb	n/a
PubMed search		n/a

UL16 binding protein 3 (ULBP3) is a cell surface glycoprotein encoded by ULBP3 gene located on the chromosome 6.^[1][2] ULBP3 is related to MHC class I molecules, but its gene maps outside the MHC locus.^[1][2] The domain structure of ULBP3 differs significantly from those of conventional MHC class I molecules. It does not contain the α3 domain and the transmembrane segment. ULBP3 is thus composed of only the α1α2 domain which is linked to the cell membrane by the GPI anchor.^[1][2] It functions as a stress-induced ligand for NKG2D receptor.^[1]

References

1. Cosman D, Müllberg J, Sutherland CL, Chin W, Armitage R, Fanslow W, Kubin M, Chalupny NJ (Feb 2001). "ULBPs, novel MHC class I-related molecules, bind to CMV glycoprotein UL16 and stimulate NK cytotoxicity through the NKG2D receptor". Immunity 14 (2): 123–33. doi:10.1016/S1074-7613(01)00095-4. PMID 11239445.
2. Radosavljevic M, Cuillerier B, Wilson MJ, Clément O, Wicker S, Gilfillan S, Beck S, Trowsdale J, Bahram S (Jan 2002). "A cluster of ten novel MHC class I related genes on human chromosome 6q24.2-q25.3". Genomics 79 (1): 114–23. doi:10.1006/geno.2001.6673. PMID 11827464.

Further reading

• Cerwenka A, Lanier LL (May 2003). "NKG2D ligands: unconventional MHC class I-like molecules exploited by viruses and cancer". Tissue Antigens 61 (5): 335–43. doi:10.1034/j.1399-0039.2003.00070.x. PMID 12753652.
• Eleme K, Taner SB, Onfelt B, Collinson LM, McCann FE, Chalupny NJ, Cosman D, Hopkins C, Magee AI, Davis DM (Apr 2004). "Cell surface organization of stress-inducible proteins ULBP and MICA that stimulate human NK cells and T cells via NKG2D". The Journal of Experimental Medicine 199 (7): 1005–10. doi:10.1084/jem.20032194. PMC 2211882. PMID 15051759.
• Sutherland CL, Chalupny NJ, Schooley K, VandenBos T, Kubin M, Cosman D (Jan 2002). "UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D and activate multiple signaling pathways in primary NK cells". Journal of Immunology 168 (2): 671–9. doi:10.4049/jimmunol.168.2.671. PMID 11777960.
• Radaev S, Rostro B, Brooks AG, Colonna M, Sun PD (Dec 2001). "Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3". Immunity 15 (6): 1039–49. doi:10.1016/S1074-7613(01)00241-2. PMID 11754823.
• Steinle A, Li P, Morris DL, Groh V, Lanier LL, Strong RK, Spies T (2001). "Interactions of human NKG2D with its ligands MICA, MICB, and homologs of the mouse RAE-1 protein family". Immunogenetics 53 (4): 279–87. doi:10.1007/s002510100325. PMID 11491531.