Butyrophilin, subfamily 3, member A1

Butyrophilin subfamily 3 member A1 is a protein that in humans is encoded by the BTN3A1 gene.^[3][4] BTN3A1 protein is involved in innate immunity in primates and other mammals to protect them against pathogens and cancer.

BTN3A1
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 4F80, 4F9L, 4F9P, 4JKW, 4K55, 4N7I, 4N7U, 4V1P
Identifiers
Aliases	BTN3A1, BT3.1, BTF5, BTN3.1, CD277, Butyrophilin, subfamily 3, member A1, butyrophilin subfamily 3 member A1
External IDs	OMIM: 613593; HomoloGene: 56016; GeneCards: BTN3A1; OMA:BTN3A1 - orthologs
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p22.2 Start 26,402,237 bp[1] End 26,415,208 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte spleen pancreatic ductal cell lymph node monocyte blood rectum gallbladder appendix epithelium of colon n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding signaling receptor binding Cellular component integral component of membrane membrane plasma membrane external side of plasma membrane Biological process activated T cell proliferation T cell receptor signaling pathway adaptive immune response immune system process regulation of immune response Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11119 n/a Ensembl ENSG00000026950 n/a UniProt O00481 n/a RefSeq (mRNA) NM_001145008 NM_001145009 NM_007048 NM_194441 n/a RefSeq (protein) NP_001138480 NP_001138481 NP_008979 NP_919423 n/a Location (UCSC) Chr 6: 26.4 – 26.42 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Function

The intracellular domain of BTN3A1 protein binds intracellular phosphoantigens. Accumulation of phosphoantigens such as isopentenyl Pyrophosphate (IPP) is a universal sign of cellular stress or infection by an intracellular bacterium. The binding of phosphoantigens to BTN3A1 leads to an allosterically mediated change in conformation of BTN3A1's extracellular domain. This changed conformation is detected by the T cell receptor on cytotoxic gamma delta T cells, which can then kill the stressed or infected cell.^[5]