Interleukin-13 receptor subunit alpha-2 (IL-13Rα2) (IL13RA2 (gene) / IL-13Rα2 (protein))

Interleukin-13 receptor subunit alpha-2 (IL-13Rα2) is a membrane protein encoded by IL13RA2 that binds IL-13 with femtomolar affinity and primarily functions as a decoy receptor lacking a canonical signaling cytoplasmic domain; it regulates IL-13 and IL-4 effects and can mediate alternative signaling via AP-1 leading to TGF-β1 production. It is overexpressed in several cancers (e.g., glioma, pancreatic, ovarian, melanoma), making it a therapeutic target and a biomarker for targeted immunotherapies. The queried “HLA-A2-restricted epitope presented to CD8+ T cells” refers to peptides derived from IL-13Rα2 that can be presented by HLA-A*02:01, enabling cytotoxic T-cell targeting of IL-13Rα2-expressing tumors, but this is not the canonical name of the receptor.

Other names

IL-13 receptor subunit alpha-2IL13RA2IL-13Rα2CD213A2Interleukin-13-binding proteinIL13R

Target engagement often exploits tumor-associated overexpression for selective delivery or immune recognition (e.g., antibody/CAR T binding to IL-13Rα2 extracellular domain), leveraging its decoy role and restricted normal expression pattern; general mechanistic framing from the receptor’s biology: high-affinity IL-13 binding and modulation of downstream cytokine signaling.