Interleukin-13 receptor subunit alpha-1(IL-13RA1), also known as NR4, belongs to the hemopoietin receptor family. Interleukin-13 receptor is a complex of IL4R, IL13RA1, and possibly other components. It interacts with TRAF3IP1 and binds with low affinity to interleukin-13(IL3). IL-13RA1, together with IL4RA, can form a functional receptor for IL13. It also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity. The WSXWS motif in domains appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Interleukin-4 receptor subunit alpha(IL-4RA), alos known as Soluble IL-4 receptor subunit alpha, belongs to the type I cytokine receptor family and type 4 subfamily. It expressed in both Th1 and Th2 cells. It functions as receptor for both interleukin 4 and interleukin 13 and couples to the JAK1 2 3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4 IL13 responses are involved in regulating IgE production and chemokine and mucus production at sites of allergic inflammation. In certain cell types, IL-4RA can signal through activation of insulin receptor substrates, IRS1 IRS2. The functional IL4 receptor is formed by initial binding of IL4 to IL4R. Subsequently it recruits to the complex of the common gamma chain. In immune cells, IL-4RA creates a type I receptor. In non-immune cells, it forms a type II receptor with of IL13RA1. IL4R can also interact with the IL13 IL13RA1 complex to form a similar type II receptor and interacts with the SH2-containing phosphatases, PTPN6 SHIP1, PTPN11 SHIP2 and INPP5D SHIP.