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Beschreibung

Interleukin-13 receptor subunit alpha-1 (UniProt: O09030, also known as IL-13 receptor subunit alpha-1, IL-13R subunit alpha-1, IL-13R-alpha-1, IL-13RA1, Interleukin-13-binding protein, Novel cytokine receptor 4, NR4, CD213a1) is encoded by the Il13ra1 (also known as Il13r, Il13ra) gene (Gene ID: 16164) in murine species. Interleukin 13 (IL-13) is a T cell derived cytokine involved in the regulation of inflammatory and immune responses. IL-13RA1 is a single-pass type I membrane protein that binds with low affinity to interleukin-13 (IL13). Together with IL-4RA it forms a functional receptor for IL13. It is also reported to serve 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 (IL-2) binding activity. IL13-RA1 is expressed I Spleen, liver, thymus, heart, lung, kidney, testis, stomach, brain, skin, and colon. However, is not expressed in the skeletal muscle. It is also shown to bind tyrosine kinase TYK2, and thereby mediate the signaling processes that lead to the activation of JAK1, STAT3, and STAT6 induced by IL-13 and IL-4. IL-13RA1 is synthesized with a signal peptide (aa 1-25) that is cleaved off to produce mature form. It contains an extracellular domain (aa 26-340), a helical domain (aa 341-364), and a cytoplasmic region (aa 365-424). It also contain two fibronectin type III domains (aa 32-121 and 224-336). The WSXWS motif (aa 324-328) appears to be essential for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.