Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This protein combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as inactivated-C3b (iC3b) receptor 4 (CR4). The alpha X beta 2 complex seems to overlap the properties of the alpha M beta 2 integrin in the adherence of neutrophils and monocytes to stimulated endothelium cells, and in the phagocytosis of complement coated particles. Two transcript variants encoding different isoforms have been found for this gene.
Functional IL-2 receptors can exist in two affinity states on cell surfaces, the high affinity complex consisting of heterotrimers of the alpha, beta, and gamma chains and the intermediate affinity complex comprising heterodimers of the beta and gamma chains. Individual beta chains and alpha chains exhibit low affinity IL-2 binding, and the gamma chain alone does not bind IL-2. In addition to their involvement in IL-2 mediated signal transduction, both the beta chain and gamma chain have been shown to be required for IL-15 mediated signaling. IL-2 R beta is a member of the cytokine receptor superfamily.
The protein encoded by this gene is a plasma membrane protein that is important in spermatogenesis, embryo implantation, neural network formation, and tumor progression. The encoded protein is also a member of the immunoglobulin superfamily. Multiple transcript variants encoding different isoforms have been found for this gene.
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