Official Full Name
interleukin 6 signal transducer
Glycoprotein 130 (also known as gp130, IL6ST, IL6-beta or CD130) is a transmembrane protein which is the founding member of the class of all cytokine receptors. It forms one subunit of type I cytokine receptors within the IL-6 receptor family. It is often referred to as the common gp130 subunit, and is important for signal transduction following cytokine engagement. As with other type I cytokine receptors, gp130 possesses a WSXWS amino acid motif that ensures correct protein folding and ligand binding. It interacts with Janus kinases to elicit an intracellular signal following receptor interaction with its ligand. Structurally, gp130 is composed of five fibronectin type-III domains and one immunoglobulin-like C2-type (immunoglobulin-like) domain in its extracellular portion.
IL6ST; CD130; CDW130; GP130; IL-6RB; Interleukin 6 signal transducer (gp130, oncostatin M receptor); interleukin-6 receptor subunit beta; CD130 antigen; IL-6R subunit beta; membrane glycoprotein 130; IL-6 receptor subunit beta; membrane glycoprotein gp130; interleukin receptor beta chain; oncostatin-M receptor subunit alpha; gp130 of the rheumatoid arthritis antigenic peptide-bearing soluble form; DKFZp564F053; CD130, GP130, CDW130, IL-6RB; glycoprotein 130; interleukin 6 signal transducer