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Tetraspanin 11 is a small integral membrane glycoprotein characterized by four transmembrane domains, a small extracellular loop (EC1), and a large extracellular loop (EC2) containing a conserved Cysteine-Cysteine-Glycine (CCG) motif, which is important for structural stability via disulfide bonding[1][2][3]. Tetraspanins in general are involved in organizing protein complexes and microdomains at the cell surface and regulate processes such as migration, adhesion, and cell signaling by interacting with a diverse array of partner proteins, including integrins, immunoglobulin superfamily members, and enzymes[1]. Although some tetraspanins are well-documented for their disease involvement and as drug targets, there is a paucity of functional data specifically relating to tetraspanin 11, and its physiological and pathological roles remain poorly defined.
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