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Beschreibung

Alpha-Parvin (UniProt: Q9NVD7, also known as Actopaxin, CH-ILKBP, Calponin-like integrin-linked kinase-binding protein, Matrix-remodeling-associated protein 2) is encoded by the PARVA (also known as MXRA2) gene (Gene ID: 55742) in human. a-Parvin is a widely expressed, highly conserved, peripheral membrane protein that is highly expressed in heart, skeletal muscle, kidney, and liver. It contains two calponin-homology (CH1 and CH2) domains that are localized in amino acids 95-202 and 262-369. It interacts with the carboxy terminal of integrin-linked kinase (ILK) via its CH2 domain and deletion of its CH2 domain is reported to abolish its ability to localize to focal adhesions. a-Parvin plays a role in sarcomere organization and in smooth muscle cell contraction and is also required for normal development of the embryonic cardiovascular system. It is also essential for normal septation of the heart outflow tract. a-Parvin also plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development. It is also reported to play a role in establishing cell polarity, reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. (Ref.: Tu, Y., et al. (2001). J. Cell Biol. 153(3), 585-598).