Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B promote myoblast migration on laminin 1 and laminin 2/4, but isoform Alpha-7X1B is less active on laminin 1 (In vitro). Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity). Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells. Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-7 associates with beta-1. Interacts with COMP (By similarity). Interacts (via C-terminus intracellular tail region) with CIB1; the interaction is stabilized/increased in a calcium- and magnesium-dependent manner. Additional isoforms seem to exist. There is a combination of at least five alternatively spliced domains, three extracellular (X1, X2 and D) and two cytoplasmic (A and B). A third potential alternatively spliced cytoplasmic domain (C) does not appear to be expressed. Isoforms containing segment A are predominantly expressed in skeletal muscle. Isoforms containing segment B are abundantly expressed in skeletal muscle, moderately in cardiac muscle, small intestine, colon, ovary and prostate and weakly in lung and testes. Isoforms containing segment X2D are expressed at low levels in fetal and adult skeletal muscle and in cardiac muscle, but are not detected in myoblasts and myotubes. In muscle fibers isoforms containing segment A and B are expressed at myotendinous and neuromuscular junctions; isoforms containing segment C are expressed at neuromuscular junctions and at extrasynaptic sites. Isoforms containing segments X1 or X2 or, at low levels, X1X2 are expressed in fetal and adult skeletal muscle (myoblasts and myotubes) and cardiac muscle. In renewing intestinal epithelium, expression of isoforms containing segment B correlates with the onset of enterocytic differentiation. ADP-ribosylated on at least two sites of the extracellular domain in skeletal myotubes. A 70 kDa form is created by proteolytic cleavage. Cleavage is elevated during myogenic differentiation and the cleaved form enhances cell adhesion and spreading on laminin. The disease is caused by variants affecting the gene represented in this entry. Belongs to the integrin alpha chain family.