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. Involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells (By similarity). 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. Interacts (via C-terminus intracellular tail region) with CIB1; the interaction is stabilized/increased in a calcium- and magnesium-dependent manner (By similarity). 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. Additional isoforms seem to exist. Expressed in skeletal and cardiac muscle. Expressed in replicating myoblasts. In differentiated muscle fibers localizes between fibers and the surrounding matrix. Isoform Alpha-7X1A and isoform Alpha-7X1B are expressed at myotendinous and neuromuscular junctions; isoform Alpha-7X1C is expressed at neuromuscular junctions and at extrasynaptic sites. Isoforms are developmentally regulated during the formation of skeletal muscle. Isoform Alpha-7X1A and isoform Alpha-7X1C are induced upon terminal myogenic differentiation; isoform Alpha-7X1B is present earlier in replicating cells and diminishes upon 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. Belongs to the integrin alpha chain family.