Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix. (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human rotavirus A. (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human echoviruses 1 and 8. Heterodimer of an alpha and a beta subunit. Alpha-2 associates with beta-1. Interacts with HPS5 and RAB21. (Microbial infection) Integrin ITGA2:ITGB1 interacts (via ITAG2 I-domain) with rotavirus A VP4 protein. (Microbial infection) Integrin ITGA2:ITGB1 interacts with human echoviruses 1 and 8 capsid proteins. The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage. Position 534 is associated with platelet-specific alloantigen HPA-5 (Br). HPA-5B/Br(a) has Lys-534 and HPA-5A/Br(b) has Glu-534. HPA-5B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP). The Lys-534-Glu polymorphism may play a role in coronary artery disease (CAD). Belongs to the integrin alpha chain family.