Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (By similarity). Required for Ndg localization to the basement membrane (PubMed:30260959). Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Found in the basement membranes (major component). In the larva, expressed mainly by fat body adipocytes and blood cells and secreted in the basal membranes that surround the fat body, imaginal disks, tracheae, salivary glands, midgut, mature muscles and heart (at protein level). The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. Domains VI and IV are globular. Results in strong reduction of Ndg accumulation at the basement membrane in the gut, muscles and ventral nerve cord (PubMed:30260959). RNAi-mediated knockdown in the larvae reduces Ndg accumulation and created holes in the basal membrane of fat bodies (PubMed:30260959). Truncated N-terminus.