Component of an integrin containing attachment complex, which is required for muscle development and maintenance (PubMed:22253611). Probable structural role in myofilament assembly and/or attachment of the myofilament lattice to the cell membrane (PubMed:8393416, PubMed:11438655, PubMed:17326220). May be an extracellular anchor for integrin receptors in body wall muscles and myoepithelial sheath cells (PubMed:8393416, PubMed:17326220). During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably downstream of the integrin complex formed by pat-2 and pat-3 (PubMed:16495308). Involved in ovulation (PubMed:17326220). Component of an integrin containing attachment complex, composed of at least pat-2, pat-3, pat-4, pat-6, unc-52, unc-97 and unc-112. In body wall muscles, colocalizes to dense bodies and M lines with beta-integrin pat-3 (PubMed:10512861). In myoepithelial sheath cells, colocalizes in dense body-like structures with actin thin filaments and pat-3 (PubMed:17326220). Detected on embryonic and adult body wall muscle cells (at protein level) (PubMed:8393416, PubMed:10512861). Found in the basement membrane of all contractile tissues (at protein level) (PubMed:10512861). Expressed in gonadal sheath cells and spermatheca (PubMed:17326220). Synthesized early in embryogenesis. RNAi-mediated knockdown in L4 larval stage, causes a small increase in ectopic membrane extensions from body wall muscles (PubMed:16495308). RNAi-mediated knockdown causes an accumulation in the proximal gonad of endomitotic mature oocytes in 30 percent of animals (PubMed:17326220). RNAi-mediated knockdown results in impaired mobility, mitochondrial fragmentation, and disrupted integrin attachment complexes in muscle (PubMed:22253611). This leads to degradation of muscle proteins in the cytosol, myofibrillar defects and disruption of sarcomere organization (PubMed:22253611).