Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF. Signals probably through G-proteins. Forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety. Interacts with chondroitin sulfate; the interaction with chondroitin sulfate is calcium-dependent. Interacts with CD55 (By similarity). Localized at the leading edge of migrating cells. The GPS domain is necessary, but not sufficient for receptor cleavage, which require the entire extracellular stalk. Binding to chondroitin sulfate is mediated by the fourth EGF domain. Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane beta subunit. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.