Receptor that plays a critical role in lung surfactant homeostasis. May play a role in controlling adipocyte function. Homodimer; disulfide-linked (PubMed:10391944). Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked (PubMed:11973329). Fragment generates by the processing enzyme furin remains attached to the extracellular N-terminal fragment (PubMed:16882675). Interacts (via N-terminal extracellular domain) with SFTPD (By similarity). Highly expressed in the lung and to a much lesser extent in the kidney and heart. Dense localization in alveolar walls of the lung and in the intercalated cells of the collecting duct of the kidney. Strongly induced postnatally. Proteolytically cleaved at multiple sites: one in the GPS domain (S1 site) and the other in the SEA domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. The proteolytic cleavage at S2 site generates a fragment that undergoes proteolytic cleavage by the processing enzyme furin. Highly glycosylated. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.