CDHR2 (cadherin-related family member 2) is an intermicrovillar adhesion molecule that forms calcium-dependent heterophilic complexes with CDHR5 on adjacent microvilli, thereby controlling microvillus packing and organization at the apical epithelial membrane 1. Through its extracellular domain, CDHR2 interacts with CDHR5, while its cytoplasmic domain engages microvillus proteins to form the intermicrovillar adhesion complex (IMAC), which plays a central role in brush border differentiation and microvillus stabilization 2. CDHR2 is enriched in intestinal tuft cells alongside IMAC components including CDHR5, Myosin 7b, and USH1C, regulating chemosensory microvillus organization 2. The protein also interacts with Harmonin through PDZ domain binding, a critical interaction relevant to Usher syndrome pathogenesis 3. Beyond epithelial function, CDHR2 serves as a proteomic biomarker for liver fat content and cardiometabolic disease risk 4, and is a key mediator protein in metabolic dysfunction-associated steatotic liver disease progression to liver fibrosis 5. CDHR2 is upregulated in lung adenocarcinoma and associated with poor prognosis 6, while its overexpression in breast cancer inhibits proliferation through PI3K/Akt pathway suppression 7, suggesting context-dependent roles in epithelial homeostasis and disease.