EMILIN1 is a structural extracellular matrix protein essential for elastic fiber assembly and collagen network organization 1. Localized at the interface between fibrillin microfibrils and elastin core, EMILIN1 facilitates EFEMP2 deposition and regulates collagen cross-linking through modulation of LOX activity 1. The protein exhibits cell-adhesive capacity and may anchor smooth muscle cells to elastic fibers, contributing to vascular integrity [UniProt]. EMILIN1 additionally functions as a TGF-β inhibitor in the tumor microenvironment, with high expression correlating with enhanced CD8+ T-cell infiltration and improved breast cancer prognosis 2. Bi-allelic loss-of-function EMILIN1 variants cause arterial tortuosity-bone fragility syndrome, characterized by cutis laxa, aortic aneurysm formation, and osteopenia 1. Disease pathology involves impaired elastogenesis, reduced collagen cross-linking, aberrant growth factor signaling, and abnormal trabecular bone formation 1. EMILIN1 mutations also associate with distal hereditary motor neuronopathy autosomal dominant 10 3. EMILIN1 polymorphisms show age-dependent associations with hypertension risk in certain populations, though results remain inconsistent 45. Notably, EMILIN1 can form homo- and hetero-multimers with EMILIN2 through N- and C-terminal domain interactions, potentially regulating complex tissue assembly 6.