Emilins (elastin microfibril interface located proteins) are extracellular matrix glycoproteins that localize to sites with proximity to elastin and microfibrils. They consist of an N-terminal cysteine-rich EMI domain and a conserved C-terminal gC1q-like domain. Emilin-1 is abundant in elastin-rich tissues such as blood vessels, skin, heart and lung. It influences placenta formation and initial organogenesis with a later role in interstitial connective tissue. Emilin-2 is larger than Emilin-1 and contains a unique proline-rich domain. It is likely involved in the process of elastogenesis. Multimerin-2 (also known as Emilin-3 or EndoGlyx-1) is expressed during embryonic development. Multimerin-1 (also known as Emilin-4) is expressed in platelets and the endothelium of blood vessels and may act as a carrier protein for platelet factor V. Emilin-5 is encoded by the Emilin-3 gene and is sometimes referred to as Emilin-3. It contains the N-terminal cysteine-rich EMI domain but lacks the C-terminal gC1q-like domain. Emilin-5 is expressed in human mesenchymal stem cells and plays an important role in skeletal development.