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 EMILIN3 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.