Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta (PubMed:27339457). In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin (By similarity). Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction (PubMed:18973305, PubMed:19570982). Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling (PubMed:23782690). Homodimer; disulfide-linked (PubMed:19570982, PubMed:23782690). Multimer; allows heparin binding (PubMed:23782690). Monomer (By similarity). Interacts with FBN1 (via N-terminal domain); this interaction inhibits EFEMP2 binding to LOX and ELN (PubMed:17255108, PubMed:19349279, PubMed:19570982). Interacts with LOX (via propeptide); this interaction is strong and facilitates formation of ternary complexes with ELN during elastic fiber assembly; this interaction limits interaction of EFEMP2 with FBLN5 (PubMed:19855011, PubMed:19570982, PubMed:27339457). Interacts with PITX2 (PubMed:22919265). Interacts with ELN with moderate affinity; this interaction regulates ELN self-assembly maturation stage (PubMed:19570982). Interacts with FBLN5 with moderate affinity (PubMed:19570982). Interacts with LOXL1 (via propeptide), LTBP1 and TGFB1 stronger than with LOXL2 and LTBP3 (PubMed:27339457). Interacts with PCOLCE (By similarity). Interacts with collagen type IV trimer (COL4A1-COL4A1-COL4A2), NID2 and moderately with COL15A1-derived endostatin (By similarity). Interacts with EMILIN1; this interaction promotes the incorporation of EFEMP2 into the extracellular matrix (By similarity). Interacts with LTBP4; the LTBP4 long form (LTBP4L) has a stronger binding affinity than the LTBP4 short form and the LTBP4 long form promotes fibrillar deposition of EFEMP2 (PubMed:27339457). Localizes on the microfibrils surrounding ELN cores. N-glycosylated; contains mostly complex-type glycans (PubMed:27339457, PubMed:23782690). Not O-glycosylated (PubMed:27339457). Cleaved by ELANE; produces a 50-55 kDa fragment (PubMed:27339457). Cleaved by MMP2 and MMP9; produces several fragments (PubMed:27339457). The disease is caused by variants affecting the gene represented in this entry. Belongs to the fibulin family.