Cartilage oligomeric matrix protein (COMP) is an abundant component in the extracellular matrix (ECM) of load-bearing tissues such as tendons and cartilage. It serves adaptor functions by bridging different ECM structures. We previously showed that COMP is also a constitutive component of healthy human skin and strongly induced in fibrosis. It binds directly and with high affinity to collagen I and to collagen XII that decorates the surface of collagen I fibrils. We demonstrate here that lack of COMP-collagen interaction in the extracellular space leads to changes in collagen fibril morphology and density resulting in altered skin biomechanical properties. Surprisingly, COMP also fulfills an important intracellular function in assisting efficient secretion of collagens, which were retained in the endoplasmic reticulum of COMP-null fibroblasts. Accordingly COMP-null mice showed severely attenuated fibrotic responses in skin. Collagen secretion was fully restored by introducing wild type COMP. Hence, our work unravels a novel, non-structural and intracellular function of the ECM protein COMP in controlling collagen secretion.