The mannose receptor family comprises four glycoproteins each of which is a type I transmembrane receptor with an N-terminal cysteine-rich domain, a single fibronectin type II (FNII) domain and eight to ten C-type lectin-like domains (CTLDs). Characteristically, these proteins are able to recycle between the plasma membrane and the endosomal apparatus due to discrete motifs present within their cytoplasmic domains. This review discusses the structure and function of these four proteins-the mannose receptor (MR), the M-type receptor for secretory phospholipases A(2) (PLA(2)R), DEC-205/gp200-MR6 and Endo180/uPARAP. Despite their overall structural similarity, these four receptors have evolved to use different domains to interact with discrete ligands. In addition, they differ in their ability to mediate endocytic and phagocytic events and in their intracellular destinations. Together, they represent a unique group of multidomain, multifunctional receptors.