SGIP1 is a member of the muniscin family. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis [], and is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15 [].The muniscins are a family of endocytic adaptors that is conserved from yeast to humans. Their C-terminal domain is structurally similar to mu homology domains (MHDs), and is the region of the muniscin proteins involved in the interactions with the endocytic adaptor-scaffold proteins Ede1-eps15 []. This entry represent the mu-homology domain (MHD) of SGIP1. Unlike other muniscins, SGIP1 does not contain the EFC/F-BAR domain, but does have a proline-rich domain (PRD) and a C-terminal MHD.
