Membrane Associated Ring Finger Protein 11 (MARCH11)

MARCH11 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases. These enzymes add ubiquitin to target lysines in substrate proteins, thereby signaling their intracellular transport. March11 appears to have a role in ubiquitin-mediated protein sorting in the trans-Golgi network (TGN)-multivesicular body (MVB) transport pathway. The deduced 398-amino acid protein contains an N-terminal proline-rich sequence, followed by a RING-CH finger domain, 2 transmembrane domains, and a C-terminal PDZ-binding domain. It also has a YxxL motif near its C terminus, suggesting that March11 may interact with adaptor protein complex-1 (AP1) mu subunits. Rat March11 shares highest similarity with rat and human MARCH4 and MARCH9.