InterPro domain: IPR033275

This entry includes human E3 ubiquitin-protein ligase MARCH proteins (MARCH1/2/3/4/5/8/9/11), and virus proteins (MIR1, MIR2, LAP and VIE1) that share homology with the MARCH proteins [ 1 , 2 ].

Human MARCH1 mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies [ 3 ]. Virus MIR1 has been shown to function as an E3 ubiquitin ligase for immune recognition-related molecules [ 4 ].

1. Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J. Virol. 78, 1109-20
2. c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity. J. Biol. Chem. 278, 14657-68
3. Interleukin-10-induced MARCH1 mediates intracellular sequestration of MHC class II in monocytes. Eur. J. Immunol. 38, 1225-30
4. A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J. Cell Biol. 155, 1265-73