Description
Product Characteristics:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. MARCH8 (membrane-associated ring finger (C3HC4) 8), also known as MIR or RNF178 (RING finger protein 178), is a 291 amino acid multi-pass membrane protein that localizes to vesicle membranes and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, including immature dendritic cells, MARCH8 functions as an E3 ubiquitin ligase that is thought to regulate immune responses by promoting the ubiquitination and subsequent degradation of target proteins, such as B7-2 and CD71.
Synonyms: c MIR, c-MIR, Cellular modulator of immune recognition, E3 ubiquitin protein ligase MARCH8, E3 ubiquitin-protein ligase MARCH8, MARCH 8, MARCH VIII, MARCH-VIII, MARCH8, MARH8_HUMAN, Membrane associated RING CH protein VIII, Membrane associated ring finger C3HC4 8, Membrane associated RING finger protein 8, Membrane-associated RING finger protein 8, Membrane-associated RING-CH protein VIII, MIR, RING finger protein 178, RNF178.
Target Information: MARCH8 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases (EC 6.3.2.19). MARCH enzymes add ubiquitin (see MIM 191339) to target lysines in substrate proteins, thereby signaling their vesicular transport between membrane compartments. MARCH8 induces the internalization of several membrane glycoproteins (Goto et al., 2003 [PubMed 12582153]\, Bartee et al., 2004 [PubMed 14722266]).[supplied by OMIM, Apr 2010]