Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:32573437). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (PubMed:34012115). Also acts indirectly by mediating the recruitment of the LUBAC complex, which conjugates linear polyubiquitin chains (By similarity). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (By similarity). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (By similarity). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (By similarity). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (By similarity). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (PubMed:32573437). S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. ATP + H2O = ADP + H(+) + phosphate Protein modification; protein ubiquitination. Monomer (PubMed:32573437). Interacts with UBE2L3/UBCH7; UBE2L3/UBCH7 is the most efficient ubiquitin-conjugating enzyme E2 for the ubiquitin ligase activity (PubMed:32573437). Interacts with UBE2N/UBC13; promoting 'Lys-63'-linked ubiquitination of target proteins (By similarity). Composed of an N-terminal stalk, a dynein-like core comprised of two catalytically active and four inactive ATPase domains, and a C-terminal E3 module (PubMed:32573437). The ATPase regions do not generate movement but rather act like an intricate molecular 'switch' (PubMed:32573437). The RING-type zinc finger domain is required for the ubiquitin-protein ligase activity. The RZ-type (RNF213-ZNFX1) zinc-finger is required for the ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS). No visible phenotype (PubMed:23410753, PubMed:24440776). Males and female are fertile and produce normal-sized litters (PubMed:23410753, PubMed:24440776). Mice do not spontaneously develop Moyamoya disease, a chronic occlusive cerebrovascular disease (PubMed:24440776). Mice are however more susceptible to Rift Valley fever virus infection (PubMed:33420513). Mice show elevated expression of MMP9 (PubMed:25383461). Belongs to the AAA ATPase family. The stoichiometry is unclear: was initially thought to form homohexamers (By similarity). However, the electron microscopy structure showed that it is monomeric and is composed of six ATPase modules within a single polypeptide chain (PubMed:32573437). Truncated N-terminus.