Family Search for PF20173 (ZnF_RZ-type)

PF20173 hits 19 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

ZNFX1_MOUSE / Q8R151 NFX1-type zinc finger-containing protein 1 from Mus musculus (Mouse) (see paper)
Aligns to 1826:1880 / 1909 (2.9%), covers 85.2% of PF20173, 79.2 bits

• function: RNA-binding protein that initiates the antiviral response and is required to restrict the replication of RNA viruses (PubMed:31685995). Acts as a double-stranded RNA (dsRNA) sensor that recognizes viral RNA and then interacts with MAVS to initiate the type I interferon response (PubMed:31685995). Also required for immunity against some bacteria, such as mycobacteria (By similarity).
  subunit: Interacts with MAVS.
  disruption phenotype: Mice are viable without obvious physiological or behavioral abnormalities (PubMed:31685995). They however display impaired innate immune responses against RNA virus infection by producing less type I interferons (IFNs) (PubMed:31685995).

R213A_DANRE / A0A0R4IBK5 E3 ubiquitin-protein ligase rnf213-alpha; E3 ubiquitin-lipopolysaccharide ligase rnf213-alpha; Mysterin-A; Mysterin-alpha; RING finger protein 213-A; RING finger protein 213-alpha; EC 2.3.2.27; EC 3.6.4.-; EC 2.3.2.- from Danio rerio (Zebrafish) (Brachydanio rerio) (see 4 papers)
Aligns to 4494:4547 / 5209 (1.0%), covers 96.3% of PF20173, 79.1 bits

• function: 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 (By similarity). 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 (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 (PubMed:30705059). 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 (By similarity). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins 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 (By similarity). Also involved in neuromuscular regulation (PubMed:26530008).
  catalytic activity: 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.
  catalytic activity: ATP + H2O = ADP + H(+) + phosphate (RHEA:13065)
  disruption phenotype: Morpholino knockdown leads to a slight reduction in body size, a small eye and a wavy trunk (PubMed:21799892). Fishes develope abnormal angiogenesis in intersegmental vessels and cranial secondary vessels (PubMed:21799892, PubMed:27125596). Abnormal sprouting vessels are observed in the trunk and head regions, while axial trunk vessels, the dorsal aorta and posterior cardinal vein proceed almost normally (PubMed:21799892). Morpholino knockdown in larvae leads to a reduction in fast myofibrils and immature projection of primary motoneurons, leading to severe motor deficits (PubMed:26530008). Decreased lipid droplet formation (PubMed:30705059).

ZNFX1_HUMAN / Q9P2E3 NFX1-type zinc finger-containing protein 1 from Homo sapiens (Human) (see 3 papers)
Aligns to 1834:1889 / 1918 (2.9%), covers 85.2% of PF20173, 76.2 bits

• function: RNA-binding protein that initiates the antiviral response and is required to restrict the replication of RNA viruses (PubMed:33872655). Acts as a double-stranded RNA (dsRNA) sensor that recognizes viral RNA and then interacts with MAVS to initiate the type I interferon response (By similarity). Also required for immunity against some bacteria, such as mycobacteria (PubMed:33876776).
  subunit: Interacts with MAVS.

RN213_HUMAN / Q63HN8 E3 ubiquitin-protein ligase RNF213; ALK lymphoma oligomerization partner on chromosome 17; E3 ubiquitin-lipopolysaccharide ligase RNF213; Mysterin; RING finger protein 213; EC 2.3.2.27; EC 3.6.4.-; EC 2.3.2.- from Homo sapiens (Human) (see 28 papers)
Aligns to 4490:4545 / 5207 (1.1%), covers 85.2% of PF20173, 70.1 bits

• function: 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:21799892, PubMed:26126547, PubMed:26278786, PubMed:26766444, PubMed:30705059, PubMed:32139119, PubMed:34012115). 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 (PubMed:34012115). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (PubMed:34012115). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (PubMed:30705059). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (PubMed:30846318). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (PubMed:32139119, PubMed:33842849). 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 (PubMed:26766444). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (PubMed:34012115).
  catalytic activity: 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.
  catalytic activity: ATP + H2O = ADP + H(+) + phosphate (RHEA:13065)
  subunit: Monomer (By similarity). Interacts with UBE2L3/UBCH7; UBE2L3/UBCH7 is the most efficient ubiquitin-conjugating enzyme E2 for the ubiquitin ligase activity (By similarity). Interacts with UBE2N/UBC13; promoting 'Lys-63'-linked ubiquitination of target proteins (PubMed:32139119, PubMed:33842849).
  subunit: (Microbial infection) Interacts with M.tuberculosis protein Rv3655c, which impairs caspase-8 activation and suppresses macrophage apoptosis by blocking the extrinsic pathway.

RN213_MOUSE / E9Q555 E3 ubiquitin-protein ligase RNF213; E3 ubiquitin-lipopolysaccharide ligase RNF213; Mysterin; RING finger protein 213; EC 2.3.2.27; EC 3.6.4.-; EC 2.3.2.- from Mus musculus (Mouse) (see 6 papers)
Aligns to 4436:4491 / 5148 (1.1%), covers 85.2% of PF20173, 66.8 bits

• function: 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).
  catalytic activity: 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.
  catalytic activity: ATP + H2O = ADP + H(+) + phosphate (RHEA:13065)
  subunit: 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).
  disruption phenotype: 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).

R213B_DANRE / A0A0R4I9Y1 E3 ubiquitin-protein ligase rnf213-beta; E3 ubiquitin-lipopolysaccharide ligase rnf213-beta; Mysterin-B; Mysterin-beta; RING finger protein 213-B; RING finger protein 213-beta; EC 2.3.2.27; EC 3.6.4.-; EC 2.3.2.- from Danio rerio (Zebrafish) (Brachydanio rerio) (see 2 papers)
Aligns to 4437:4491 / 5061 (1.1%), covers 85.2% of PF20173, 58.3 bits

• function: 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. 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. 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. Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger. Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins downstream of rspo3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression. Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (By similarity).
  catalytic activity: 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.
  catalytic activity: ATP + H2O = ADP + H(+) + phosphate (RHEA:13065)
  disruption phenotype: No visible phenotype (PubMed:21799892, PubMed:26530008). No vascular phenotype (PubMed:21799892, PubMed:26530008).

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