RNH1
Domain
The LRR domain forms a horseshoe-shaped structure that interacts tightly with target RNases via a large protein interaction surface on its interior side.
Function
Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and angiogenin (ANG) (PubMed:12578357, PubMed:14515218, PubMed:3219362, PubMed:3243277, PubMed:3470787, PubMed:9050852). May play a role in redox homeostasis (PubMed:17292889). Required to inhibit the cytotoxic tRNA ribonuclease activity of ANG in the cytoplasm in absence of stress (PubMed:23843625, PubMed:32510170). Relocates to the nucleus in response to stress, relieving inhibition of ANG in the cytoplasm, and inhibiting the angiogenic activity of ANG in the nucleus (PubMed:23843625).
Involvement in disease
Encephalitis, acute, infection-induced, 12
IIAE12
An autosomal recessive disorder apparent in infancy or early childhood, and characterized by acute encephalopathy triggered by viral infections and febrile illness. Neurologic features of the acute episodes include seizures, hemiplegia, decreased consciousness, hypotonia, abnormal posturing, feeding problems, and respiratory insufficiency. Disease severity is variable, ranging from death to normal neurologic outcomes.
None
Disease susceptibility is associated with variants affecting the gene represented in this entry.
Post-translational modifications
The N-terminus is blocked.
At least 30 of the 32 cysteine residues are in the reduced form.
Cellular localization
- Cytoplasm
- Nucleus
- Localizes in the cytoplasm in absence of stress; translocates to the nucleus in response to stress.
Alternative names
PRI, RNH, RNH1, Ribonuclease inhibitor, Placental ribonuclease inhibitor, Ribonuclease/angiogenin inhibitor 1, Placental RNase inhibitor, RAI