Ribonuclease 4

Also known as: RNASE4, P34096

Ribonuclease 4 (RNASE4, P34096) is a member of the ribonuclease A superfamily that catalyzes the endonucleolytic cleavage of RNA, with a marked preference for uridine bases. This enzymatic activity distinguishes it from other RNase family members, which often favor cytidine or purine bases. The mechanism involves a conserved catalytic triad (His12, His119, Lys41) that facilitates transphosphorylation and hydrolysis of the phosphodiester bond, yielding 3'-phosphate-terminated products. RNASE4 is expressed in multiple tissues, including the liver, kidney, and pancreas, and is secreted into bodily fluids such as plasma and milk. Current experimental research on RNASE4 is limited, with 36 PubMed references indicating an early stage of investigation. Key findings suggest potential roles beyond RNA degradation, including antimicrobial activity, angiogenesis modulation, and neuroprotection. For instance, RNASE4 has been shown to inhibit bacterial growth and promote endothelial cell proliferation in vitro. Its expression is upregulated under hypoxic conditions, hinting at a possible function in stress responses. However, mechanistic details and in vivo validation remain sparse. Clinically, RNASE4 has not yet been translated into therapeutic applications. Its experimental status reflects a need for further studies to clarify its physiological significance and disease associations, such as potential links to cancer or inflammatory conditions. Given the limited evidence, no clinical recommendations can be made at this time. For research purposes only — not medical advice.

Key data

Mechanism of action

Cleaves preferentially after uridine bases (PubMed:3467790). Has antimicrobial activity against uropathogenic E.coli (UPEC) (PubMed:33818125). Probably contributes to urinary tract sterility (PubMed:33818125)

Research & studies

Frequently asked questions

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