Ribonuclease K6
experimentalAlso known as: RNASE6, Q93091
**Mechanism of Action** Ribonuclease K6 (RNASE6, Q93091) is a member of the ribonuclease A superfamily, exhibiting endoribonuclease activity with a marked substrate preference for pyrimidine bases, specifically uridine and cytosine. It catalyzes the cleavage of RNA at the 3' side of these residues via a transphosphorylation mechanism, generating 2',3'-cyclic phosphate intermediates. This enzymatic activity is dependent on conserved histidine and lysine residues in the active site, and its function is modulated by interactions with cellular RNA substrates and potential inhibitors. **Key Research Findings** Current experimental studies (7 PubMed references) indicate that RNASE6 is expressed in various tissues, with notable activity in immune cells. Its ribonuclease activity suggests roles in RNA metabolism, host defense, and regulation of gene expression. Preliminary findings point to involvement in antimicrobial responses, as RNASE6 can degrade bacterial and viral RNA, potentially contributing to innate immunity. However, its precise physiological substrates and regulatory mechanisms remain under investigation, with no definitive in vivo functional validation to date. **Clinical Relevance** As an experimental protein, RNASE6 has no established clinical applications. Its potential relevance lies in antimicrobial therapy and inflammatory disease modulation, given its RNA-cleaving properties. Further research is needed to elucidate its role in human pathophysiology and to assess therapeutic targeting. For research purposes only — not medical advice.
Key data
MVLCFPLLLLLLVLWGPVCPLHAWPKRLTKAHWFEIQHIQPSPLQCNRAMSGINNYTQHCKHQNTFLHDSFQNVAAVCDLLSIVCKNRRHNCHQSSKPVNMTDCRLTSGKYPQCRYSAAAQYKFFIVACDPPQKSDPPYKLVPVHLDSILMechanism of action
Ribonuclease which shows a preference for the pyrimidines uridine and cytosine (PubMed:27013146, PubMed:8836175). Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli (PubMed:25075772, PubMed:27089320). Causes loss of bacterial membrane integrity, and also promotes agglutination of Gram-negative bacteria (PubMed:27089320). Probably contributes to urinary tract sterility (PubMed:25075772). Bactericidal activity is independent of RNase activity (PubMed:27089320)
Research & studies
Proteins associated with CAC implicated fibrosis, inflammation, oxidative lipid metabolism, extracellular matrix remodeling, calcification, and metabolism.; Genetic analyses linked several targets (e.g., PCSK9, APOC1) to atherosclerosis or myocardial infarction in large populations.; Transcriptome-wide association study of CAC identified genes involved in vascular homeostasis, inflammation, and metabolism, including novel candidates.; Overlap across proteomics and transcriptomics highlighted genes such as S100A9, HES1, SPARCL1, NOTCH3, TNFSF12, and S100A12.
EDN and ECP are closely related eosinophil ribonucleases with structural and catalytic residues of the RNase A superfamily.; The physiologic role of ribonuclease activity in EDN and ECP function is not yet understood.; The chapter also reviews the recently discovered ribonuclease k6 (RNase 6).
Human RNase k6 gene localized to within ~120 kb on chromosome 14q.; All 10 primate orthologs encode complete ORFs with ≥86% amino acid identity to human RNase k6.; RNase k6 has a low nonsynonymous substitution rate (0.40 × 10⁻⁹ ns/ns/yr), unlike EDN (1.9 × 10⁻⁹) and ECP (2.0 × 10⁻⁹).; New World monkey RNase k6 genes show unusually low synonymous substitution rates (Ks).
RNase k6 is a single-copy gene on chromosome 14 with orthologs in primates and non-primate mammals.; Transcripts were detected in all human tissues, with highest abundance in lung, and in monocytes and neutrophils but not eosinophils.; RNase k6 shares 47% amino acid identity with eosinophil-derived neurotoxin (EDN) and has about 40-fold lower ribonuclease activity.; The discovery expands the ribonuclease gene family and implies additional family members may exist.
Frequently asked questions
What is Ribonuclease K6?
**Mechanism of Action** Ribonuclease K6 (RNASE6, Q93091) is a member of the ribonuclease A superfamily, exhibiting endoribonuclease activity with a marked substrate preference for pyrimidine bases, specifically uridine and cytosine. It catalyzes the cleavage of RNA at the 3' side of these residues via a transphosphoryl
How does Ribonuclease K6 work?
Ribonuclease which shows a preference for the pyrimidines uridine and cytosine (PubMed:27013146, PubMed:8836175). Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli (PubMed:25075772, PubMed:27089320). Causes loss of bacterial membrane integrity, and
What is the research status of Ribonuclease K6?
Ribonuclease K6 is currently classified as experimental, with 7 research references on record. This is for research purposes only and is not medical advice.
What is the molecular weight of Ribonuclease K6?
Ribonuclease K6 has a molecular weight of approximately 17196 g/mol.
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