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Overview

Uniprot IDQ9Y3B8
Protein NameOligoribonuclease, mitochondrial
Gene NameREXO2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
173 IIDVSTVKELCRRWY
225 KIDEKKRKIIENGEN

Function

3'-to-5'exoribonuclease that preferentially degrades DNA and RNA oligonucleotides composed of only two nucleotides (PubMed:23741365, PubMed:30926754, PubMed:31588022, PubMed:32365187). Binds and degrades longer oligonucleotides with a lower affinity (PubMed:30926754, PubMed:31588022, PubMed:32365187). Plays dual roles in mitochondria, scavenging nanoRNAs (small RNA oligonucleotides of <5 nucleotides) that are produced by the degradosome and clearing short RNAs that are generated by RNA processing (PubMed:30926754, PubMed:31588022, PubMed:32365187). Essential for correct initiation of mitochondrial transcription, degrading mitochondrial RNA dinucleotides to prevent RNA-primed transcription at non-canonical sites in the mitochondrial genome (PubMed:31588022). Essential for embryonic development (By similarity)

Protein Sequence

10 MLGGSLGSRL 20 LRGVGGSHGR 30 FGARGVREGG 40 AAMAAGESMA 50 QRMVWVDLEM 60 TGLDIEKDQI 70 IEMACLITDS 80 DLNILAEGPN 90 LIIKQPDELL 100 DSMSDWCKEH 110 HGKSGLTKAV 120 KESTITLQQA 130 EYEFLSFVRQ 140 QTPPGLCPLA 150 GNSVHEDKKF 160 LDKYMPQFMK 170 HLHYRIIDVS 180 TVKELCRRWY 190 PEEYEFAPKK 200 AASHRALDDI 210 SESIKELQFY 220 RNNIFKKKID 230 EKKRKIIENG ENEKTVS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005758 mitochondrial intermembrane space
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Molecular Function GO:0008408 3'-5' exonuclease activity
Molecular Function GO:0008296 3'-5'-DNA exonuclease activity
Molecular Function GO:0000175 3'-5'-RNA exonuclease activity
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0003676 nucleic acid binding
Biological Process GO:2000827 mitochondrial RNA surveillance
Biological Process GO:0006139 nucleobase-containing compound metabolic process
Biological Process GO:0009117 nucleotide metabolic process

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.