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Overview

Uniprot IDO95571
Protein NamePersulfide dioxygenase ETHE1, mitochondrial
Gene NameETHE1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
172 DFQQGCAKTLYHSVH
66 PRDAQLIKELGLRLL

Function

Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (PubMed:12398897)

Protein Sequence

10 MAEAVLRVAR 20 RQLSQRGGSG 30 APILLRQMFE 40 PVSCTFTYLL 50 GDRESREAVL 60 IDPVLETAPR 70 DAQLIKELGL 80 RLLYAVNTHC 90 HADHITGSGL 100 LRSLLPGCQS 110 VISRLSGAQA 120 DLHIEDGDSI 130 RFGRFALETR 140 ASPGHTPGCV 150 TFVLNDHSMA 160 FTGDALLIRG 170 CGRTDFQQGC 180 AKTLYHSVHE 190 KIFTLPGDCL 200 IYPAHDYHGF 210 TVSTVEEERT 220 LNPRLTLSCE 230 EFVKIMGNLN 240 LPKPQQIDFA 250 VPANMRCGVQ TPTA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0005506 iron ion binding
Molecular Function GO:0050313 sulfur dioxygenase activity
Biological Process GO:0006749 glutathione metabolic process
Biological Process GO:0070813 hydrogen sulfide metabolic process

Reference

[1] 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.