CPLM-021000

Genbank Nucleotide ID

Persulfide dioxygenase ETHE1, mitochondrial

Protein Synonyms/Alias

Ethylmalonic encephalopathy protein 1 homolog; Hepatoma subtracted clone one protein; Sulfur dioxygenase ETHE1

Mus musculus (Mouse)

Position	Peptide	Type	References
32	LRQMFEPKSCTYTYL	acetylation	[1, 2, 3, 4, 5, 6]
32	LRQMFEPKSCTYTYL	succinylation	[5]
66	HRDAQLIKELGLKLL	acetylation	[1, 2, 3, 4, 6, 7]
66	HRDAQLIKELGLKLL	ubiquitination	[8]
71	LIKELGLKLLYAVNT	acetylation	[6]
172	DFQQGCAKTLYHSVH	acetylation	[1, 3, 4, 5, 6, 7, 9]
172	DFQQGCAKTLYHSVH	succinylation	[5]
181	LYHSVHEKIFTLPGN	acetylation	[6]

[1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
[5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[8] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[9] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]

Functional Description

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 (By similarity). 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.

METAL 79 79 Iron; catalytic (By similarity).
METAL 135 135 Iron; catalytic (By similarity).
METAL 154 154 Iron; catalytic (By similarity).
MOD_RES 14 14 Phosphoserine.
MOD_RES 66 66 N6-acetyllysine (By similarity).

Acetylation; Complete proteome; Cytoplasm; Dioxygenase; Metal-binding; Mitochondrion; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:MGI.
GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO:0050313; F:sulfur dioxygenase activity; ISS:UniProtKB.
GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
GO:0070813; P:hydrogen sulfide metabolic process; ISS:UniProtKB.

IPR001279; Beta-lactamas-like.

PF00753; Lactamase_B

SM00849; Lactamase_B