Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9DCM0 (ETHE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Persulfide dioxygenase ETHE1, mitochondrial

EC=1.13.11.18
Alternative name(s):
Ethylmalonic encephalopathy protein 1 homolog
Hepatoma subtracted clone one protein
Sulfur dioxygenase ETHE1
Gene names
Name:Ethe1
Synonyms:Hsco
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 (H2S) 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 H2S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. Ref.4

Catalytic activity

Sulfur + O2 + H2O = sulfite + 2 H+.

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Subunit structure

Monomer. Interacts with TST. May interact with RELA By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Mitochondrion matrix By similarity.

Disruption phenotype

Mice are born at slightly less than the expected Mendelian rate. Pups display growth arrest at about 15 days after birth and die five to six weeks after birth. Mice exhibit elevated levels of hydrogen sulfide (H2S) in liver, muscle and brain, together with increased urinary levels of ethylmalonic acid and thiosulfate. Their mitochondria show decreased cytochrome c oxidase activity, probably due to the toxic effects of supraphysiological levels of hydrogen sulfide. Ref.4

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 77Mitochondrion By similarity
Chain8 – 254247Persulfide dioxygenase ETHE1, mitochondrial
PRO_0000012290

Sites

Metal binding791Iron; catalytic By similarity
Metal binding1351Iron; catalytic By similarity
Metal binding1541Iron; catalytic By similarity

Amino acid modifications

Modified residue321N6-acetyllysine; alternate Ref.6
Modified residue321N6-succinyllysine; alternate Ref.5
Modified residue661N6-acetyllysine Ref.6
Modified residue1721N6-acetyllysine; alternate Ref.6
Modified residue1721N6-succinyllysine; alternate Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9DCM0 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: 3F28C0ED465A3062

FASTA25427,739
        10         20         30         40         50         60 
MASAVVRVAG RRLSQQSASG APVLLRQMFE PKSCTYTYLL GDRESREAVL IDPVLETAHR 

        70         80         90        100        110        120 
DAQLIKELGL KLLYAVNTHC HADHITGTGV LRSLLPGCQS VISRLSGAQA DLHIGEGDSI 

       130        140        150        160        170        180 
RFGRFALETR ASPGHTPGCV TFVLNDQSMA FTGDALLIRG CGRTDFQQGC AKTLYHSVHE 

       190        200        210        220        230        240 
KIFTLPGNCL IYPAHDYHGL TVSTVEEERT LNPRLTLSCE EFIKVMDNLN LPKPQQIDIA 

       250 
VPANMRCGVQ TPPS 

« Hide

References

« Hide 'large scale' references
[1]"Expression of HSCO in hepatomas."
Fujita J., Higashitsuji H., Higashitsuji H.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon, Kidney and Mammary tumor.
[4]"Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy."
Tiranti V., Viscomi C., Hildebrandt T., Di Meo I., Mineri R., Tiveron C., Levitt M.D., Prelle A., Fagiolari G., Rimoldi M., Zeviani M.
Nat. Med. 15:200-205(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-66 AND LYS-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB049623 mRNA. Translation: BAB16409.1.
AK002666 mRNA. Translation: BAB22271.2.
BC010592 mRNA. Translation: AAH10592.1.
BC083162 mRNA. Translation: AAH83162.1.
BC094044 mRNA. Translation: AAH94044.1.
CCDSCCDS20957.1.
RefSeqNP_075643.1. NM_023154.3.
XP_006540342.1. XM_006540279.1.
UniGeneMm.29553.

3D structure databases

ProteinModelPortalQ9DCM0.
SMRQ9DCM0. Positions 23-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DCM0. 2 interactions.
MINTMINT-1850653.
STRING10090.ENSMUSP00000076433.

PTM databases

PhosphoSiteQ9DCM0.

2D gel databases

REPRODUCTION-2DPAGEQ9DCM0.

Proteomic databases

MaxQBQ9DCM0.
PaxDbQ9DCM0.
PRIDEQ9DCM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077191; ENSMUSP00000076433; ENSMUSG00000064254.
GeneID66071.
KEGGmmu:66071.
UCSCuc009fqb.2. mouse.

Organism-specific databases

CTD23474.
MGIMGI:1913321. Ethe1.

Phylogenomic databases

eggNOGCOG0491.
GeneTreeENSGT00530000063033.
HOGENOMHOG000058040.
HOVERGENHBG053310.
InParanoidQ9DCM0.
KOK17725.
OMANPKMMDV.
OrthoDBEOG7MH107.
PhylomeDBQ9DCM0.
TreeFamTF312952.

Gene expression databases

BgeeQ9DCM0.
CleanExMM_ETHE1.
GenevestigatorQ9DCM0.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
[Graphical view]
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
ProtoNetSearch...

Other

ChiTaRSETHE1. mouse.
NextBio320540.
PROQ9DCM0.
SOURCESearch...

Entry information

Entry nameETHE1_MOUSE
AccessionPrimary (citable) accession number: Q9DCM0
Secondary accession number(s): Q9ESL5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot