ETHE1_BOVIN
ID ETHE1_BOVIN Reviewed; 254 AA.
AC Q3T094;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Persulfide dioxygenase ETHE1, mitochondrial;
DE EC=1.13.11.18 {ECO:0000250|UniProtKB:O95571};
DE AltName: Full=Sulfur dioxygenase ETHE1;
DE Flags: Precursor;
GN Name=ETHE1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sulfur dioxygenase that plays an essential role in hydrogen
CC sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide
CC (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide
CC residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of
CC the persulfide, once it has been transferred to a thiophilic acceptor,
CC such as glutathione (R-SSH). Plays an important role in metabolic
CC homeostasis in mitochondria by metabolizing hydrogen sulfide and
CC preventing the accumulation of supraphysiological H(2)S levels that
CC have toxic effects, due to the inhibition of cytochrome c oxidase.
CC First described as a protein that can shuttle between the nucleus and
CC the cytoplasm and suppress p53-induced apoptosis by sequestering the
CC transcription factor RELA/NFKB3 in the cytoplasm and preventing its
CC accumulation in the nucleus. {ECO:0000250|UniProtKB:O95571}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + S-sulfanylglutathione = glutathione + 2 H(+) +
CC sulfite; Xref=Rhea:RHEA:12981, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17359, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58905; EC=1.13.11.18;
CC Evidence={ECO:0000250|UniProtKB:O95571};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O95571};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:O95571};
CC -!- ACTIVITY REGULATION: Glutathione increases enzyme activity.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Monomer. Interacts with TST. May interact with
CC RELA. {ECO:0000250|UniProtKB:O95571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95571}. Nucleus
CC {ECO:0000250|UniProtKB:O95571}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:O95571}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; BC102496; AAI02497.1; -; mRNA.
DR RefSeq; NP_001029516.1; NM_001034344.1.
DR AlphaFoldDB; Q3T094; -.
DR SMR; Q3T094; -.
DR STRING; 9913.ENSBTAP00000005747; -.
DR PaxDb; Q3T094; -.
DR PeptideAtlas; Q3T094; -.
DR PRIDE; Q3T094; -.
DR Ensembl; ENSBTAT00000005747; ENSBTAP00000005747; ENSBTAG00000004379.
DR GeneID; 509150; -.
DR KEGG; bta:509150; -.
DR CTD; 23474; -.
DR VEuPathDB; HostDB:ENSBTAG00000004379; -.
DR VGNC; VGNC:28623; ETHE1.
DR eggNOG; KOG0814; Eukaryota.
DR GeneTree; ENSGT00940000159046; -.
DR HOGENOM; CLU_030571_7_0_1; -.
DR InParanoid; Q3T094; -.
DR OMA; DYKGDTV; -.
DR OrthoDB; 1203911at2759; -.
DR TreeFam; TF312952; -.
DR Reactome; R-BTA-1614517; Sulfide oxidation to sulfate.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000004379; Expressed in digestive system secreted substance and 104 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0050313; F:sulfur dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0070813; P:hydrogen sulfide metabolic process; ISS:UniProtKB.
DR CDD; cd07724; POD-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Dioxygenase; Iron; Metal-binding; Mitochondrion;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..7
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:O95571"
FT CHAIN 8..254
FT /note="Persulfide dioxygenase ETHE1, mitochondrial"
FT /id="PRO_0000278566"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95571"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95571"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95571"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM0"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95571"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM0"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM0"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95571"
SQ SEQUENCE 254 AA; 27900 MW; 4699DEA856F5DB37 CRC64;
MAGSVLKIAG RRLSQHTGSG APVLLRQMFE PKSCTYTYLL GDRESREAVL IDPVLETAQR
DAQLVKELGL RLLYAVNTHC HADHITGSGL LRSLLPGCQS VISRLSGAQA DWHIEDGDSI
QFGRFALETR ASPGHTPGCV TFVLNDHSMA FTGDALLIRG CGRTDFQQGC AETLYHSVHE
KIFTLPGNCL IYPAHDYHGL TVSTVEEERT LNPRLTLSCE EFVKVMDKLN LPKPQQIDFA
VPANMRCGIQ TPPS
