LOCUS NP_034492 240 aa linear ROD 27-APR-2025
DEFINITION glutathione S-transferase omega-1 [Mus musculus].
ACCESSION NP_034492
VERSION NP_034492.1
DBSOURCE REFSEQ: accession NM_010362.3
KEYWORDS RefSeq; RefSeq Select.
SOURCE Mus musculus (house mouse)
ORGANISM Mus musculus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE 1 (residues 1 to 240)
AUTHORS Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
Jackson,S.P. and Balmus,G.
CONSRTM Sanger Mouse Genetics Project
TITLE Genetic determinants of micronucleus formation in vivo
JOURNAL Nature 627 (8002), 130-136 (2024)
PUBMED 38355793
REFERENCE 2 (residues 1 to 240)
AUTHORS Iram,S., Mashaal,A., Go,S. and Kim,J.
TITLE Inhibition of glutathione S-transferase omega 1-catalyzed protein
deglutathionylation suppresses adipocyte differentiation
JOURNAL BMB Rep 56 (8), 457-462 (2023)
PUBMED 37156632
REMARK GeneRIF: Inhibition of glutathione S-transferase omega 1-catalyzed
protein deglutathionylation suppresses adipocyte differentiation.
REFERENCE 3 (residues 1 to 240)
AUTHORS Piaggi,S., Marchi,E., Carnicelli,V., Zucchi,R., Griese,M.,
Hector,A., Sorio,C., Pompella,A. and Corti,A.
TITLE Airways glutathione S-transferase omega-1 and its A140D
polymorphism are associated with severity of inflammation and
respiratory dysfunction in cystic fibrosis
JOURNAL J Cyst Fibros 20 (6), 1053-1061 (2021)
PUBMED 33583732
REMARK GeneRIF: Airways glutathione S-transferase omega-1 and its A140D
polymorphism are associated with severity of inflammation and
respiratory dysfunction in cystic fibrosis.
REFERENCE 4 (residues 1 to 240)
AUTHORS Li,S., Wang,L., Xu,Z., Huang,Y., Xue,R., Yue,T., Xu,L., Gong,F.,
Bai,S., Wu,Q., Liu,J., Lin,B., Zhang,H., Xue,Y., Xu,P., Hou,J.,
Yang,X., Jin,T., Zhou,R., Lou,J., Xu,T. and Bai,L.
TITLE ASC deglutathionylation is a checkpoint for NLRP3 inflammasome
activation
JOURNAL J Exp Med 218 (9) (2021)
PUBMED 34342641
REMARK GeneRIF: ASC deglutathionylation is a checkpoint for NLRP3
inflammasome activation.
REFERENCE 5 (residues 1 to 240)
AUTHORS Tummala,P., Rooke,M., Dahlstrom,J.E., Takahashi,S., Casarotto,M.G.,
Fernando,N., Hughes,M.M., O'Neill,L.A.J. and Board,P.G.
TITLE Glutathione transferase Omega 1 confers protection against
azoxymethane-induced colorectal tumour formation
JOURNAL Carcinogenesis 42 (6), 853-863 (2021)
PUBMED 33564842
REMARK GeneRIF: Glutathione transferase Omega 1 confers protection against
azoxymethane-induced colorectal tumour formation.
REFERENCE 6 (residues 1 to 240)
AUTHORS Tanaka,K., Tamura,H., Tanaka,H., Katoh,M., Futamata,Y., Seki,N.,
Nishimune,Y. and Hara,T.
TITLE Spermatogonia-dependent expression of testicular genes in mice
JOURNAL Dev Biol 246 (2), 466-479 (2002)
PUBMED 12051830
REFERENCE 7 (residues 1 to 240)
AUTHORS Rouimi,P., Anglade,P., Benzekri,A., Costet,P., Debrauwer,L.,
Pineau,T. and Tulliez,J.
TITLE Purification and characterization of a glutathione S-transferase
Omega in pig: evidence for two distinct organ-specific transcripts
JOURNAL Biochem J 358 (Pt 1), 257-262 (2001)
PUBMED 11485575
REFERENCE 8 (residues 1 to 240)
AUTHORS Board,P.G., Coggan,M., Chelvanayagam,G., Easteal,S., Jermiin,L.S.,
Schulte,G.K., Danley,D.E., Hoth,L.R., Griffor,M.C., Kamath,A.V.,
Rosner,M.H., Chrunyk,B.A., Perregaux,D.E., Gabel,C.A.,
Geoghegan,K.F. and Pandit,J.
TITLE Identification, characterization, and crystal structure of the
Omega class glutathione transferases
JOURNAL J Biol Chem 275 (32), 24798-24806 (2000)
PUBMED 10783391
REFERENCE 9 (residues 1 to 240)
AUTHORS Retief,J.D., Lynch,K.R. and Pearson,W.R.
TITLE Panning for genes--A visual strategy for identifying novel gene
orthologs and paralogs
JOURNAL Genome Res 9 (4), 373-382 (1999)
PUBMED 10207159
REFERENCE 10 (residues 1 to 240)
AUTHORS Kodym,R., Calkins,P. and Story,M.
TITLE The cloning and characterization of a new stress response protein.
A mammalian member of a family of theta class glutathione
s-transferase-like proteins
JOURNAL J Biol Chem 274 (8), 5131-5137 (1999)
PUBMED 9988762
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AC126679.2, BE860946.1,
AK146834.1 and AI846704.1.
Summary: This gene encodes a member of the omega class of
glutathione S-transferase (GST) proteins. GSTs are involved in the
metabolism of xenobiotics and carcinogens. There is evidence that
the encoded protein is involved in the biotransformation of
arsenic. [provided by RefSeq, Dec 2015].
Sequence Note:.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: BC085165.1, U80819.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMN00849374, SAMN00849375
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
RefSeq Select criteria :: based on single protein-coding transcript
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..240
/organism="Mus musculus"
/strain="C57BL/6"
/db_xref="taxon:10090"
/chromosome="19"
/map="19 40.41 cM"
Protein 1..240
/product="glutathione S-transferase omega-1"
/EC_number="2.5.1.18"
/EC_number="1.8.5.1"
/EC_number="1.20.4.2"
/note="glutathione-S-transferase like; Glutathione
transferase omega 1 (GSTO 1-1) (p28); MMA(V) reductase;
monomethylarsonic acid reductase; S-(Phenacyl)glutathione
reductase; glutathione S-transferase omega 1-1;
glutathione-dependent dehydroascorbate reductase"
/calculated_mol_wt=27367
Site 2
/site_type="acetylation"
/note="N-acetylserine.
/evidence=ECO:0000250|UniProtKB:P78417; propagated from
UniProtKB/Swiss-Prot (O09131.2)"
Region 5..94
/region_name="GST_N_Omega"
/note="GST_N family, Class Omega subfamily; GSTs are
cytosolic dimeric proteins involved in cellular
detoxification by catalyzing the conjugation of
glutathione (GSH) with a wide range of endogenous and
xenobiotic alkylating agents, including carcinogens;
cd03055"
/db_xref="CDD:239353"
Site order(7..8,29..31,33,36..37,39..41,43..44,55,57)
/site_type="other"
/note="C-terminal domain interface [polypeptide binding]"
/db_xref="CDD:239353"
Site order(32,34,59,71..73,85..86)
/site_type="other"
/note="GSH binding site (G-site) [chemical binding]"
/db_xref="CDD:239353"
Site 32
/site_type="active"
/note="active site cysteine [active]"
/db_xref="CDD:239353"
Site 57
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P78417; propagated from
UniProtKB/Swiss-Prot (O09131.2)"
Site order(71,84..85,87..88,91)
/site_type="other"
/note="putative dimer interface [polypeptide binding]"
/db_xref="CDD:239353"
Region 108..228
/region_name="GST_C_Omega"
/note="C-terminal, alpha helical domain of Class Omega
Glutathione S-transferases; cd03184"
/db_xref="CDD:198293"
Site order(114..115,118..119,122,148)
/site_type="other"
/note="putative dimer interface [polypeptide binding]"
/db_xref="CDD:198293"
Site order(121,124..125,128..129,179,182,221)
/site_type="other"
/note="substrate binding pocket (H-site) [chemical
binding]"
/db_xref="CDD:198293"
Site 129
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:21183079; propagated from
UniProtKB/Swiss-Prot (O09131.2)"
Site 152
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P78417; propagated from
UniProtKB/Swiss-Prot (O09131.2)"
Site order(171,174..175,178,181..182,210,214,224,228)
/site_type="other"
/note="N-terminal domain interface [polypeptide binding]"
/db_xref="CDD:198293"
CDS 1..240
/gene="Gsto1"
/gene_synonym="Gsto-1; Gstx; p28; Spg-r"
/coded_by="NM_010362.3:117..839"
/db_xref="CCDS:CCDS29893.1"
/db_xref="GeneID:14873"
/db_xref="MGI:MGI:1342273"
ORIGIN
1 msgessrslg kgsappgpvp egqirvysmr fcpfaqrtlm vlkakgirhe vininlknkp
61 ewffeknplg lvpvlensqg hlvtesvitc eyldeaypek klfpddpykk arqkmtlesf
121 skvppliasf vrskrkedsp nlrealenef kkleegmdny ksflggdsps mvdyltwpwf
181 qrlealelke clahtpklkl wmaamqqdpv asshkidakt yreylnlylq dspeacdygl
//
