GenomeNet

Database: RefSeq
Entry: NP_034492
LinkDB: NP_034492
Original site: NP_034492 
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
//
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