Database: RefSeq
Entry: NP_034492
LinkDB: NP_034492
Original site: NP_034492 
LOCUS       NP_034492                240 aa            linear   ROD 16-DEC-2018
DEFINITION  glutathione S-transferase omega-1 [Mus musculus].
VERSION     NP_034492.1
DBSOURCE    REFSEQ: accession NM_010362.3
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   Fernando N, Wooff Y, Aggio-Bruce R, Chu-Tan JA, Jiao H, Dietrich C,
            Rutar M, Rooke M, Menon D, Eells JT, Valter K, Board PG, Provis J
            and Natoli R.
  TITLE     Photoreceptor Survival Is Regulated by GSTO1-1 in the Degenerating
  JOURNAL   Invest. Ophthalmol. Vis. Sci. 59 (11), 4362-4374 (2018)
   PUBMED   30193308
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Menon D, Coll R, O'Neill LA and Board PG.
  TITLE     GSTO1-1 modulates metabolism in macrophages activated through the
            LPS and TLR4 pathway
  JOURNAL   J. Cell. Sci. 128 (10), 1982-1990 (2015)
   PUBMED   25908843
  REMARK    GeneRIF: Data indicate that GSTO1-1 is required for LPS-mediated
            signalling in macrophages and that it acts early in the LPS-TLR4
            pro-inflammatory pathway.
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Menon D, Coll R, O'Neill LA and Board PG.
  TITLE     Glutathione transferase omega 1 is required for the
            lipopolysaccharide-stimulated induction of NADPH oxidase 1 and the
            production of reactive oxygen species in macrophages
  JOURNAL   Free Radic. Biol. Med. 73, 318-327 (2014)
   PUBMED   24873723
  REMARK    GeneRIF: shRNA knockdown of GSTO1-1 in macrophage-like J774.1A
            cells blocks the expression of NADPH oxidase 1 and the generation
            of reactive oxygen species after Bacterial lipopolysaccharide
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Pei L, Leblanc M, Barish G, Atkins A, Nofsinger R, Whyte J, Gold D,
            He M, Kawamura K, Li HR, Downes M, Yu RT, Powell HC, Lingrel JB and
            Evans RM.
  TITLE     Thyroid hormone receptor repression is linked to type I
            pneumocyte-associated respiratory distress syndrome
  JOURNAL   Nat. Med. 17 (11), 1466-1472 (2011)
   PUBMED   22001906
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Dittrich AM, Meyer HA, Krokowski M, Quarcoo D, Ahrens B, Kube SM,
            Witzenrath M, Esworthy RS, Chu FF and Hamelmann E.
  TITLE     Glutathione peroxidase-2 protects from allergen-induced airway
            inflammation in mice
  JOURNAL   Eur. Respir. J. 35 (5), 1148-1154 (2010)
   PUBMED   19897562
  REMARK    GeneRIF: Genes encoding the antioxidants GPX2 and GSTO 1-1 are
            common inflammatory genes expressed upon induction of allergic
            airway inflammation, and independently of allergic susceptibility.
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 PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte
            GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk
            BA, Perregaux DE, Gabel CA, Geoghegan KF 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 JD, Lynch KR and Pearson WR.
  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.
            Transcript exon combination :: U80819.1, AK146834.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Mus musculus"
     Protein         1..240
                     /product="glutathione S-transferase omega-1"
                     /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"
     Site            2
                     /experiment="experimental evidence, no additional details
                     /note="N-acetylserine. {ECO:0000250|UniProtKB:P78417};
                     propagated from UniProtKB/Swiss-Prot (O09131.2)"
     Region          5..94
                     /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;
     Site            order(7..8,29..31,33,36..37,39..41,43..44,55,57)
                     /note="C-terminal domain interface [polypeptide binding]"
     Region          26..224
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
     Site            order(32,34,59,71..73,85..86)
                     /note="GSH binding site (G-site) [chemical binding]"
     Site            32
                     /note="active site cysteine [active]"
     Site            57
                     /experiment="experimental evidence, no additional details
                     /note="N6-acetyllysine. {ECO:0000250|UniProtKB:P78417};
                     propagated from UniProtKB/Swiss-Prot (O09131.2)"
     Site            order(71,84..85,87..88,91)
                     /note="putative dimer interface [polypeptide binding]"
     Region          85..86
                     /region_name="Glutathione binding.
                     /experiment="experimental evidence, no additional details
                     /note="propagated from UniProtKB/Swiss-Prot (O09131.2)"
     Region          108..228
                     /note="C-terminal, alpha helical domain of Class Omega
                     Glutathione S-transferases; cd03184"
     Site            order(114..115,118..119,122,148)
                     /note="putative dimer interface [polypeptide binding]"
     Site            order(121,124..125,128..129,179,182,221)
                     /note="substrate binding pocket (H-site) [chemical
     Site            129
                     /experiment="experimental evidence, no additional details
                     /note="Phosphoserine. {ECO:0000244|PubMed:21183079};
                     propagated from UniProtKB/Swiss-Prot (O09131.2)"
     Site            152
                     /experiment="experimental evidence, no additional details
                     /note="N6-acetyllysine. {ECO:0000250|UniProtKB:P78417};
                     propagated from UniProtKB/Swiss-Prot (O09131.2)"
     Site            order(171,174..175,178,181..182,210,214,224,228)
                     /note="N-terminal domain interface [polypeptide binding]"
     CDS             1..240
                     /gene_synonym="AA407097; AI194287; AU018802; Gsto-1; Gstx;
                     p28; Spg-r"
        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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