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Database: UniProt/SWISS-PROT
Entry: GSTO1_MOUSE
LinkDB: GSTO1_MOUSE
Original site: GSTO1_MOUSE 
ID   GSTO1_MOUSE             Reviewed;         240 AA.
AC   O09131; Q3TH87;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   12-AUG-2020, entry version 164.
DE   RecName: Full=Glutathione S-transferase omega-1;
DE            Short=GSTO-1;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P78417};
DE   AltName: Full=Glutathione S-transferase omega 1-1;
DE            Short=GSTO 1-1;
DE   AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE            EC=1.8.5.1 {ECO:0000250|UniProtKB:P78417};
DE   AltName: Full=Monomethylarsonic acid reductase;
DE            Short=MMA(V) reductase;
DE            EC=1.20.4.2 {ECO:0000250|UniProtKB:P78417};
DE   AltName: Full=S-(Phenacyl)glutathione reductase;
DE            Short=SPG-R;
DE   AltName: Full=p28;
GN   Name=Gsto1; Synonyms=Gstx, Gtsttl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9988762; DOI=10.1074/jbc.274.8.5131;
RA   Kodym R., Calkins P., Story M.D.;
RT   "The cloning and characterization of a new stress response protein. A
RT   mammalian member of a family of theta class glutathione s-transferase-like
RT   proteins.";
RL   J. Biol. Chem. 274:5131-5137(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Exhibits glutathione-dependent thiol transferase and
CC       dehydroascorbate reductase activities. Has S-(phenacyl)glutathione
CC       reductase activity. Has also glutathione S-transferase activity.
CC       Participates in the biotransformation of inorganic arsenic and reduces
CC       monomethylarsonic acid (MMA) and dimethylarsonic acid.
CC       {ECO:0000250|UniProtKB:P78417}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000250|UniProtKB:P78417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC         L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000250|UniProtKB:P78417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC         + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC         Evidence={ECO:0000250|UniProtKB:P78417};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P78417}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P78417}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
DR   EMBL; U80819; AAB70110.1; -; mRNA.
DR   EMBL; AK027922; BAC25667.1; -; mRNA.
DR   EMBL; AK146834; BAE27469.1; -; mRNA.
DR   EMBL; AK168383; BAE40311.1; -; mRNA.
DR   EMBL; BC085165; AAH85165.1; -; mRNA.
DR   CCDS; CCDS29893.1; -.
DR   RefSeq; NP_034492.1; NM_010362.3.
DR   SMR; O09131; -.
DR   BioGRID; 200104; 3.
DR   IntAct; O09131; 3.
DR   MINT; O09131; -.
DR   STRING; 10090.ENSMUSP00000026050; -.
DR   iPTMnet; O09131; -.
DR   PhosphoSitePlus; O09131; -.
DR   SwissPalm; O09131; -.
DR   REPRODUCTION-2DPAGE; IPI00114285; -.
DR   CPTAC; non-CPTAC-3712; -.
DR   EPD; O09131; -.
DR   jPOST; O09131; -.
DR   MaxQB; O09131; -.
DR   PaxDb; O09131; -.
DR   PeptideAtlas; O09131; -.
DR   PRIDE; O09131; -.
DR   Antibodypedia; 31606; 272 antibodies.
DR   Ensembl; ENSMUST00000026050; ENSMUSP00000026050; ENSMUSG00000025068.
DR   GeneID; 14873; -.
DR   KEGG; mmu:14873; -.
DR   UCSC; uc008hvq.1; mouse.
DR   CTD; 9446; -.
DR   MGI; MGI:1342273; Gsto1.
DR   eggNOG; KOG0406; Eukaryota.
DR   GeneTree; ENSGT00940000155351; -.
DR   HOGENOM; CLU_011226_9_2_1; -.
DR   InParanoid; O09131; -.
DR   KO; K00799; -.
DR   OMA; ITLYTNH; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; O09131; -.
DR   TreeFam; TF105325; -.
DR   Reactome; R-MMU-156581; Methylation.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism.
DR   BioGRID-ORCS; 14873; 1 hit in 18 CRISPR screens.
DR   ChiTaRS; Gsto1; mouse.
DR   PRO; PR:O09131; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; O09131; protein.
DR   Bgee; ENSMUSG00000025068; Expressed in camera-type eye and 324 other tissues.
DR   ExpressionAtlas; O09131; baseline and differential.
DR   Genevisible; O09131; MM.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0005604; C:basement membrane; ISO:MGI.
DR   GO; GO:0044297; C:cell body; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; ISO:MGI.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
DR   GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR   GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:MGI.
DR   GO; GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR005442; GST_omega.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   CHAIN           2..240
FT                   /note="Glutathione S-transferase omega-1"
FT                   /id="PRO_0000185885"
FT   DOMAIN          22..101
FT                   /note="GST N-terminal"
FT   DOMAIN          106..227
FT                   /note="GST C-terminal"
FT   REGION          85..86
FT                   /note="Glutathione binding"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         59
FT                   /note="Glutathione"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         72
FT                   /note="Glutathione; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   MOD_RES         152
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
SQ   SEQUENCE   240 AA;  27498 MW;  17FEB52DB4BBE506 CRC64;
     MSGESSRSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE VININLKNKP
     EWFFEKNPLG LVPVLENSQG HLVTESVITC EYLDEAYPEK KLFPDDPYKK ARQKMTLESF
     SKVPPLIASF VRSKRKEDSP NLREALENEF KKLEEGMDNY KSFLGGDSPS MVDYLTWPWF
     QRLEALELKE CLAHTPKLKL WMAAMQQDPV ASSHKIDAKT YREYLNLYLQ DSPEACDYGL
//
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