GenomeNet

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   13-FEB-2019, entry version 156.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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-
RT   like 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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
RT   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
CC       reduces 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
CC         disulfide + L-ascorbate; Xref=Rhea:RHEA:24424,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000250|UniProtKB:P78417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione
CC         disulfide + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17826,
CC         ChEBI:CHEBI:33409, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297;
CC         EC=1.20.4.2; 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   UniGene; Mm.378931; -.
DR   ProteinModelPortal; O09131; -.
DR   SMR; O09131; -.
DR   BioGrid; 200104; 1.
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   EPD; O09131; -.
DR   jPOST; O09131; -.
DR   MaxQB; O09131; -.
DR   PaxDb; O09131; -.
DR   PeptideAtlas; O09131; -.
DR   PRIDE; O09131; -.
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   eggNOG; ENOG410XSIX; LUCA.
DR   GeneTree; ENSGT00940000155351; -.
DR   HOGENOM; HOG000006560; -.
DR   HOVERGEN; HBG051853; -.
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   PRO; PR:O09131; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000025068; Expressed in 308 organ(s), highest expression level in camera-type eye.
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: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   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; Complete proteome; Cytoplasm; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P78417}.
FT   CHAIN         2    240       Glutathione S-transferase omega-1.
FT                                /FTId=PRO_0000185885.
FT   DOMAIN       22    101       GST N-terminal.
FT   DOMAIN      106    227       GST C-terminal.
FT   REGION       85     86       Glutathione binding.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   ACT_SITE     32     32       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   BINDING      59     59       Glutathione.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   BINDING      72     72       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   MOD_RES      57     57       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   MOD_RES     129    129       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     152    152       N6-acetyllysine.
FT                                {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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