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 03-AUG-2022, entry version 172.
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}.
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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 AlphaFoldDB; O09131; -.
DR SMR; O09131; -.
DR BioGRID; 200104; 3.
DR IntAct; O09131; 1.
DR STRING; 10090.ENSMUSP00000026050; -.
DR ChEMBL; CHEMBL4523122; -.
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 ProteomicsDB; 271106; -.
DR Antibodypedia; 31606; 308 antibodies from 34 providers.
DR DNASU; 14873; -.
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 VEuPathDB; HostDB:ENSMUSG00000025068; -.
DR eggNOG; KOG0406; Eukaryota.
DR GeneTree; ENSGT00940000155351; -.
DR HOGENOM; CLU_011226_9_2_1; -.
DR InParanoid; O09131; -.
DR OMA; ADHYSHR; -.
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; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gsto1; mouse.
DR PRO; PR:O09131; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O09131; protein.
DR Bgee; ENSMUSG00000025068; Expressed in conjunctival fornix and 268 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: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:0006749; P:glutathione metabolic process; IBA:GO_Central.
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: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; 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 ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 59
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 72
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 85..86
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
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:0007744|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
