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
//
