ID   MGST3_MOUSE             Reviewed;         153 AA.
AC   Q9CPU4; Q3UXC5; Q9D834;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Glutathione S-transferase 3, mitochondrial {ECO:0000250|UniProtKB:O14880};
DE            EC=2.5.1.- {ECO:0000250|UniProtKB:O14880};
DE   AltName: Full=Glutathione peroxidase MGST3 {ECO:0000250|UniProtKB:O14880};
DE            EC=1.11.1.- {ECO:0000250|UniProtKB:O14880};
DE   AltName: Full=LTC4 synthase MGST3 {ECO:0000250|UniProtKB:O14880};
DE            EC=4.4.1.20 {ECO:0000250|UniProtKB:O14880};
GN   Name=Mgst3 {ECO:0000312|MGI:MGI:1913697};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, Embryo, and Small intestine;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   PROTEIN SEQUENCE OF 85-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION 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 expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Displays both glutathione S-transferase and glutathione
CC       peroxidase activities toward oxyeicosanoids. Catalyzes the Michael
CC       addition reaction of reduced glutathione (GSH) to electrophilic
CC       eicosanoids to form GSH adducts, as part of detoxification or metabolic
CC       shunt processes. Mediates GSH conjugation to leukotriene A4 to form the
CC       sulfidopeptide leukotriene C4. Metabolizes cyclopentenone prostanoids,
CC       specifically mediates GSH addition at C9 within the cyclopentenone ring
CC       of 15-deoxy-Delta12,14-prostaglandin J2 (15dPGJ2) to form 15dPGJ2-
CC       glutathione. L-cysteine can not substitute for GSH. Catalyzes the
CC       reduction of eicosanoid peroxides to yield eicosanoid hydroxides.
CC       {ECO:0000250|UniProtKB:O14880}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=leukotriene C4 = glutathione + leukotriene A4;
CC         Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:57973; EC=4.4.1.20;
CC         Evidence={ECO:0000250|UniProtKB:O14880};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17619;
CC         Evidence={ECO:0000250|UniProtKB:O14880};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-deoxy-Delta(12,14)-prostaglandin J2 + glutathione = 15-
CC         deoxy-Delta(12,14)-prostaglandin J2-S-(R)-glutathione;
CC         Xref=Rhea:RHEA:75963, ChEBI:CHEBI:57925, ChEBI:CHEBI:85236,
CC         ChEBI:CHEBI:194498; Evidence={ECO:0000250|UniProtKB:O14880};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75964;
CC         Evidence={ECO:0000250|UniProtKB:O14880};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2
CC         glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate +
CC         glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:O14880};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621;
CC         Evidence={ECO:0000250|UniProtKB:O14880};
CC   -!- PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis.
CC       {ECO:0000250|UniProtKB:O14880}.
CC   -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC       {ECO:0000250|UniProtKB:O14880}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:O14880}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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DR   EMBL; AK003246; BAB22665.1; -; mRNA.
DR   EMBL; AK003309; BAB22706.1; -; mRNA.
DR   EMBL; AK003476; BAB22808.1; -; mRNA.
DR   EMBL; AK003492; BAB22819.1; -; mRNA.
DR   EMBL; AK008533; BAB25726.1; -; mRNA.
DR   EMBL; AK135742; BAE22638.1; -; mRNA.
DR   EMBL; BC029669; AAH29669.1; -; mRNA.
DR   CCDS; CCDS15457.1; -.
DR   RefSeq; NP_079845.1; NM_025569.1.
DR   AlphaFoldDB; Q9CPU4; -.
DR   SMR; Q9CPU4; -.
DR   BioGRID; 211481; 5.
DR   IntAct; Q9CPU4; 4.
DR   STRING; 10090.ENSMUSP00000028005; -.
DR   GlyGen; Q9CPU4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CPU4; -.
DR   PhosphoSitePlus; Q9CPU4; -.
DR   SwissPalm; Q9CPU4; -.
DR   EPD; Q9CPU4; -.
DR   jPOST; Q9CPU4; -.
DR   MaxQB; Q9CPU4; -.
DR   PaxDb; 10090-ENSMUSP00000028005; -.
DR   PeptideAtlas; Q9CPU4; -.
DR   ProteomicsDB; 290226; -.
DR   Pumba; Q9CPU4; -.
DR   Antibodypedia; 34331; 150 antibodies from 21 providers.
DR   DNASU; 66447; -.
DR   Ensembl; ENSMUST00000028005.3; ENSMUSP00000028005.3; ENSMUSG00000026688.6.
DR   GeneID; 66447; -.
DR   KEGG; mmu:66447; -.
DR   UCSC; uc007dky.1; mouse.
DR   AGR; MGI:1913697; -.
DR   CTD; 4259; -.
DR   MGI; MGI:1913697; Mgst3.
DR   VEuPathDB; HostDB:ENSMUSG00000026688; -.
DR   eggNOG; ENOG502S4E5; Eukaryota.
DR   GeneTree; ENSGT00390000008608; -.
DR   HOGENOM; CLU_110291_1_0_1; -.
DR   InParanoid; Q9CPU4; -.
DR   OMA; ACQHLGW; -.
DR   OrthoDB; 5487436at2759; -.
DR   PhylomeDB; Q9CPU4; -.
DR   TreeFam; TF105328; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR   UniPathway; UPA00383; -.
DR   UniPathway; UPA00879; -.
DR   BioGRID-ORCS; 66447; 0 hits in 76 CRISPR screens.
DR   ChiTaRS; Mgst3; mouse.
DR   PRO; PR:Q9CPU4; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9CPU4; Protein.
DR   Bgee; ENSMUSG00000026688; Expressed in fetal liver hematopoietic progenitor cell and 272 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0004464; F:leukotriene-C4 synthase activity; ISO:MGI.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; ISO:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
DR   GO; GO:0006692; P:prostanoid metabolic process; ISS:UniProtKB.
DR   Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR   InterPro; IPR023352; MAPEG-like_dom_sf.
DR   InterPro; IPR001129; Membr-assoc_MAPEG.
DR   PANTHER; PTHR10250; MICROSOMAL GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR10250:SF27; MICROSOMAL GLUTATHIONE S-TRANSFERASE 3; 1.
DR   Pfam; PF01124; MAPEG; 1.
DR   SUPFAM; SSF161084; MAPEG domain-like; 1.
DR   Genevisible; Q9CPU4; MM.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lipid metabolism; Lipoprotein; Lyase; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Oxidoreductase; Palmitate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..153
FT                   /note="Glutathione S-transferase 3, mitochondrial"
FT                   /id="PRO_0000217742"
FT   TOPO_DOM        1..8
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..119
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..153
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   LIPID           151
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O14880"
FT   CONFLICT        142
FT                   /note="P -> R (in Ref. 1; BAB25726)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   153 AA;  16958 MW;  F54175ACB9C4C845 CRC64;
     MAVLSKEYGF VLLTGAASFV MVLHLAINVG KARKKYKVEY PVMYSTDPEN GHMFNCIQRA
     HQNTLEVYPP FLFFLTVGGV YHPRIASGLG LAWIIGRVLY AYGYYTGDPS KRYRGAVGSL
     ALFALMGTTV CSAFQHLGWI RPGLGYGSRS CHH
//