ID   MGST3_BOVIN             Reviewed;         152 AA.
AC   Q3T100;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102190; AAI02191.1; -; mRNA.
DR   RefSeq; NP_001030218.1; NM_001035046.2.
DR   RefSeq; XP_010801016.1; XM_010802714.1.
DR   AlphaFoldDB; Q3T100; -.
DR   SMR; Q3T100; -.
DR   STRING; 9913.ENSBTAP00000013559; -.
DR   PaxDb; 9913-ENSBTAP00000013559; -.
DR   Ensembl; ENSBTAT00000072321.1; ENSBTAP00000071203.1; ENSBTAG00000010265.5.
DR   GeneID; 507346; -.
DR   KEGG; bta:507346; -.
DR   CTD; 4259; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010265; -.
DR   VGNC; VGNC:31453; MGST3.
DR   eggNOG; ENOG502S4E5; Eukaryota.
DR   GeneTree; ENSGT00390000008608; -.
DR   HOGENOM; CLU_110291_1_0_1; -.
DR   InParanoid; Q3T100; -.
DR   OMA; ACQHLGW; -.
DR   OrthoDB; 5487436at2759; -.
DR   TreeFam; TF105328; -.
DR   Reactome; R-BTA-156590; Glutathione conjugation.
DR   Reactome; R-BTA-5423646; Aflatoxin activation and detoxification.
DR   UniPathway; UPA00383; -.
DR   UniPathway; UPA00879; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000010265; Expressed in abomasum and 102 other cell types or tissues.
DR   ExpressionAtlas; Q3T100; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004464; F:leukotriene-C4 synthase activity; IEA:Ensembl.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; IEA:Ensembl.
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.
PE   2: Evidence at transcript level;
KW   Lipid metabolism; Lipoprotein; Lyase; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Oxidoreductase; Palmitate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..152
FT                   /note="Glutathione S-transferase 3, mitochondrial"
FT                   /id="PRO_0000246088"
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..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   LIPID           151
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O14880"
SQ   SEQUENCE   152 AA;  16884 MW;  440C63094FD1999E CRC64;
     MAVLSKEYGF VILTGAASFL MVTHLAINVS KARKKYKVEY PTMYSTDPEN GHIFNCIQRA
     HQNTLEVYPP FLFFLAVGGV YHPRIVSGLG LAWIVGRVLY AYGYYTGEPR KRQRGALSFI
     ALIGLMGTTV CSAFQHLGWV RTGLNSGCKS CH
//