ID   MGST2_BOVIN             Reviewed;         146 AA.
AC   Q2KJG4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=Microsomal glutathione S-transferase 2;
DE            Short=Microsomal GST-2;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:Q99735};
DE   AltName: Full=Glutathione peroxidase MGST2;
DE            EC=1.11.1.- {ECO:0000250|UniProtKB:Q99735};
DE   AltName: Full=Leukotriene C4 synthase MGST2;
DE            EC=4.4.1.20 {ECO:0000250|UniProtKB:Q99735};
DE   AltName: Full=Microsomal glutathione S-transferase II;
DE            Short=Microsomal GST-II;
GN   Name=MGST2;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes several different glutathione-dependent reactions.
CC       Catalyzes the glutathione-dependent reduction of lipid hydroperoxides,
CC       such as 5-HPETE. Has glutathione transferase activity, toward
CC       xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB).
CC       Catalyzes also the conjugation of leukotriene A4 with reduced
CC       glutathione to form leukotriene C4 (LTC4). Involved in oxidative DNA
CC       damage induced by ER stress and anticancer agents by activating LTC4
CC       biosynthetic machinery in nonimmune cells.
CC       {ECO:0000250|UniProtKB:Q99735}.
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:Q99735};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC         S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18;
CC         Evidence={ECO:0000250|UniProtKB:Q99735};
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:Q99735};
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:Q99735};
CC   -!- ACTIVITY REGULATION: Each monomer binds on GSH molecule but only one
CC       subunit is catalytically active. {ECO:0000250|UniProtKB:Q99735}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q99735}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q99735}; Multi-pass membrane protein
CC       {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q99735};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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DR   EMBL; BT025439; ABF57395.1; -; mRNA.
DR   EMBL; BC105356; AAI05357.1; -; mRNA.
DR   RefSeq; NP_001069850.1; NM_001076382.1.
DR   AlphaFoldDB; Q2KJG4; -.
DR   SMR; Q2KJG4; -.
DR   STRING; 9913.ENSBTAP00000029028; -.
DR   PaxDb; 9913-ENSBTAP00000029028; -.
DR   Ensembl; ENSBTAT00000029028.4; ENSBTAP00000029028.3; ENSBTAG00000021779.4.
DR   GeneID; 615552; -.
DR   KEGG; bta:615552; -.
DR   CTD; 4258; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021779; -.
DR   VGNC; VGNC:31452; MGST2.
DR   eggNOG; ENOG502S082; Eukaryota.
DR   GeneTree; ENSGT00940000160288; -.
DR   HOGENOM; CLU_110291_3_0_1; -.
DR   InParanoid; Q2KJG4; -.
DR   OMA; HKYFWGY; -.
DR   OrthoDB; 5396066at2759; -.
DR   TreeFam; TF105328; -.
DR   Reactome; R-BTA-156590; Glutathione conjugation.
DR   Reactome; R-BTA-5423646; Aflatoxin activation and detoxification.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000021779; Expressed in metanephros cortex and 104 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0004464; F:leukotriene-C4 synthase activity; ISS:UniProtKB.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
DR   Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR   InterPro; IPR001446; 5_LipOase_AP.
DR   InterPro; IPR023352; MAPEG-like_dom_sf.
DR   InterPro; IPR001129; Membr-assoc_MAPEG.
DR   PANTHER; PTHR10250; MICROSOMAL GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR10250:SF13; MICROSOMAL GLUTATHIONE S-TRANSFERASE 2; 1.
DR   Pfam; PF01124; MAPEG; 1.
DR   PRINTS; PR00488; 5LPOXGNASEAP.
DR   SUPFAM; SSF161084; MAPEG domain-like; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Leukotriene biosynthesis; Lipid metabolism; Lyase;
KW   Membrane; Microsome; Oxidoreductase; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..146
FT                   /note="Microsomal glutathione S-transferase 2"
FT                   /id="PRO_0000246087"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   146 AA;  16483 MW;  24BCF4E5E9CE0393 CRC64;
     MAGNSILLAA LSVLSACQQS YFAMQVGKAR SKYKVTPPSV SGSPDFERIF RAQQNCVEFY
     PIFIITLWMA GWYFNQVFAT CLGLVYIYSR HQYFWGYAEA AKKRVTGFRL SLGVLALLTV
     LGAVGILNSF LDEYLDIDIA KKLRHF
//