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MGST3_BOVIN
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   03-AUG-2022, entry version 107.
DE   RecName: Full=Microsomal glutathione S-transferase 3 {ECO:0000250|UniProtKB:O14880};
DE            Short=Microsomal GST-3;
DE   AltName: Full=Glutathione peroxidase MGST3 {ECO:0000250|UniProtKB:O14880};
DE            EC=1.11.1.-;
DE   AltName: Full=Microsomal glutathione S-transferase III {ECO:0000250|UniProtKB:O14880};
DE            Short=Microsomal GST-III {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: Also functions as a glutathione peroxidase. {ECO:0000250}.
CC   -!- FUNCTION: Catalyzes oxydation of hydroxy-fatty acids. May participate
CC       to the lipid metabolism. {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   -!- ACTIVITY REGULATION: Inhibited by MK-886 and leukotriene C4.
CC       {ECO:0000250|UniProtKB:D4ADS4}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O14880}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:O14880}. Microsome membrane
CC       {ECO:0000250|UniProtKB:O14880}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:O14880}. Microsome membrane
CC       {ECO:0000250|UniProtKB:O14880}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:O14880}. Membrane
CC       {ECO:0000250|UniProtKB:O14880}.
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; Q3T100; -.
DR   PRIDE; Q3T100; -.
DR   Ensembl; ENSBTAT00000072321; ENSBTAP00000071203; ENSBTAG00000010265.
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; YTGEPKN; -.
DR   OrthoDB; 1609516at2759; -.
DR   TreeFam; TF105328; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000010265; Expressed in abomasum and 102 other tissues.
DR   ExpressionAtlas; Q3T100; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.550; -; 1.
DR   InterPro; IPR023352; MAPEG-like_dom_sf.
DR   InterPro; IPR001129; Membr-assoc_MAPEG.
DR   Pfam; PF01124; MAPEG; 1.
DR   SUPFAM; SSF161084; SSF161084; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid metabolism; Lipoprotein; Membrane; Microsome;
KW   Oxidoreductase; Palmitate; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..152
FT                   /note="Microsomal glutathione S-transferase 3"
FT                   /id="PRO_0000246088"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
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
 
 
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