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