ID G3SQZ7_LOXAF Unreviewed; 155 AA.
AC G3SQZ7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Microsomal glutathione S-transferase 1 {ECO:0000256|ARBA:ARBA00039397};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN Name=MGST1 {ECO:0000313|Ensembl:ENSLAFP00000002255.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000002255.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000002255.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002255.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000002255.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002255.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|ARBA:ARBA00003701}.
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:0000256|ARBA:ARBA00035754};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000256|ARBA:ARBA00035754};
CC -!- SUBUNIT: Homotrimer; The trimer binds only one molecule of glutathione.
CC {ECO:0000256|ARBA:ARBA00038540}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
CC -!- SIMILARITY: Belongs to the MAPEG family.
CC {ECO:0000256|ARBA:ARBA00010459}.
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DR RefSeq; XP_003405723.1; XM_003405675.2.
DR RefSeq; XP_010593497.1; XM_010595195.1.
DR AlphaFoldDB; G3SQZ7; -.
DR STRING; 9785.ENSLAFP00000002255; -.
DR Ensembl; ENSLAFT00000002693.2; ENSLAFP00000002255.2; ENSLAFG00000002693.2.
DR GeneID; 100654951; -.
DR KEGG; lav:100654951; -.
DR CTD; 4257; -.
DR eggNOG; ENOG502S0BD; Eukaryota.
DR GeneTree; ENSGT00390000011980; -.
DR HOGENOM; CLU_105467_1_0_1; -.
DR InParanoid; G3SQZ7; -.
DR OMA; TFSMAYN; -.
DR OrthoDB; 5347993at2759; -.
DR TreeFam; TF105327; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:Ensembl.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071449; P:cellular response to lipid hydroperoxide; IEA:Ensembl.
DR GO; GO:0034635; P:glutathione transport; IEA:Ensembl.
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 InterPro; IPR040162; MGST1-like.
DR PANTHER; PTHR10689; MICROSOMAL GLUTATHIONE S-TRANSFERASE 1; 1.
DR PANTHER; PTHR10689:SF3; MICROSOMAL GLUTATHIONE S-TRANSFERASE 1; 1.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; MAPEG domain-like; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 155 AA; 17596 MW; 0DF1BF890D162366 CRC64;
MVDLTQVAEN EAFMAFASYA TIILSKMMFM STATAFQRLT KKVFVNPEDC AHFGKGENAK
KYLRTDDRVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDV STALLHFRLF VGSRIYHTIA
YLTPLPQPNR ALAFFVGYGV TFSMAYNLLK NRLYL
//