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Database: UniProt
Entry: G3SQZ7_LOXAF
LinkDB: G3SQZ7_LOXAF
Original site: G3SQZ7_LOXAF 
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
//
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