ID M3WUX3_FELCA Unreviewed; 155 AA.
AC M3WUX3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:ENSFCAP00000018160.1,
GN ECO:0000313|VGNC:VGNC:68251};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000018160.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000018160.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018160.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000018160.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018160.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000018160.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000018160.1};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04001751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003988506.1; XM_003988457.4.
DR RefSeq; XP_006933601.1; XM_006933539.2.
DR RefSeq; XP_006933602.1; XM_006933540.2.
DR RefSeq; XP_006933603.1; XM_006933541.2.
DR RefSeq; XP_006933604.1; XM_006933542.3.
DR RefSeq; XP_006933605.1; XM_006933543.3.
DR AlphaFoldDB; M3WUX3; -.
DR PaxDb; 9685-ENSFCAP00000018160; -.
DR Ensembl; ENSFCAT00000028875.4; ENSFCAP00000018160.1; ENSFCAG00000030404.4.
DR GeneID; 101099565; -.
DR KEGG; fca:101099565; -.
DR CTD; 4257; -.
DR VGNC; VGNC:68251; MGST1.
DR eggNOG; ENOG502S0BD; Eukaryota.
DR GeneTree; ENSGT00390000011980; -.
DR HOGENOM; CLU_105467_1_0_1; -.
DR OMA; TFSMAYN; -.
DR OrthoDB; 5347993at2759; -.
DR Proteomes; UP000011712; Chromosome B4.
DR Bgee; ENSFCAG00000030404; Expressed in liver and 11 other cell types or tissues.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
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:UP000011712};
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..37
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; 17653 MW; 6DF0CE31CA19AC40 CRC64;
MVDLTELMEN EVFMAFASYT TIILSKMMFM STATAFFRLT RKVFANPEDC AGFGKGENAK
KYLRTDDKVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL STAILHFRLF VGARIYHTVA
YLTPLPQPNR ALAFFLGYGV TFSMAYRLLK SRLYL
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