GSTM7_RAT
ID GSTM7_RAT Reviewed; 218 AA.
AC P08009;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Glutathione S-transferase Mu 7;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P28161};
DE AltName: Full=Chain 4;
DE AltName: Full=GST Yb3;
DE AltName: Full=GST class-mu 3;
DE AltName: Full=Glutathione S-transferase Yb-3 {ECO:0000303|PubMed:3584141};
GN Name=Gstm7 {ECO:0000312|RGD:621287}; Synonyms=Gstm3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3584141; DOI=10.1016/s0021-9258(18)47634-x;
RA Abramovitz M., Listowsky I.;
RT "Selective expression of a unique glutathione S-transferase Yb3 gene in rat
RT brain.";
RL J. Biol. Chem. 262:7770-7773(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Tail;
RX PubMed=7707876; DOI=10.1016/0169-328x(94)00182-e;
RA Abramovitz M., Testori A., Angelov I.V., Darmon A., Listowsky I.;
RT "Brain and testis selective expression of the glutathione S-transferase Yb3
RT subunit is governed by tandem direct repeat octamer motifs in the 5'-
RT flanking region of its gene.";
RL Brain Res. Mol. Brain Res. 28:37-46(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 19-50; 53-69; 137-144 AND 153-182, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000250|UniProtKB:P28161}.
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:0000250|UniProtKB:P28161};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28161}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28161}.
CC -!- MISCELLANEOUS: Yb subclass selectively binds steroid hormones.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC -!- CAUTION: Gstm7 is the putative ortholog of human GSTM2. {ECO:0000305}.
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DR EMBL; J02744; AAA41292.1; -; mRNA.
DR EMBL; L35330; AAB00123.1; -; Genomic_DNA.
DR EMBL; BC059130; AAH59130.1; -; mRNA.
DR PIR; A29036; A29036.
DR RefSeq; NP_112416.1; NM_031154.1.
DR AlphaFoldDB; P08009; -.
DR SMR; P08009; -.
DR STRING; 10116.ENSRNOP00000025689; -.
DR iPTMnet; P08009; -.
DR PhosphoSitePlus; P08009; -.
DR SwissPalm; P08009; -.
DR World-2DPAGE; 0004:P08009; -.
DR jPOST; P08009; -.
DR PaxDb; P08009; -.
DR PRIDE; P08009; -.
DR Ensembl; ENSRNOT00000025689; ENSRNOP00000025689; ENSRNOG00000018937.
DR GeneID; 81869; -.
DR KEGG; rno:81869; -.
DR UCSC; RGD:621287; rat.
DR CTD; 68312; -.
DR RGD; 621287; Gstm7.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000155416; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; P08009; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P08009; -.
DR TreeFam; TF353040; -.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR PRO; PR:P08009; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000018937; Expressed in liver and 20 other tissues.
DR ExpressionAtlas; P08009; baseline and differential.
DR Genevisible; P08009; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase Mu 7"
FT /id="PRO_0000185833"
FT DOMAIN 2..88
FT /note="GST N-terminal"
FT DOMAIN 90..208
FT /note="GST C-terminal"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 46..50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 25681 MW; BBC0B61288AB069A CRC64;
MPMTLGYWDI RGLAHAIRLL LEYTDSSYEE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL
PYLIDGSHKI TQSNAILRYL GRKHNLCGET EEERIRVDIL ENQLMDNRMV LARLCYNPDF
EKLKPGYLEQ LPGMMRLYSE FLGKRPWFAG DKITFVDFIA YDVLERNQVF EATCLDAFPN
LKDFIARFEG LKKISDYMKS SRFLPRPLFT KMAIWGSK
