GSTM7_MOUSE
ID GSTM7_MOUSE Reviewed; 218 AA.
AC Q80W21; Q3TRV7; Q3V4E2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glutathione S-transferase Mu 7;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P28161};
DE AltName: Full=GST class-mu 7;
DE Short=GSTM-7;
GN Name=Gstm7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of mouse glutathione S-transferase, mu7 (gstm7) at 1.6 A
RT resolution.";
RL Submitted (JUN-2006) to the PDB data bank.
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 -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC -!- CAUTION: Gstm7 is the putative homolog of human GSTM2. {ECO:0000305}.
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DR EMBL; AK162441; BAE36919.1; -; mRNA.
DR EMBL; AK002213; BAE43145.1; -; mRNA.
DR EMBL; BC051924; AAH51924.1; -; mRNA.
DR CCDS; CCDS38595.1; -.
DR RefSeq; NP_080948.2; NM_026672.2.
DR PDB; 2DC5; X-ray; 1.60 A; A/B=1-218.
DR PDBsum; 2DC5; -.
DR AlphaFoldDB; Q80W21; -.
DR SMR; Q80W21; -.
DR BioGRID; 212800; 2.
DR IntAct; Q80W21; 1.
DR STRING; 10090.ENSMUSP00000004137; -.
DR iPTMnet; Q80W21; -.
DR PhosphoSitePlus; Q80W21; -.
DR SwissPalm; Q80W21; -.
DR jPOST; Q80W21; -.
DR MaxQB; Q80W21; -.
DR PaxDb; Q80W21; -.
DR PeptideAtlas; Q80W21; -.
DR PRIDE; Q80W21; -.
DR ProteomicsDB; 271105; -.
DR Antibodypedia; 20072; 247 antibodies from 31 providers.
DR Ensembl; ENSMUST00000004137; ENSMUSP00000004137; ENSMUSG00000004035.
DR GeneID; 68312; -.
DR KEGG; mmu:68312; -.
DR UCSC; uc008qxt.1; mouse.
DR CTD; 68312; -.
DR MGI; MGI:1915562; Gstm7.
DR VEuPathDB; HostDB:ENSMUSG00000004035; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000155416; -.
DR InParanoid; Q80W21; -.
DR OMA; NRLPEMM; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; Q80W21; -.
DR TreeFam; TF353040; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR BioGRID-ORCS; 68312; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Gstm7; mouse.
DR EvolutionaryTrace; Q80W21; -.
DR PRO; PR:Q80W21; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80W21; protein.
DR Bgee; ENSMUSG00000004035; Expressed in efferent duct and 187 other tissues.
DR ExpressionAtlas; Q80W21; baseline and differential.
DR Genevisible; Q80W21; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0043295; F:glutathione binding; ISO:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; ISO:MGI.
DR GO; GO:0071313; P:cellular response to caffeine; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISO:MGI.
DR GO; GO:0043651; P:linoleic acid metabolic process; ISO:MGI.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:0018916; P:nitrobenzene metabolic process; ISO:MGI.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:MGI.
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 3D-structure; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase Mu 7"
FT /id="PRO_0000333228"
FT DOMAIN 1..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"
FT CONFLICT 92
FT /note="E -> V (in Ref. 1; BAE43145)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="K -> R (in Ref. 1; BAE36919)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:2DC5"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2DC5"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:2DC5"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2DC5"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 91..115
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 120..142
FT /evidence="ECO:0007829|PDB:2DC5"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:2DC5"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:2DC5"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:2DC5"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2DC5"
SQ SEQUENCE 218 AA; 25710 MW; 0A971C2E117BCBC5 CRC64;
MPMTLGYWDI RGLAHAIRLF LEYTDSSYEE KRYTMGDAPD YDQSQWLNEK FKLGLDFPNL
PYLIDGSHKI TQSNAILRYL GRKHNLCGET EEERIRVDIL ENQLMDNRMV LARLCYNADF
EKLKPGYLEQ LPGMMRLYSE FLGKRPWFAG DKITFVDFIA YDVLERNQVF EAKCLDAFPN
LKDFIARFEG LKKISDYMKT SRFLPRPMFT KMATWGSN
