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Glutathione S-transferase Mu 3 (EC 2.5.1.18) (GST class-mu 3) (GSTM3-3) (hGSTM3-3)

 GSTM3_HUMAN             Reviewed;         225 AA.
P21266; O60550; Q96HA3;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 190.
RecName: Full=Glutathione S-transferase Mu 3;
EC=2.5.1.18;
AltName: Full=GST class-mu 3;
AltName: Full=GSTM3-3;
Short=hGSTM3-3;
Name=GSTM3; Synonyms=GST5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Brain, and Testis;
PubMed=2345169;
Campbell E., Takahashi Y., Abramovitz M., Peretz M., Listowsky I.;
"A distinct human testis and brain mu-class glutathione S-transferase.
Molecular cloning and characterization of a form present even in
individuals lacking hepatic type mu isoenzymes.";
J. Biol. Chem. 265:9188-9193(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9882431; DOI=10.1006/abbi.1998.0964;
Patskovsky Y.V., Huang M.Q., Takayama T., Listowsky I., Pearson W.R.;
"Distinctive structure of the human GSTM3 gene-inverted orientation
relative to the mu class glutathione transferase gene cluster.";
Arch. Biochem. Biophys. 361:85-93(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-224.
TISSUE=Brain, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF N-TERMINUS.
TISSUE=Testis;
PubMed=8373352; DOI=10.1042/bj2940373;
Ross V.L., Board P.G.;
"Molecular cloning and heterologous expression of an alternatively
spliced human Mu class glutathione S-transferase transcript.";
Biochem. J. 294:373-380(1993).
[6]
PROTEIN SEQUENCE OF 190-209.
PubMed=8218382; DOI=10.1016/0167-4838(93)90047-U;
Hussey A.J., Hayes J.D.;
"Human Mu-class glutathione S-transferases present in liver, skeletal
muscle and testicular tissue.";
Biochim. Biophys. Acta 1203:131-141(1993).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-73, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), CATALYTIC ACTIVITY, FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF TYR-120 AND
ASN-213.
PubMed=10587441; DOI=10.1021/bi991714t;
Patskovsky Y.V., Patskovska L.N., Listowsky I.;
"An asparagine-phenylalanine substitution accounts for catalytic
differences between hGSTM3-3 and other human class mu glutathione S-
transferases.";
Biochemistry 38:16187-16194(1999).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles. May govern
uptake and detoxification of both endogenous compounds and
xenobiotics at the testis and brain blood barriers.
{ECO:0000269|PubMed:10587441}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:10587441}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.1 mM for 1-chloro-2,4-dinitrobenzene
{ECO:0000269|PubMed:10587441};
KM=0.084 mM for glutathione {ECO:0000269|PubMed:10587441};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10587441}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-350350, EBI-350350;
P46439:GSTM5; NbExp=4; IntAct=EBI-350350, EBI-4312072;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Testis and brain.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the GST superfamily. Mu family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J05459; AAA60964.1; -; mRNA.
EMBL; AF043105; AAC17866.1; -; Genomic_DNA.
EMBL; BT019945; AAV38748.1; -; mRNA.
EMBL; BC000088; AAH00088.1; -; mRNA.
EMBL; BC008790; AAH08790.1; -; mRNA.
CCDS; CCDS812.1; -.
PIR; A35295; A35295.
RefSeq; NP_000840.2; NM_000849.4.
UniGene; Hs.2006; -.
PDB; 3GTU; X-ray; 2.80 A; B/D=2-225.
PDBsum; 3GTU; -.
ProteinModelPortal; P21266; -.
SMR; P21266; -.
BioGrid; 109202; 24.
IntAct; P21266; 5.
STRING; 9606.ENSP00000256594; -.
ChEMBL; CHEMBL2242; -.
DrugBank; DB00143; Glutathione.
DrugBank; DB00163; Vitamin E.
iPTMnet; P21266; -.
PhosphoSitePlus; P21266; -.
BioMuta; GSTM3; -.
DMDM; 21264423; -.
OGP; P21266; -.
REPRODUCTION-2DPAGE; IPI00246975; -.
EPD; P21266; -.
PaxDb; P21266; -.
PeptideAtlas; P21266; -.
PRIDE; P21266; -.
DNASU; 2947; -.
Ensembl; ENST00000256594; ENSP00000256594; ENSG00000134202.
Ensembl; ENST00000361066; ENSP00000354357; ENSG00000134202.
GeneID; 2947; -.
KEGG; hsa:2947; -.
CTD; 2947; -.
DisGeNET; 2947; -.
EuPathDB; HostDB:ENSG00000134202.10; -.
GeneCards; GSTM3; -.
HGNC; HGNC:4635; GSTM3.
HPA; CAB017130; -.
HPA; CAB040583; -.
HPA; HPA035190; -.
HPA; HPA055972; -.
MIM; 138390; gene.
neXtProt; NX_P21266; -.
OpenTargets; ENSG00000134202; -.
PharmGKB; PA29024; -.
eggNOG; ENOG410IN5J; Eukaryota.
eggNOG; ENOG4110YU0; LUCA.
GeneTree; ENSGT00550000074559; -.
HOVERGEN; HBG106842; -.
InParanoid; P21266; -.
KO; K00799; -.
OMA; DIMENQV; -.
OrthoDB; EOG091G0K2E; -.
PhylomeDB; P21266; -.
TreeFam; TF353040; -.
BRENDA; 2.5.1.18; 2681.
Reactome; R-HSA-156590; Glutathione conjugation.
EvolutionaryTrace; P21266; -.
GeneWiki; GSTM3; -.
GenomeRNAi; 2947; -.
PRO; PR:P21266; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134202; -.
CleanEx; HS_GSTM3; -.
ExpressionAtlas; P21266; baseline and differential.
Genevisible; P21266; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035686; C:sperm fibrous sheath; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0043295; F:glutathione binding; IDA:BHF-UCL.
GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0070458; P:cellular detoxification of nitrogen compound; IDA:BHF-UCL.
GO; GO:0008065; P:establishment of blood-nerve barrier; TAS:ProtInc.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
GO; GO:0018916; P:nitrobenzene metabolic process; IDA:BHF-UCL.
GO; GO:0043627; P:response to estrogen; IEP:UniProtKB.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:BHF-UCL.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003081; GST_mu.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01267; GSTRNSFRASEM.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Polymorphism; Reference proteome; Transferase;
Ubl conjugation.
CHAIN 1 225 Glutathione S-transferase Mu 3.
/FTId=PRO_0000185822.
DOMAIN 5 92 GST N-terminal.
DOMAIN 94 212 GST C-terminal.
REGION 11 12 Glutathione binding.
{ECO:0000250|UniProtKB:P08515}.
REGION 50 54 Glutathione binding.
{ECO:0000250|UniProtKB:P08515}.
REGION 63 64 Glutathione binding.
{ECO:0000250|UniProtKB:P08515}.
REGION 76 77 Glutathione binding.
{ECO:0000250|UniProtKB:P08515}.
BINDING 120 120 Substrate. {ECO:0000250}.
CROSSLNK 54 54 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 224 224 V -> I (in dbSNP:rs7483).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_014498.
MUTAGEN 120 120 Y->A: No effect.
{ECO:0000269|PubMed:10587441}.
MUTAGEN 120 120 Y->F: Strongly increased catalytic
activity. {ECO:0000269|PubMed:10587441}.
MUTAGEN 213 213 N->F: Strongly increased catalytic
activity. {ECO:0000269|PubMed:10587441}.
MUTAGEN 213 213 N->G: No effect.
{ECO:0000269|PubMed:10587441}.
CONFLICT 147 147 G -> W (in Ref. 1; AAA60964).
{ECO:0000305}.
STRAND 7 15 {ECO:0000244|PDB:3GTU}.
HELIX 16 18 {ECO:0000244|PDB:3GTU}.
HELIX 19 27 {ECO:0000244|PDB:3GTU}.
STRAND 32 37 {ECO:0000244|PDB:3GTU}.
STRAND 42 44 {ECO:0000244|PDB:3GTU}.
HELIX 48 54 {ECO:0000244|PDB:3GTU}.
STRAND 64 69 {ECO:0000244|PDB:3GTU}.
STRAND 72 76 {ECO:0000244|PDB:3GTU}.
HELIX 77 87 {ECO:0000244|PDB:3GTU}.
HELIX 95 120 {ECO:0000244|PDB:3GTU}.
HELIX 124 146 {ECO:0000244|PDB:3GTU}.
STRAND 154 156 {ECO:0000244|PDB:3GTU}.
HELIX 159 174 {ECO:0000244|PDB:3GTU}.
HELIX 176 179 {ECO:0000244|PDB:3GTU}.
HELIX 183 193 {ECO:0000244|PDB:3GTU}.
HELIX 196 203 {ECO:0000244|PDB:3GTU}.
HELIX 205 208 {ECO:0000244|PDB:3GTU}.
STRAND 211 213 {ECO:0000244|PDB:3GTU}.
STRAND 217 220 {ECO:0000244|PDB:3GTU}.
SEQUENCE 225 AA; 26560 MW; 79093161ECEF5396 CRC64;
MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW LDVKFKLDLD
FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR VDIIENQVMD FRTQLIRLCY
SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD
EFPNLKAFMC RFEALEKIAA YLQSDQFCKM PINNKMAQWG NKPVC


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