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Protein

Glutathione S-transferase Mu 1

Gene

Gstm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: RGD
  2. nickel cation binding Source: RGD
  3. protein homodimerization activity Source: RGD
  4. steroid binding Source: RGD

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB
  2. response to amino acid Source: RGD
  3. response to antibiotic Source: RGD
  4. response to axon injury Source: RGD
  5. response to drug Source: RGD
  6. response to ethanol Source: RGD
  7. response to lead ion Source: RGD
  8. response to lithium ion Source: RGD
  9. response to metal ion Source: RGD
  10. sensory perception of smell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Olfaction, Sensory transduction

Enzyme and pathway databases

BRENDAi2.5.1.18. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 1 (EC:2.5.1.18)
Alternative name(s):
GST 3-3
GSTM1-1
Glutathione S-transferase Yb-1
Short name:
GST Yb1
Gene namesi
Name:Gstm1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2755. Gstm1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular region Source: RGD
  3. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71Y → F or L: Reduces catalytic activity about 100-fold. 1 Publication
Mutagenesisi87 – 871C → S: No change in activity. 1 Publication
Mutagenesisi116 – 1161Y → F: Reduces enzyme activity about 100-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 218217Glutathione S-transferase Mu 1PRO_0000185831Add
BLAST

Proteomic databases

PaxDbiP04905.
PRIDEiP04905.

PTM databases

PhosphoSiteiP04905.

Expressioni

Gene expression databases

GenevestigatoriP04905.

Interactioni

Subunit structurei

Homodimer or heterodimer.3 Publications

Protein-protein interaction databases

MINTiMINT-4564586.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Turni12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi28 – 336Combined sources
Turni38 – 414Combined sources
Helixi44 – 474Combined sources
Turni48 – 514Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 725Combined sources
Helixi73 – 8311Combined sources
Helixi91 – 11525Combined sources
Helixi120 – 14223Combined sources
Beta strandi146 – 1527Combined sources
Helixi155 – 17016Combined sources
Turni172 – 1754Combined sources
Helixi179 – 18911Combined sources
Helixi192 – 1987Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi213 – 2164Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GSBX-ray2.50A/B/C/D2-218[»]
1GSCX-ray2.50A/B/C/D2-218[»]
1MTCX-ray2.20A/B2-218[»]
2GSTX-ray1.80A/B2-218[»]
3FYGX-ray2.20A/B2-218[»]
3GSTX-ray1.90A/B2-218[»]
4GSTX-ray1.90A/B2-218[»]
5FWGX-ray2.00A/B2-218[»]
5GSTX-ray2.00A/B2-218[»]
6GSTX-ray2.20A/B2-218[»]
6GSUX-ray1.85A/B2-218[»]
6GSVX-ray1.75A/B2-218[»]
6GSWX-ray1.85A/B2-218[»]
6GSXX-ray1.91A/B2-218[»]
6GSYX-ray2.20A/B2-218[»]
ProteinModelPortaliP04905.
SMRiP04905. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04905.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8887GST N-terminalAdd
BLAST
Domaini90 – 208119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione binding
Regioni43 – 508Glutathione binding
Regioni59 – 602Glutathione binding
Regioni72 – 732Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiKOG1695.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP04905.
KOiK00799.
PhylomeDBiP04905.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMILGYWNV RGLTHPIRLL LEYTDSSYEE KRYAMGDAPD YDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGSRKI TQSNAIMRYL ARKHHLCGET EEERIRADIV
110 120 130 140 150
ENQVMDNRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG
160 170 180 190 200
DKVTYVDFLA YDILDQYHIF EPKCLDAFPN LKDFLARFEG LKKISAYMKS
210
SRYLSTPIFS KLAQWSNK
Length:218
Mass (Da):25,914
Last modified:January 23, 2007 - v2
Checksum:i1A8E80D09A5CACA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 2002KS → NC in AAA41287 (PubMed:3840477).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04229 mRNA. Translation: CAA27811.1.
M11719 mRNA. Translation: AAA41287.1.
J02810 mRNA. Translation: AAA41293.1.
BC063172 mRNA. Translation: AAH63172.1.
PIRiA29794.
RefSeqiNP_058710.1. NM_017014.1.
UniGeneiRn.202944.

Genome annotation databases

GeneIDi24423.
KEGGirno:24423.
UCSCiRGD:2755. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04229 mRNA. Translation: CAA27811.1.
M11719 mRNA. Translation: AAA41287.1.
J02810 mRNA. Translation: AAA41293.1.
BC063172 mRNA. Translation: AAH63172.1.
PIRiA29794.
RefSeqiNP_058710.1. NM_017014.1.
UniGeneiRn.202944.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GSBX-ray2.50A/B/C/D2-218[»]
1GSCX-ray2.50A/B/C/D2-218[»]
1MTCX-ray2.20A/B2-218[»]
2GSTX-ray1.80A/B2-218[»]
3FYGX-ray2.20A/B2-218[»]
3GSTX-ray1.90A/B2-218[»]
4GSTX-ray1.90A/B2-218[»]
5FWGX-ray2.00A/B2-218[»]
5GSTX-ray2.00A/B2-218[»]
6GSTX-ray2.20A/B2-218[»]
6GSUX-ray1.85A/B2-218[»]
6GSVX-ray1.75A/B2-218[»]
6GSWX-ray1.85A/B2-218[»]
6GSXX-ray1.91A/B2-218[»]
6GSYX-ray2.20A/B2-218[»]
ProteinModelPortaliP04905.
SMRiP04905. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4564586.

Chemistry

ChEMBLiCHEMBL2209.

PTM databases

PhosphoSiteiP04905.

Proteomic databases

PaxDbiP04905.
PRIDEiP04905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24423.
KEGGirno:24423.
UCSCiRGD:2755. rat.

Organism-specific databases

CTDi2944.
RGDi2755. Gstm1.

Phylogenomic databases

eggNOGiKOG1695.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP04905.
KOiK00799.
PhylomeDBiP04905.

Enzyme and pathway databases

BRENDAi2.5.1.18. 5301.

Miscellaneous databases

EvolutionaryTraceiP04905.
NextBioi603287.
PROiP04905.

Gene expression databases

GenevestigatoriP04905.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of a cDNA for a rat liver glutathione S-transferase Yb subunit."
    Lai H.-C.J., Grove G., Tu C.-P.D.
    Nucleic Acids Res. 14:6101-6114(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Rat liver glutathione S-transferases. Nucleotide sequence analysis of a Yb1 cDNA clone and prediction of the complete amino acid sequence of the Yb1 subunit."
    Ding G.J.-F., Lu A.Y.H., Pickett C.B.
    J. Biol. Chem. 260:13268-13271(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 cDNA clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital."
    Ding G.J.-F., Ding V.D.-H., Rodkey J.A., Bennett C.D., Lu A.Y.H., Pickett C.B.
    J. Biol. Chem. 261:7952-7957(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-24, SUBUNIT.
  4. "Identification of glutathione S-transferase Yb1 mRNA as the androgen-repressed mRNA by cDNA cloning and sequence analysis."
    Chang C., Saltzman A.G., Sorensen N.S., Hiipakka R.A., Liao S.
    J. Biol. Chem. 262:11901-11903(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  6. "Identification of Tyr115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3."
    Katusz R.M., Bono B., Colman R.F.
    Arch. Biochem. Biophys. 298:667-677(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20; 83-96 AND 109-122.
  7. "Expression of Yb1 glutathione S-transferase using a baculovirus expression system."
    Hsieh J.C., Liu L.F., Chen W.L., Tam M.F.
    Biochem. Biophys. Res. Commun. 162:1147-1154(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21 AND 212-218.
  8. "Identification of rat liver glutathione S-transferase Yb subunits by partial N-terminal sequencing after electroblotting of proteins onto a polyvinylidene difluoride membrane from an analytical isoelectric focusing gel."
    Chang L.H., Hsieh J.C., Chen W.L., Tam M.F.
    Electrophoresis 11:589-593(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26.
  9. "Glutathione S-transferases in rat olfactory epithelium: purification, molecular properties and odorant biotransformation."
    Ben-Arie N., Khen M., Lancet D.
    Biochem. J. 292:379-384(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-24.
    Strain: Wistar.
    Tissue: Olfactory epithelium.
  10. "Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
    Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
    Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20.
  11. Lubec G., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 19-32; 33-50; 53-68; 70-78; 97-108; 137-144; 174-187 AND 203-218, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Hippocampus.
  12. "Cysteine-86 is not needed for the enzymic activity of glutathione S-transferase 3-3."
    Hsieh J.-C., Huang S.-C., Chen W.-L., Lai Y.-C., Tam M.F.
    Biochem. J. 278:293-297(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-87.
  13. "The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution."
    Ji X., Zhang P., Armstrong R.N., Gilliland G.L.
    Biochemistry 31:10169-10184(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
  14. "New crystal forms of a mu-class glutathione S-transferase from rat liver."
    Fu J.-H., Rose J., Tam M.F., Wang B.-C.
    Acta Crystallogr. D 50:219-224(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  15. "Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene."
    Ji X., Johnson W.W., Sesay M.A., Dickert L., Prasad S.M., Ammon H.L., Armstrong R.N., Gilliland G.L.
    Biochemistry 33:1043-1052(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-116.
  16. "First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase."
    Xiao G., Liu S., Ji X., Johnson W.W., Chen J., Parsons J.F., Stevens W.J., Gilliland G.L., Armstrong R.N.
    Biochemistry 35:4753-4765(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT PHE-7 IN COMPLEXES WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-7.

Entry informationi

Entry nameiGSTM1_RAT
AccessioniPrimary (citable) accession number: P04905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Yb subclass selectively binds steroid hormones.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.