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Protein

Glutathione S-transferase Mu 2

Gene

Gstm2

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.

Sites

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

GO - Molecular functioni

  1. glutathione transferase activity Source: RGD
  2. protein homodimerization activity Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. response to catechin Source: RGD
  3. response to genistein Source: RGD
  4. response to metal ion Source: RGD
  5. response to organic cyclic compound Source: RGD
  6. sensory perception of smell Source: UniProtKB-KW
  7. xenobiotic metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Olfaction, Sensory transduction

Enzyme and pathway databases

ReactomeiREACT_251519. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 2 (EC:2.5.1.18)
Alternative name(s):
GST 4-4
GSTM2-2
Glutathione S-transferase Yb-2
Short name:
GST Yb2
Gene namesi
Name:Gstm2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi2756. Gstm2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. plasma membrane Source: RGD
  3. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 218217Glutathione S-transferase Mu 2PRO_0000185832Add
BLAST

Proteomic databases

PaxDbiP08010.
PRIDEiP08010.

Expressioni

Gene expression databases

ExpressionAtlasiP08010. baseline and differential.
GenevestigatoriP08010.

Interactioni

Subunit structurei

Homodimer or heterodimer.1 Publication

Protein-protein interaction databases

IntActiP08010. 1 interaction.

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 – 403Combined sources
Helixi44 – 507Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 725Combined sources
Helixi73 – 8311Combined sources
Helixi91 – 11626Combined sources
Helixi120 – 14223Combined sources
Beta strandi150 – 1523Combined sources
Helixi155 – 17016Combined sources
Turni172 – 1776Combined sources
Helixi179 – 18911Combined sources
Helixi192 – 1987Combined sources
Beta strandi214 – 2163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4PX-ray1.70A2-218[»]
ProteinModelPortaliP08010.
SMRiP08010. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08010.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8887GST N-terminalAdd
BLAST
Domaini90 – 214125GST 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

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP08010.
KOiK00799.
OMAiRVCYNPD.
OrthoDBiEOG7KH9M3.
PhylomeDBiP08010.
TreeFamiTF353040.

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.

P08010-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPMTLGYWDI RGLAHAIRLF LEYTDTSYED KKYSMGDAPD YDRSQWLSEK
60 70 80 90 100
FKLGLDFPNL PYLIDGSHKI TQSNAILRYL GRKHNLCGET EEERIRVDVL
110 120 130 140 150
ENQAMDTRLQ LAMVCYSPDF ERKKPEYLEG LPEKMKLYSE FLGKQPWFAG
160 170 180 190 200
NKITYVDFLV YDVLDQHRIF EPKCLDAFPN LKDFVARFEG LKKISDYMKS
210
GRFLSKPIFA KMAFWNPK
Length:218
Mass (Da):25,703
Last modified:January 23, 2007 - v2
Checksum:iC23B30C171DB852F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471W → S AA sequence (PubMed:3699019)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02592 mRNA. Translation: AAA41285.1.
M13590 mRNA. Translation: AAA42351.1.
J03914 Genomic DNA. Translation: AAA41296.1.
PIRiA29231. XURTG4.
RefSeqiNP_803175.1. NM_177426.1.
UniGeneiRn.625.

Genome annotation databases

EnsembliENSRNOT00000025939; ENSRNOP00000025939; ENSRNOG00000019094.
GeneIDi24424.
KEGGirno:24424.
UCSCiRGD:2756. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02592 mRNA. Translation: AAA41285.1.
M13590 mRNA. Translation: AAA42351.1.
J03914 Genomic DNA. Translation: AAA41296.1.
PIRiA29231. XURTG4.
RefSeqiNP_803175.1. NM_177426.1.
UniGeneiRn.625.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4PX-ray1.70A2-218[»]
ProteinModelPortaliP08010.
SMRiP08010. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08010. 1 interaction.

Chemistry

ChEMBLiCHEMBL2504.

Proteomic databases

PaxDbiP08010.
PRIDEiP08010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025939; ENSRNOP00000025939; ENSRNOG00000019094.
GeneIDi24424.
KEGGirno:24424.
UCSCiRGD:2756. rat.

Organism-specific databases

CTDi2946.
RGDi2756. Gstm2.

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP08010.
KOiK00799.
OMAiRVCYNPD.
OrthoDBiEOG7KH9M3.
PhylomeDBiP08010.
TreeFamiTF353040.

Enzyme and pathway databases

ReactomeiREACT_251519. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTraceiP08010.
NextBioi603291.
PROiP08010.

Gene expression databases

ExpressionAtlasiP08010. baseline and differential.
GenevestigatoriP08010.

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

  1. "Gene expression of rat glutathione S-transferases. Evidence for gene conversion in the evolution of the Yb multigene family."
    Lai H.-C.J., Qian B., Grove G., Tu C.-P.D.
    J. Biol. Chem. 263:11389-11395(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cytosolic rat liver glutathione transferase 4-4. Primary structure of the protein reveals extensive differences between homologous glutathione transferases of classes alpha and mu."
    Alin P., Mannervik B., Joernvall H.
    Eur. J. Biochem. 156:343-350(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-218.
    Strain: Sprague-Dawley.
  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] OF 25-218.
  4. "Rat glutathione S-transferases supergene family. Characterization of an anionic Yb subunit cDNA clone."
    Lai H.-C.J., Tu C.-P.D.
    J. Biol. Chem. 261:13793-13799(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-218.
  5. "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 2-26.
  6. "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 2-28.
  7. "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 2-22.
    Strain: Wistar.
    Tissue: Olfactory epithelium.
  8. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-43; 137-144; 153-168 AND 174-182, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  9. "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 (1.7 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.

Entry informationi

Entry nameiGSTM2_RAT
AccessioniPrimary (citable) accession number: P08010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 143 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.