Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P19639 (GSTM4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase Mu 3

EC=2.5.1.18
Alternative name(s):
GST class-mu 3
Glutathione S-transferase GT9.3
Gene names
Name:Gstm3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence caution

The sequence AAA37748.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 218217Glutathione S-transferase Mu 3
PRO_0000185828

Regions

Domain2 – 8887GST N-terminal
Domain90 – 208119GST C-terminal
Region7 – 82Glutathione binding By similarity
Region46 – 505Glutathione binding By similarity
Region59 – 602Glutathione binding By similarity
Region72 – 732Glutathione binding By similarity

Sequences

Sequence LengthMass (Da)Tools
P19639 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F4989897BE817868

FASTA21825,702
        10         20         30         40         50         60 
MPMTLGYWNT RGLTHSIRLL LEYTDSSYEE KRYVMGDAPN FDRSQWLSEK FNLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGSHKV TQSNAILRYL GRKHNLCGET EEERIRVDTL ENQVMDTRIQ LMIVCCSPDF 

       130        140        150        160        170        180 
EKQKPEFLKA IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN 

       190        200        210 
LRDFLARFEG LKKISAYMKS SRFLPRPVFT KIAQWGTD 

« Hide

References

« Hide 'large scale' references
[1]"Tissue-specific induction of murine glutathione transferase mRNAs by butylated hydroxyanisole."
Pearson W.R., Reinhart J., Sisk S.C., Anderson K.S., Adler P.N.
J. Biol. Chem. 263:13324-13332(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Strain: FVB/N.
Tissue: Liver.
[3]"Increased synthesis of glutathione S-transferases in response to anticarcinogenic antioxidants. Cloning and measurement of messenger RNA."
Pearson W.R., Windle J.J., Morrow J.F., Benson A.M., Talalay P.
J. Biol. Chem. 258:2052-2062(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-41.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC044927 mRNA. Translation: AAH44927.1.
J03953 mRNA. Translation: AAA37748.1. Different initiation.
CCDSCCDS17744.1.
PIRB28946.
E37520.
RefSeqNP_034489.1. NM_010359.2.
UniGeneMm.440885.

3D structure databases

ProteinModelPortalP19639.
SMRP19639. Positions 2-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1869606.
STRING10090.ENSMUSP00000102289.

Proteomic databases

MaxQBP19639.
PaxDbP19639.
PRIDEP19639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004136; ENSMUSP00000004136; ENSMUSG00000004038.
ENSMUST00000106678; ENSMUSP00000102289; ENSMUSG00000004038.
GeneID14864.
KEGGmmu:14864.
UCSCuc008qxv.2. mouse.

Organism-specific databases

CTD2947.
MGIMGI:106026. Gstm3.

Phylogenomic databases

eggNOGNOG300089.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115735.
HOVERGENHBG106842.
InParanoidP19639.
KOK00799.
OMALENQVME.
OrthoDBEOG7KH9M3.
PhylomeDBP19639.
TreeFamTF353040.

Gene expression databases

BgeeP19639.
CleanExMM_GSTM3.
GenevestigatorP19639.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287113.
PROP19639.
SOURCESearch...

Entry information

Entry nameGSTM4_MOUSE
AccessionPrimary (citable) accession number: P19639
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot