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Q9Z1B2 (GSTM5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 5

EC=2.5.1.18
Alternative name(s):
GST class-mu 5
Gene names
Name:Gstm5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
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 By similarity.

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Expressed in testis and brain. Very low expression in liver, kidney, heart and lung. Ref.1

Post-translational modification

The N-terminus is blocked Probable.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.14 mM for glutathione Ref.1

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from direct assay Ref.1. Source: MGI

protein homodimerization activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Glutathione S-transferase Mu 5
PRO_0000271421

Regions

Domain5 – 9288GST N-terminal
Domain94 – 212119GST C-terminal
Region11 – 122Glutathione binding By similarity
Region50 – 545Glutathione binding By similarity
Region63 – 642Glutathione binding By similarity
Region76 – 772Glutathione binding By similarity

Sites

Binding site1201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z1B2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 45A2DC2DDCE5ACA4

FASTA22526,629
        10         20         30         40         50         60 
MSCSKSMVLG YWDIRGLAHA IRMLLEFTDT SYEEKQYTCG EAPDYDRSQW LDVKFKLDLD 

        70         80         90        100        110        120 
FPNLPYLMDG KNKITQSNAI LRYIARKHNM CGDTEEEKIR VDIMENQIMD FRMQLVRLCY 

       130        140        150        160        170        180 
NSNHESLKPQ YLEQLPAQLK QFSLFLGKFT WFAGEKLTFV DFLTYDVLDQ NRMFEPKCLD 

       190        200        210        220 
EFPNLKAFMC RFEALEKIAA FLQSDRCFKM PINNKMAKWG NKSIC 

« Hide

References

[1]"Rationale for reclassification of a distinctive subdivision of mammalian class Mu glutathione S-transferases that are primarily expressed in testis."
Rowe J.D., Patskovsky Y.V., Patskovska L.N., Novikova E., Listowsky I.
J. Biol. Chem. 273:9593-9601(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-27; 36-50; 57-71; 74-87; 89-120; 157-177; 179-186; 198-215 AND 219-224, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, KINETIC PARAMETERS.
Strain: Sprague-Dawley.
Tissue: Testis.
[2]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 157-172, INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U86635 mRNA. Translation: AAD00603.1.
RefSeqNP_742035.1. NM_172038.1.
XP_003749426.1. XM_003749378.2.
UniGeneRn.9158.

3D structure databases

ProteinModelPortalQ9Z1B2.
SMRQ9Z1B2. Positions 2-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000025589.

2D gel databases

World-2DPAGE0004:Q9Z1B2.

Proteomic databases

PaxDbQ9Z1B2.
PRIDEQ9Z1B2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000072342; ENSRNOP00000065389; ENSRNOG00000049743.
ENSRNOT00000073649; ENSRNOP00000064813; ENSRNOG00000047034.
GeneID100912430.
64352.
KEGGrno:100912430.
rno:64352.
UCSCRGD:61964. rat.

Organism-specific databases

CTD2949.
RGD61964. Gstm5.

Phylogenomic databases

eggNOGNOG300089.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115735.
HOVERGENHBG106842.
InParanoidQ9Z1B2.
KOK00799.
OMAMSCESSM.
OrthoDBEOG7KH9M3.
PhylomeDBQ9Z1B2.
TreeFamTF353040.

Gene expression databases

GenevestigatorQ9Z1B2.

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

NextBio613032.
PROQ9Z1B2.

Entry information

Entry nameGSTM5_RAT
AccessionPrimary (citable) accession number: Q9Z1B2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 96 of the entry and version 3 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