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P46409 (GSTMU_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 85. 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 1

EC=2.5.1.18
Alternative name(s):
GST Mu I
GST class-mu
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length218 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.

Subcellular location

Cytoplasm.

Tissue specificity

Well expressed in rabbit liver, brain and kidney.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Glutathione S-transferase Mu 1
PRO_0000185837

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

Sites

Binding site1161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P46409 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 481EA4AB85671102

FASTA21825,417
        10         20         30         40         50         60 
MPMTLGYWDV RGLALPIRML LEYTDTSYEE KKYTMGDAPN YDQSKWLSEK FTLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGTHKL TQSNAILRYL ARKHGLCGET EEERIRVDIL ENQLMDNRFQ LVNVCYSPDF 

       130        140        150        160        170        180 
EKLKPEYLKG LPEKLQLYSQ FLGSLPWFAG DKITFADFLV YDVLDQNRIF VPGCLDAFPN 

       190        200        210 
LKDFHVRFEG LPKISAYMKS SRFIRVPVFL KKATWTGI 

« Hide

References

[1]"Cloning and expression of a cDNA for mu-class glutathione S-transferase from rabbit liver."
Lee S.H., Lee S.H., Han J.S., Kim Y.S., Koh J.K.
Arch. Biochem. Biophys. 318:424-429(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Purification and characterization of class mu glutathione S-transferase isozymes from rabbit hepatic tissue."
Primiano T., Novak R.F.
Arch. Biochem. Biophys. 301:404-410(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L23766 mRNA. Translation: AAA69665.1.
PIRS65674.
RefSeqNP_001075721.1. NM_001082252.1.
UniGeneOcu.2029.

3D structure databases

ProteinModelPortalP46409.
SMRP46409. Positions 1-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000021965.

Proteomic databases

PRIDEP46409.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009073.

Organism-specific databases

CTD2946.

Phylogenomic databases

eggNOGNOG300089.
HOGENOMHOG000115735.
HOVERGENHBG106842.

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...

Entry information

Entry nameGSTMU_RABIT
AccessionPrimary (citable) accession number: P46409
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 85 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