Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione S-transferase Mu 5

Gene

Gstm5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Kineticsi

  1. KM=0.14 mM for glutathione1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_316307. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 5 (EC:2.5.1.18)
Alternative name(s):
GST class-mu 5
Gene namesi
Name:Gstm5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi61964. Gstm5.

Subcellular locationi

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225Glutathione S-transferase Mu 5PRO_0000271421Add
BLAST

Post-translational modificationi

The N-terminus is blocked.Curated

Proteomic databases

PaxDbiQ9Z1B2.
PRIDEiQ9Z1B2.

2D gel databases

World-2DPAGE0004:Q9Z1B2.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ9Z1B2.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025589.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1B2.
SMRiQ9Z1B2. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 9288GST N-terminalAdd
BLAST
Domaini94 – 212119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 122Glutathione bindingBy similarity
Regioni50 – 545Glutathione bindingBy similarity
Regioni63 – 642Glutathione bindingBy similarity
Regioni76 – 772Glutathione bindingBy similarity

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.
InParanoidiQ9Z1B2.
KOiK00799.
OMAiMSCESSM.
OrthoDBiEOG7KH9M3.
PhylomeDBiQ9Z1B2.
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.

Q9Z1B2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCSKSMVLG YWDIRGLAHA IRMLLEFTDT SYEEKQYTCG EAPDYDRSQW
60 70 80 90 100
LDVKFKLDLD FPNLPYLMDG KNKITQSNAI LRYIARKHNM CGDTEEEKIR
110 120 130 140 150
VDIMENQIMD FRMQLVRLCY NSNHESLKPQ YLEQLPAQLK QFSLFLGKFT
160 170 180 190 200
WFAGEKLTFV DFLTYDVLDQ NRMFEPKCLD EFPNLKAFMC RFEALEKIAA
210 220
FLQSDRCFKM PINNKMAKWG NKSIC
Length:225
Mass (Da):26,629
Last modified:January 23, 2007 - v3
Checksum:i45A2DC2DDCE5ACA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86635 mRNA. Translation: AAD00603.1.
RefSeqiNP_742035.1. NM_172038.1.
XP_003749426.1. XM_003749378.3.
UniGeneiRn.9158.

Genome annotation databases

EnsembliENSRNOT00000072342; ENSRNOP00000065389; ENSRNOG00000049743.
ENSRNOT00000073649; ENSRNOP00000064813; ENSRNOG00000047034.
GeneIDi100912430.
64352.
KEGGirno:100912430.
rno:64352.
UCSCiRGD:61964. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86635 mRNA. Translation: AAD00603.1.
RefSeqiNP_742035.1. NM_172038.1.
XP_003749426.1. XM_003749378.3.
UniGeneiRn.9158.

3D structure databases

ProteinModelPortaliQ9Z1B2.
SMRiQ9Z1B2. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025589.

2D gel databases

World-2DPAGE0004:Q9Z1B2.

Proteomic databases

PaxDbiQ9Z1B2.
PRIDEiQ9Z1B2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000072342; ENSRNOP00000065389; ENSRNOG00000049743.
ENSRNOT00000073649; ENSRNOP00000064813; ENSRNOG00000047034.
GeneIDi100912430.
64352.
KEGGirno:100912430.
rno:64352.
UCSCiRGD:61964. rat.

Organism-specific databases

CTDi2949.
RGDi61964. Gstm5.

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiQ9Z1B2.
KOiK00799.
OMAiMSCESSM.
OrthoDBiEOG7KH9M3.
PhylomeDBiQ9Z1B2.
TreeFamiTF353040.

Enzyme and pathway databases

ReactomeiREACT_316307. Glutathione conjugation.

Miscellaneous databases

NextBioi613032.
PROiQ9Z1B2.

Gene expression databases

GenevestigatoriQ9Z1B2.

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. "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.

Entry informationi

Entry nameiGSTM5_RAT
AccessioniPrimary (citable) accession number: Q9Z1B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.