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Protein

Glutathione S-transferase Mu 5

Gene

GSTM5

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 5By similarity (EC:2.5.1.18)
Alternative name(s):
GST class-mu 5By similarity
Gene namesi
Name:GSTM5By similarity
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Cytoplasm By similarity

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 – ›138›138Glutathione S-transferase Mu 5PRO_0000394302Add
BLAST

Proteomic databases

PRIDEiP86214.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP86214.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini‹1 – ›71›71GST N-terminalBy similarityAdd
BLAST
Domaini‹72 – 135›64GST C-terminalBy similarityAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 72Glutathione bindingBy similarity
Regioni39 – 435Glutathione bindingBy similarity
Regioni52 – 532Glutathione bindingBy similarity
Regioni65 – 662Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Sequence Analysis
Contains 1 GST C-terminal domain.Sequence Analysis
Contains 1 GST N-terminal domain.Sequence Analysis

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: Fragments.

P86214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SMVLGYWDIR RMLLEFTDTS YEEKRYICGE APDYDRSQWL DVKFKLDLDF
60 70 80 90 100
PNLPYLMDGK NKITQSNAIL RIRVDIMENQ IMDFRQFSLF LGKKLTFVDF
110 120 130
LTYDVLDQNR MFEPKCLDEF PNLKAFMCRC FKMPINNK
Length:138
Mass (Da):16,658
Last modified:May 18, 2010 - v1
Checksum:i68C99F8E788423A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-adjacent residuesi10 – 112Curated
Non-adjacent residuesi71 – 722Curated
Non-adjacent residuesi85 – 862Curated
Non-adjacent residuesi93 – 942Curated
Non-adjacent residuesi129 – 1302Curated
Non-terminal residuei138 – 1381

Cross-referencesi

3D structure databases

ProteinModelPortaliP86214.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP86214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
    Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
    Asian J. Androl. 12:344-355(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiGSTM5_MESAU
AccessioniPrimary (citable) accession number: P86214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: January 7, 2015
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.