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Protein

Glutathione S-transferase class-mu 26 kDa isozyme

Gene
N/A
Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111SubstrateBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase class-mu 26 kDa isozyme (EC:2.5.1.18)
Short name:
GST 26
Alternative name(s):
Sm26/1 antigen
SmGST
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Glutathione S-transferase class-mu 26 kDa isozymePRO_0000185806Add
BLAST

Expressioni

Tissue specificityi

Tegument and in subtegumentary parenchymal cells. GST 26 may be actively excreted by adult worms.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP15964.
SMRiP15964. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8383GST N-terminalAdd
BLAST
Domaini85 – 203119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione bindingBy similarity
Regioni41 – 455Glutathione bindingBy similarity
Regioni54 – 552Glutathione bindingBy similarity
Regioni67 – 682Glutathione 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

HOGENOMiHOG000115735.

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15964-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPKFGYWKV KGLVQPTRLL LEHLEETYEE RAYDRNEIDA WSNDKFKLGL
60 70 80 90 100
EFPNLPYYID GDFKLTQSMA IIRYIADKHN MLGACPKERA EISMLEGAVL
110 120 130 140 150
DIRMGVLRIA YNKEYETLKV DFLNKLPGRL KMFEDRLSNK TYLNGNCVTH
160 170 180 190 200
PDFMLYDALD VVLYMDSQCL NEFPKLVSFK KCIEDLPQIK NYLNSSRYIK
210
WPLQGWDATF GGGDTPPK
Length:218
Mass (Da):25,401
Last modified:April 1, 1990 - v1
Checksum:i061A6548A842D6E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31106 mRNA. Translation: AAA29888.1.
M26913 mRNA. Translation: AAA29889.1.
PIRiA45523.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31106 mRNA. Translation: AAA29888.1.
M26913 mRNA. Translation: AAA29889.1.
PIRiA45523.

3D structure databases

ProteinModelPortaliP15964.
SMRiP15964. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000115735.

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and tissue distribution of a 26-kilodalton Schistosoma mansoni glutathione S-transferase."
    Trottein F., Kieny M.P., Verwaerde C., Torpier G., Pierce R.J., Balloul J.-M., Schmitt D., Lecocq J.-P., Capron A.
    Mol. Biochem. Parasitol. 41:35-44(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Puerto Rican.
  2. "Comparison of the cloned genes of the 26- and 28-kilodalton glutathione S-transferases of Schistosoma japonicum and Schistosoma mansoni."
    Henkle K.J., Davern K.M., Wright M.D., Ramos A.J., Mitchell G.F.
    Mol. Biochem. Parasitol. 40:23-34(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-218.
    Strain: Puerto Rican.

Entry informationi

Entry nameiGST26_SCHMA
AccessioniPrimary (citable) accession number: P15964
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 1, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

There are at least three isoenzymes of GST in S.mansoni.

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.