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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: -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.

Miscellaneous

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei111SubstrateBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

BRENDAi2.5.1.18 5608

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001858061 – 218Glutathione S-transferase class-mu 26 kDa isozymeAdd BLAST218

Proteomic databases

PRIDEiP15964

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiP15964 baseline

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP15964
SMRiP15964
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 83GST N-terminalAdd BLAST83
Domaini85 – 203GST C-terminalAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 8Glutathione bindingBy similarity2
Regioni41 – 45Glutathione bindingBy similarity5
Regioni54 – 55Glutathione bindingBy similarity2
Regioni67 – 68Glutathione bindingBy similarity2

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated

Phylogenomic databases

eggNOGiENOG410IN5J Eukaryota
ENOG4110YU0 LUCA
HOGENOMiHOG000115735
OrthoDBiEOG091G0K2E

Family and domain databases

InterProiView protein in InterPro
IPR010987 Glutathione-S-Trfase_C-like
IPR036282 Glutathione-S-Trfase_C_sf
IPR004045 Glutathione_S-Trfase_N
IPR004046 GST_C
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF14497 GST_C_3, 1 hit
PF02798 GST_N, 1 hit
SUPFAMiSSF47616 SSF47616, 1 hit
SSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS50405 GST_CTER, 1 hit
PS50404 GST_NTER, 1 hit

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

Genome annotation databases

GeneDBiSmp_163610.1:pep

Similar proteinsi

Entry informationi

Entry nameiGST26_SCHMA
AccessioniPrimary (citable) accession number: P15964
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 23, 2018
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health