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P15964

- GST26_SCHMA

UniProt

P15964 - GST26_SCHMA

Protein

Glutathione S-transferase class-mu 26 kDa isozyme

Gene
N/A
Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    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

    MAPKFGYWKV KGLVQPTRLL LEHLEETYEE RAYDRNEIDA WSNDKFKLGL    50
    EFPNLPYYID GDFKLTQSMA IIRYIADKHN MLGACPKERA EISMLEGAVL 100
    DIRMGVLRIA YNKEYETLKV DFLNKLPGRL KMFEDRLSNK TYLNGNCVTH 150
    PDFMLYDALD VVLYMDSQCL NEFPKLVSFK KCIEDLPQIK NYLNSSRYIK 200
    WPLQGWDATF GGGDTPPK 218
    Length:218
    Mass (Da):25,401
    Last modified:April 1, 1990 - v1
    Checksum:i061A6548A842D6E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31106 mRNA. Translation: AAA29888.1.
    M26913 mRNA. Translation: AAA29889.1.
    PIRiA45523.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31106 mRNA. Translation: AAA29888.1 .
    M26913 mRNA. Translation: AAA29889.1 .
    PIRi A45523.

    3D structure databases

    ProteinModelPortali P15964.
    SMRi P15964. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOGENOMi HOG000115735.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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