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P09792

- GST28_SCHMA

UniProt

P09792 - GST28_SCHMA

Protein

Glutathione S-transferase class-mu 28 kDa isozyme

Gene

GST28

Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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 sitei10 – 101Glutathione1 Publication
    Binding sitei16 – 161Glutathione1 Publication
    Binding sitei53 – 531Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

    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 28 kDa isozyme (EC:2.5.1.18)
    Short name:
    GST 28
    Alternative name(s):
    GSH transferase S.m. 1-1
    Protective 28 kDa antigen
    Sm28 antigen
    Sm28GST
    Smp28
    Gene namesi
    Name:GST28
    ORF Names:Smp_054160
    OrganismiSchistosoma mansoni (Blood fluke)
    Taxonomic identifieri6183 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma
    ProteomesiUP000008854: Unassembled WGS sequence

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 211210Glutathione S-transferase class-mu 28 kDa isozymePRO_0000185815Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Expressioni

    Tissue specificityi

    In the adult, expressed in excretory epithelial cells but absent from the caecal epithelium and flame cells. Also expressed in the tegument and its extensions into the parenchyma. In the schistosomulum, expressed in the tegument and associated structures. Not expressed in digestive tract, reproductive organs or muscles (at protein level).1 Publication

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1410
    Helixi15 – 173
    Helixi18 – 2710
    Beta strandi32 – 365
    Turni38 – 403
    Helixi41 – 444
    Helixi45 – 473
    Beta strandi55 – 595
    Beta strandi61 – 633
    Beta strandi65 – 695
    Helixi71 – 8111
    Helixi89 – 11022
    Turni111 – 1144
    Helixi119 – 12911
    Helixi131 – 14414
    Beta strandi147 – 1526
    Helixi158 – 17316
    Turni175 – 1806
    Helixi183 – 19513
    Helixi197 – 2059

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U3IX-ray1.89A1-211[»]
    ProteinModelPortaliP09792.
    SMRiP09792. Positions 4-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09792.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 8683GST N-terminalAdd
    BLAST
    Domaini88 – 211124GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 455Glutathione binding
    Regioni70 – 712Glutathione binding

    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

    HOGENOMiHOG000115733.
    KOiK01830.
    PhylomeDBiP09792.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P09792-1 [UniParc]FASTAAdd to Basket

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    MAGEHIKVIY FDGRGRAESI RMTLVAAGVD YEDERISFQD WPKIKPTIPG    50
    GRLPAVKVTD DHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYSVEKLIG 100
    QAEDVEHEYH KTLMKPQEEK EKITKEILNG KVPVLLNMIC ESLKGSTGKL 150
    AVGDKVTLAD LVLIAVIDHV TDLDKGFLTG KYPEIHKHRE NLLASSPRLA 200
    KYLSNRPATP F 211
    Length:211
    Mass (Da):23,820
    Last modified:July 1, 1989 - v1
    Checksum:iF988AAF041D767E3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti47 – 471T → I AA sequence (PubMed:3284744)Curated
    Sequence conflicti106 – 1061E → D AA sequence (PubMed:3284744)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05148 mRNA. Translation: CAA28796.1.
    M98271 Genomic DNA. Translation: AAA29891.1.
    S71584 mRNA. Translation: AAC60508.1.
    CABG01000068 Genomic DNA. Translation: CCD60449.1.
    PIRiJU0137.
    S02458.
    UniGeneiSma.6813.

    Genome annotation databases

    EnsemblMetazoaiSmp_054160.1; Smp_054160.1:pep; Smp_054160.
    KEGGismm:Smp_054160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05148 mRNA. Translation: CAA28796.1 .
    M98271 Genomic DNA. Translation: AAA29891.1 .
    S71584 mRNA. Translation: AAC60508.1 .
    CABG01000068 Genomic DNA. Translation: CCD60449.1 .
    PIRi JU0137.
    S02458.
    UniGenei Sma.6813.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U3I X-ray 1.89 A 1-211 [» ]
    ProteinModelPortali P09792.
    SMRi P09792. Positions 4-211.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai Smp_054160.1 ; Smp_054160.1:pep ; Smp_054160 .
    KEGGi smm:Smp_054160.

    Phylogenomic databases

    HOGENOMi HOG000115733.
    KOi K01830.
    PhylomeDBi P09792.

    Miscellaneous databases

    EvolutionaryTracei P09792.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Cloning and characterisation of the gene encoding the 28-kDa glutathione S-transferase of Schistosoma mansoni."
      McNair A.T., Dissous C., Duvaux-Miret O., Capron A.
      Gene 124:245-249(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Schistosoma mansoni: characterization of sequence variants of the 28-kDa glutathione S-transferase."
      Pierce R.J., Khalife J., Williams D.L., Kanno R., Trottein F., Lepresle T., Sabatier J., Achstetter T., Capron A.
      Exp. Parasitol. 79:81-84(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Puerto Rican.
    4. "The genome of the blood fluke Schistosoma mansoni."
      Berriman M., Haas B.J., LoVerde P.T., Wilson R.A., Dillon G.P., Cerqueira G.C., Mashiyama S.T., Al-Lazikani B., Andrade L.F., Ashton P.D., Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R., Coghlan A., Coulson R., Day T.A., Delcher A.
      , DeMarco R., Djikeng A., Eyre T., Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H., Hirai Y., Houston R., Ivens A., Johnston D.A., Lacerda D., Macedo C.D., McVeigh P., Ning Z., Oliveira G., Overington J.P., Parkhill J., Pertea M., Pierce R.J., Protasio A.V., Quail M.A., Rajandream M.A., Rogers J., Sajid M., Salzberg S.L., Stanke M., Tivey A.R., White O., Williams D.L., Wortman J., Wu W., Zamanian M., Zerlotini A., Fraser-Liggett C.M., Barrell B.G., El-Sayed N.M.
      Nature 460:352-358(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Puerto Rican.
    6. "The glutathione transferase activity and tissue distribution of a cloned Mr28K protective antigen of Schistosoma mansoni."
      Taylor J.B., Vidal A., Torpier G., Meyer D.J., Roitsch C., Balloul J.M., Southan C., Sondermeyer P., Pemble S., Lecocq J.P., Capron A., Ketterer B.
      EMBO J. 7:465-472(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-47; 71-82; 92-106; 127-138; 142-152 AND 191-205, SUBUNIT, TISSUE SPECIFICITY.
    7. "Analysis of the primary structure and post-translational modifications of the Schistosoma mansoni antigen Smp28 by electrospray mass spectrometry."
      Bouchon B., Jaquinod M., Klarskov K., Trottein F., Klein M., van Dorsselaer A., Bischoff R., Roitsch C.
      J. Chromatogr. B 662:279-290(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Crystallization and preliminary X-ray diffraction studies of a protective cloned 28 kDa glutathione S-transferase from Schistosoma mansoni."
      Trottein F., Vaney M.C., Bachet B., Pierce R.J., Colloc'h N., Lecocq J.-P., Capron A., Mornon J.-P.
      J. Mol. Biol. 224:515-518(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.

    Entry informationi

    Entry nameiGST28_SCHMA
    AccessioniPrimary (citable) accession number: P09792
    Secondary accession number(s): G4LZY1, Q7M446
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 100 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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3