P09792 (GST28_SCHMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 84.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutathione S-transferase class-mu 28 kDa isozyme Short name=GST 28 EC=2.5.1.18 Alternative name(s): GSH transferase S.m. 1-1 Protective 28 kDa antigen Sm28 antigen Sm28GST Smp28 | ||||
| Gene names |
| ||||
| Organism | Schistosoma mansoni (Blood fluke) [Complete proteome] | ||||
| Taxonomic identifier | 6183 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Platyhelminthes › Trematoda › Digenea › Strigeidida › Schistosomatoidea › Schistosomatidae › Schistosoma |
Protein attributes
| Sequence length | 211 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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 activity | RX + glutathione = HX + R-S-glutathione. |
| Subunit structure | Homodimer. |
| Tissue specificity | 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). |
| Miscellaneous | There are at least three isoenzymes of GST in S.mansoni. |
| Sequence similarities | Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Transferase |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular function | glutathione transferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | |||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 211 | 210 | Glutathione S-transferase class-mu 28 kDa isozyme | PRO_0000185815 | ||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||
| Domain | 4 – 86 | 83 | GST N-terminal | |||||||||||||||||||||||||||||||||||||||||
| Domain | 88 – 211 | 124 | GST C-terminal | |||||||||||||||||||||||||||||||||||||||||
| Region | 41 – 45 | 5 | Glutathione binding | |||||||||||||||||||||||||||||||||||||||||
| Region | 70 – 71 | 2 | Glutathione binding | |||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 10 | 1 | Glutathione | |||||||||||||||||||||||||||||||||||||||||
| Binding site | 16 | 1 | Glutathione | |||||||||||||||||||||||||||||||||||||||||
| Binding site | 53 | 1 | Glutathione; via amide nitrogen and carbonyl oxygen | |||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.6 | |||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 47 | 1 | T → I AA sequence Ref.5 | |||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 106 | 1 | E → D AA sequence Ref.5 | |||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 5 – 14 | 10 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 15 – 17 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 18 – 27 | 10 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 32 – 36 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Turn | 38 – 40 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 41 – 44 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 45 – 47 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 59 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 61 – 63 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 65 – 69 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 71 – 81 | 11 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 89 – 110 | 22 | ||||||||||||||||||||||||||||||||||||||||||
| Turn | 111 – 114 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 119 – 129 | 11 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 131 – 144 | 14 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 152 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 158 – 173 | 16 | ||||||||||||||||||||||||||||||||||||||||||
| Turn | 175 – 180 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 183 – 195 | 13 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 197 – 205 | 9 | ||||||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning of a protective antigen of schistosomes." Balloul J.-M., Sondermeyer P., Dreyer D., Capron M., Grzych J.M., Pierce R.J., Carvallo D., Lecocq J.-P., Capron A. Nature 326:149-153(1987) [PubMed: 2434863] [Abstract] 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: 8444348] [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: 7519566] [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. El-Sayed N.M.Nature 460:352-358(2009) [PubMed: 19606141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "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: 3284744] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-47; 71-82; 92-106; 127-138; 142-152 AND 191-205, SUBUNIT, TISSUE SPECIFICITY. |
| [6] | "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: 7719482] [Abstract] Cited for: ACETYLATION AT ALA-2, MASS SPECTROMETRY. |
| [7] | "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: 1560466] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X05148 mRNA. Translation: CAA28796.1. M98271 Genomic DNA. Translation: AAA29891.1. S71584 mRNA. Translation: AAC60508.1. CABG01000068 Genomic DNA. Translation: CCD60449.1. | ||||||||||||
| PIR | JU0137. S02458. | ||||||||||||
| RefSeq | XP_002576704.1. XM_002576658.1. | ||||||||||||
| UniGene | Sma.6813. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P09792. | ||||||||||||
| SMR | P09792. Positions 4-211. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblMetazoa | Smp_054160__mRNA; Smp_054160__mRNA; Smp_054160. | ||||||||||||
| GeneID | 8342765. | ||||||||||||
| KEGG | smm:Smp_054160. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 8342765. | ||||||||||||
Phylogenomic databases | |||||||||||||
| PhylomeDB | P09792. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.20.1050.10. GST_C_like. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. | ||||||||||||
| KO | K01830. | ||||||||||||
| Pfam | PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit. | ||||||||||||
| PROSITE | PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | GST28_SCHMA | ||||||||
| Accession | Primary (citable) accession number: P09792 Secondary accession number(s): G4LZY1, Q7M446 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with