Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P09792

- GST28_SCHMA

UniProt

P09792 - GST28_SCHMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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 – 1410Combined sources
Helixi15 – 173Combined sources
Helixi18 – 2710Combined sources
Beta strandi32 – 365Combined sources
Turni38 – 403Combined sources
Helixi41 – 444Combined sources
Helixi45 – 473Combined sources
Beta strandi55 – 595Combined sources
Beta strandi61 – 633Combined sources
Beta strandi65 – 695Combined sources
Helixi71 – 8111Combined sources
Helixi89 – 11022Combined sources
Turni111 – 1144Combined sources
Helixi119 – 12911Combined sources
Helixi131 – 14414Combined sources
Beta strandi147 – 1526Combined sources
Helixi158 – 17316Combined sources
Turni175 – 1806Combined sources
Helixi183 – 19513Combined sources
Helixi197 – 2059Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP09792.
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

« Hide

        10         20         30         40         50
MAGEHIKVIY FDGRGRAESI RMTLVAAGVD YEDERISFQD WPKIKPTIPG
60 70 80 90 100
GRLPAVKVTD DHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYSVEKLIG
110 120 130 140 150
QAEDVEHEYH KTLMKPQEEK EKITKEILNG KVPVLLNMIC ESLKGSTGKL
160 170 180 190 200
AVGDKVTLAD LVLIAVIDHV TDLDKGFLTG KYPEIHKHRE NLLASSPRLA
210
KYLSNRPATP F
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:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 .

Phylogenomic databases

HOGENOMi HOG000115733.
InParanoidi P09792.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 102 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