ID   GST28_SCHMA             Reviewed;         211 AA.
AC   P09792; G4LZY1; Q7M446;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Glutathione S-transferase class-mu 28 kDa isozyme;
DE            Short=GST 28;
DE            EC=2.5.1.18;
DE   AltName: Full=GSH transferase S.m. 1-1;
DE   AltName: Full=Protective 28 kDa antigen;
DE   AltName: Full=Sm28 antigen;
DE   AltName: Full=Sm28GST;
DE   AltName: Full=Smp28;
GN   Name=GST28; ORFNames=Smp_054160;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2434863; DOI=10.1038/326149a0;
RA   Balloul J.-M., Sondermeyer P., Dreyer D., Capron M., Grzych J.M.,
RA   Pierce R.J., Carvallo D., Lecocq J.-P., Capron A.;
RT   "Molecular cloning of a protective antigen of schistosomes.";
RL   Nature 326:149-153(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8444348; DOI=10.1016/0378-1119(93)90400-w;
RA   McNair A.T., Dissous C., Duvaux-Miret O., Capron A.;
RT   "Cloning and characterisation of the gene encoding the 28-kDa glutathione
RT   S-transferase of Schistosoma mansoni.";
RL   Gene 124:245-249(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Puerto Rican;
RX   PubMed=7519566; DOI=10.1006/expr.1994.1065;
RA   Pierce R.J., Khalife J., Williams D.L., Kanno R., Trottein F., Lepresle T.,
RA   Sabatier J., Achstetter T., Capron A.;
RT   "Schistosoma mansoni: characterization of sequence variants of the 28-kDa
RT   glutathione S-transferase.";
RL   Exp. Parasitol. 79:81-84(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19606141; DOI=10.1038/nature08160;
RA   Berriman M., Haas B.J., LoVerde P.T., Wilson R.A., Dillon G.P.,
RA   Cerqueira G.C., Mashiyama S.T., Al-Lazikani B., Andrade L.F., Ashton P.D.,
RA   Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R., Coghlan A.,
RA   Coulson R., Day T.A., Delcher A., DeMarco R., Djikeng A., Eyre T.,
RA   Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H., Hirai Y.,
RA   Houston R., Ivens A., Johnston D.A., Lacerda D., Macedo C.D., McVeigh P.,
RA   Ning Z., Oliveira G., Overington J.P., Parkhill J., Pertea M., Pierce R.J.,
RA   Protasio A.V., Quail M.A., Rajandream M.A., Rogers J., Sajid M.,
RA   Salzberg S.L., Stanke M., Tivey A.R., White O., Williams D.L., Wortman J.,
RA   Wu W., Zamanian M., Zerlotini A., Fraser-Liggett C.M., Barrell B.G.,
RA   El-Sayed N.M.;
RT   "The genome of the blood fluke Schistosoma mansoni.";
RL   Nature 460:352-358(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican;
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [6]
RP   PROTEIN SEQUENCE OF 5-47; 71-82; 92-106; 127-138; 142-152 AND 191-205,
RP   SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=3284744; DOI=10.1002/j.1460-2075.1988.tb02834.x;
RA   Taylor J.B., Vidal A., Torpier G., Meyer D.J., Roitsch C., Balloul J.M.,
RA   Southan C., Sondermeyer P., Pemble S., Lecocq J.P., Capron A., Ketterer B.;
RT   "The glutathione transferase activity and tissue distribution of a cloned
RT   Mr28K protective antigen of Schistosoma mansoni.";
RL   EMBO J. 7:465-472(1988).
RN   [7]
RP   ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=7719482; DOI=10.1016/0378-4347(94)00298-3;
RA   Bouchon B., Jaquinod M., Klarskov K., Trottein F., Klein M.,
RA   van Dorsselaer A., Bischoff R., Roitsch C.;
RT   "Analysis of the primary structure and post-translational modifications of
RT   the Schistosoma mansoni antigen Smp28 by electrospray mass spectrometry.";
RL   J. Chromatogr. B 662:279-290(1994).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX   PubMed=1560466; DOI=10.1016/0022-2836(92)91013-f;
RA   Trottein F., Vaney M.C., Bachet B., Pierce R.J., Colloc'h N., Lecocq J.-P.,
RA   Capron A., Mornon J.-P.;
RT   "Crystallization and preliminary X-ray diffraction studies of a protective
RT   cloned 28 kDa glutathione S-transferase from Schistosoma mansoni.";
RL   J. Mol. Biol. 224:515-518(1992).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC   -!- FUNCTION: GST isoenzymes appear to play a central role in the parasite
CC       detoxification system. Other functions are also suspected including a
CC       role in increasing the solubility of haematin in the parasite gut.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1560466,
CC       ECO:0000269|PubMed:3284744}.
CC   -!- TISSUE SPECIFICITY: In the adult, expressed in excretory epithelial
CC       cells but absent from the caecal epithelium and flame cells. Also
CC       expressed in the tegument and its extensions into the parenchyma. In
CC       the schistosomulum, expressed in the tegument and associated
CC       structures. Not expressed in digestive tract, reproductive organs or
CC       muscles (at protein level). {ECO:0000269|PubMed:3284744}.
CC   -!- MISCELLANEOUS: There are at least three isoenzymes of GST in S.mansoni.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR   EMBL; X05148; CAA28796.1; -; mRNA.
DR   EMBL; M98271; AAA29891.1; -; Genomic_DNA.
DR   EMBL; S71584; AAC60508.1; -; mRNA.
DR   EMBL; CABG01000068; CCD60449.1; -; Genomic_DNA.
DR   PIR; JU0137; JU0137.
DR   PIR; S02458; S02458.
DR   RefSeq; XP_018646799.1; XM_018797487.1.
DR   PDB; 1U3I; X-ray; 1.89 A; A=1-211.
DR   PDBsum; 1U3I; -.
DR   AlphaFoldDB; P09792; -.
DR   SMR; P09792; -.
DR   STRING; 6183.P09792; -.
DR   iPTMnet; P09792; -.
DR   GeneID; 8342765; -.
DR   KEGG; smm:Smp_054160; -.
DR   CTD; 8342765; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   HOGENOM; CLU_039475_1_0_1; -.
DR   InParanoid; P09792; -.
DR   OMA; HEDAWRC; -.
DR   OrthoDB; 4995622at2759; -.
DR   PhylomeDB; P09792; -.
DR   EvolutionaryTrace; P09792; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03192; GST_C_Sigma_like; 1.
DR   CDD; cd03039; GST_N_Sigma_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF224; HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7719482"
FT   CHAIN           2..211
FT                   /note="Glutathione S-transferase class-mu 28 kDa isozyme"
FT                   /id="PRO_0000185815"
FT   DOMAIN          4..86
FT                   /note="GST N-terminal"
FT   DOMAIN          88..211
FT                   /note="GST C-terminal"
FT   BINDING         10..11
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         10
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:1560466"
FT   BINDING         16
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:1560466"
FT   BINDING         41..45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:1560466"
FT   BINDING         53
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:1560466"
FT   BINDING         55..56
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         70..71
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:1560466"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:7719482"
FT   CONFLICT        47
FT                   /note="T -> I (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="E -> D (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..14
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           18..27
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   STRAND          55..59
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           71..81
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           89..110
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           119..129
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           131..144
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           158..173
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   TURN            175..180
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           183..195
FT                   /evidence="ECO:0007829|PDB:1U3I"
FT   HELIX           197..205
FT                   /evidence="ECO:0007829|PDB:1U3I"
SQ   SEQUENCE   211 AA;  23820 MW;  F988AAF041D767E3 CRC64;
     MAGEHIKVIY FDGRGRAESI RMTLVAAGVD YEDERISFQD WPKIKPTIPG GRLPAVKVTD
     DHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYSVEKLIG QAEDVEHEYH KTLMKPQEEK
     EKITKEILNG KVPVLLNMIC ESLKGSTGKL AVGDKVTLAD LVLIAVIDHV TDLDKGFLTG
     KYPEIHKHRE NLLASSPRLA KYLSNRPATP F
//