GST28_SCHMA
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 03-AUG-2022, entry version 144.
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.Smp_054160.1; -.
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; LTYFDCR; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P09792; -.
DR EvolutionaryTrace; P09792; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 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
