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Glutathione S-transferase class-mu 28 kDa isozyme (GST 28) (EC 2.5.1.18) (GSH transferase S.m. 1-1) (Protective 28 kDa antigen) (Sm28 antigen) (Sm28GST) (Smp28)

 GST28_SCHMA             Reviewed;         211 AA.
P09792; G4LZY1; Q7M446;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
27-SEP-2017, entry version 117.
RecName: Full=Glutathione S-transferase class-mu 28 kDa isozyme;
Short=GST 28;
EC=2.5.1.18;
AltName: Full=GSH transferase S.m. 1-1;
AltName: Full=Protective 28 kDa antigen;
AltName: Full=Sm28 antigen;
AltName: Full=Sm28GST;
AltName: Full=Smp28;
Name=GST28; ORFNames=Smp_054160;
Schistosoma mansoni (Blood fluke).
Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida;
Schistosomatoidea; Schistosomatidae; Schistosoma.
NCBI_TaxID=6183;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2434863; DOI=10.1038/326149a0;
Balloul J.-M., Sondermeyer P., Dreyer D., Capron M., Grzych J.M.,
Pierce R.J., Carvallo D., Lecocq J.-P., Capron A.;
"Molecular cloning of a protective antigen of schistosomes.";
Nature 326:149-153(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8444348; DOI=10.1016/0378-1119(93)90400-W;
McNair A.T., Dissous C., Duvaux-Miret O., Capron A.;
"Cloning and characterisation of the gene encoding the 28-kDa
glutathione S-transferase of Schistosoma mansoni.";
Gene 124:245-249(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Puerto Rican;
PubMed=7519566; DOI=10.1006/expr.1994.1065;
Pierce R.J., Khalife J., Williams D.L., Kanno R., Trottein F.,
Lepresle T., Sabatier J., Achstetter T., Capron A.;
"Schistosoma mansoni: characterization of sequence variants of the 28-
kDa glutathione S-transferase.";
Exp. Parasitol. 79:81-84(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=19606141; DOI=10.1038/nature08160;
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.;
"The genome of the blood fluke Schistosoma mansoni.";
Nature 460:352-358(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Puerto Rican;
PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
Zerlotini A., Dunne D.W., Berriman M.;
"A systematically improved high quality genome and transcriptome of
the human blood fluke Schistosoma mansoni.";
PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
[6]
PROTEIN SEQUENCE OF 5-47; 71-82; 92-106; 127-138; 142-152 AND 191-205,
SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=3284744;
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.;
"The glutathione transferase activity and tissue distribution of a
cloned Mr28K protective antigen of Schistosoma mansoni.";
EMBO J. 7:465-472(1988).
[7]
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=7719482; DOI=10.1016/0378-4347(94)00298-3;
Bouchon B., Jaquinod M., Klarskov K., Trottein F., Klein M.,
van Dorsselaer A., Bischoff R., Roitsch C.;
"Analysis of the primary structure and post-translational
modifications of the Schistosoma mansoni antigen Smp28 by electrospray
mass spectrometry.";
J. Chromatogr. B 662:279-290(1994).
[8]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
PubMed=1560466; DOI=10.1016/0022-2836(92)91013-F;
Trottein F., Vaney M.C., Bachet B., Pierce R.J., Colloc'h N.,
Lecocq J.-P., Capron A., Mornon J.-P.;
"Crystallization and preliminary X-ray diffraction studies of a
protective cloned 28 kDa glutathione S-transferase from Schistosoma
mansoni.";
J. Mol. Biol. 224:515-518(1992).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles.
-!- FUNCTION: 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: Homodimer. {ECO:0000269|PubMed:1560466,
ECO:0000269|PubMed:3284744}.
-!- 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).
{ECO:0000269|PubMed:3284744}.
-!- MISCELLANEOUS: There are at least three isoenzymes of GST in
S.mansoni.
-!- SIMILARITY: Belongs to the GST superfamily. Mu family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X05148; CAA28796.1; -; mRNA.
EMBL; M98271; AAA29891.1; -; Genomic_DNA.
EMBL; S71584; AAC60508.1; -; mRNA.
EMBL; CABG01000068; CCD60449.1; -; Genomic_DNA.
PIR; JU0137; JU0137.
PIR; S02458; S02458.
RefSeq; XP_018646799.1; XM_018797487.1.
UniGene; Sma.6813; -.
PDB; 1U3I; X-ray; 1.89 A; A=1-211.
PDBsum; 1U3I; -.
ProteinModelPortal; P09792; -.
SMR; P09792; -.
STRING; 6183.Smp_054160__mRNA; -.
EnsemblMetazoa; Smp_054160.1; Smp_054160.1:pep; Smp_054160.
GeneDB; Smp_054160.1:pep; -.
GeneDB; Smp_059340.1:pep; -.
GeneID; 8342765; -.
CTD; 8342765; -.
eggNOG; ENOG410IN5B; Eukaryota.
eggNOG; ENOG4112BRZ; LUCA.
HOGENOM; HOG000115733; -.
InParanoid; P09792; -.
OMA; DYEDERI; -.
OrthoDB; EOG091G0MBB; -.
PhylomeDB; P09792; -.
EvolutionaryTrace; P09792; -.
Proteomes; UP000008854; Unassembled WGS sequence.
GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7719482}.
CHAIN 2 211 Glutathione S-transferase class-mu 28 kDa
isozyme.
/FTId=PRO_0000185815.
DOMAIN 4 86 GST N-terminal.
DOMAIN 88 211 GST C-terminal.
REGION 10 11 Glutathione binding.
{ECO:0000250|UniProtKB:P08515}.
REGION 41 45 Glutathione binding.
{ECO:0000269|PubMed:1560466}.
REGION 55 56 Glutathione binding.
{ECO:0000250|UniProtKB:P08515}.
REGION 70 71 Glutathione binding.
{ECO:0000269|PubMed:1560466}.
BINDING 10 10 Glutathione.
{ECO:0000269|PubMed:1560466}.
BINDING 16 16 Glutathione.
{ECO:0000269|PubMed:1560466}.
BINDING 53 53 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:1560466}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:7719482}.
CONFLICT 47 47 T -> I (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 106 106 E -> D (in Ref. 6; AA sequence).
{ECO:0000305}.
STRAND 5 14 {ECO:0000244|PDB:1U3I}.
HELIX 15 17 {ECO:0000244|PDB:1U3I}.
HELIX 18 27 {ECO:0000244|PDB:1U3I}.
STRAND 32 36 {ECO:0000244|PDB:1U3I}.
TURN 38 40 {ECO:0000244|PDB:1U3I}.
HELIX 41 44 {ECO:0000244|PDB:1U3I}.
HELIX 45 47 {ECO:0000244|PDB:1U3I}.
STRAND 55 59 {ECO:0000244|PDB:1U3I}.
STRAND 61 63 {ECO:0000244|PDB:1U3I}.
STRAND 65 69 {ECO:0000244|PDB:1U3I}.
HELIX 71 81 {ECO:0000244|PDB:1U3I}.
HELIX 89 110 {ECO:0000244|PDB:1U3I}.
TURN 111 114 {ECO:0000244|PDB:1U3I}.
HELIX 119 129 {ECO:0000244|PDB:1U3I}.
HELIX 131 144 {ECO:0000244|PDB:1U3I}.
STRAND 147 152 {ECO:0000244|PDB:1U3I}.
HELIX 158 173 {ECO:0000244|PDB:1U3I}.
TURN 175 180 {ECO:0000244|PDB:1U3I}.
HELIX 183 195 {ECO:0000244|PDB:1U3I}.
HELIX 197 205 {ECO:0000244|PDB:1U3I}.
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


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