GSTM_TYRPU
ID GSTM_TYRPU Reviewed; 218 AA.
AC M1RIR6;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Glutathione S-transferase {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000269|PubMed:23365207};
DE AltName: Full=GST class-mu {ECO:0000305};
DE AltName: Allergen=Tyr p 8 {ECO:0000303|PubMed:23365207};
OS Tyrophagus putrescentiae (Mold mite) (Acarus putrescentiae).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Acaroidea; Acaridae; Tyrophaginae;
OC Tyrophagus.
OX NCBI_TaxID=59818 {ECO:0000312|EMBL:AGG10560.1};
RN [1] {ECO:0000312|EMBL:AGG10560.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-17 AND 115-126,
RP IDENTIFICATION BY MASS SPECTROMETRY, 3D-STRUCTURE MODELING, CATALYTIC
RP ACTIVITY, AND ALLERGEN.
RX PubMed=23365207; DOI=10.1128/cvi.00633-12;
RA Liao E.-C., Lin Y.-H., Chiu C.-L., Lin T.-C., Tsai J.-J.;
RT "Identification of allergenic component Tyr p 8 from Tyrophagus
RT putrescentiae and cross-reactivity with Der p 8.";
RL Clin. Vaccine Immunol. 20:506-512(2013).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000250|UniProtKB:P09488}.
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 Evidence={ECO:0000269|PubMed:23365207};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 45% of
CC the 106 patients tested allergic to storage mite T.putrescentiae. The
CC percentage decreases to about 18% when sera from these patients is
CC first absorbed with D.pteronyssinus extract indicating high cross-
CC reactivity between the corresponding allergens of the two mites.
CC Induces histamine release from basophils.
CC {ECO:0000269|PubMed:23365207}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; JX255733; AGG10560.1; -; mRNA.
DR AlphaFoldDB; M1RIR6; -.
DR SMR; M1RIR6; -.
DR Allergome; 10807; Tyr p 8.
DR Allergome; 12338; Tyr p 8.0101.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
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; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
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 Allergen; Direct protein sequencing; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23365207"
FT CHAIN 2..218
FT /note="Glutathione S-transferase"
FT /id="PRO_0000447304"
FT DOMAIN 3..88
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 90..206
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT BINDING 9..10
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 43..46
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09488"
SQ SEQUENCE 218 AA; 25013 MW; AEB1A843CFE3201C CRC64;
MSSKPVLGYW DIRGLAQPIR LLLAYLDVDY EDKRYQLGAN FDRSAWLTEK FNLGLDFPNL
PYYIDGNVKL SQTLAILRYI GRKYKLTGAN EPEELRVSLV EQQVVDGNQS LSRVAYDPNA
DKLKPDFLKT LPDSVKQLSH FLGNSPFVAG TSITYVDFWL YEYLVKLSVL VPEVFGQFDN
LKKFVERIES LPRVSVYIKA QQPKLFNGPM AKWNGQYA
