GSTM1_DERPT
ID GSTM1_DERPT Reviewed; 219 AA.
AC P46419;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glutathione S-transferase;
DE EC=2.5.1.18;
DE AltName: Full=GST class-mu;
DE AltName: Full=Major allergen Der p 8;
DE AltName: Full=P dp 15;
DE AltName: Allergen=Der p 8;
OS Dermatophagoides pteronyssinus (European house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6956;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7918651; DOI=10.1016/0167-4781(94)90080-9;
RA O'Neill G.M., Donovan G.R., Baldo B.A.;
RT "Cloning and characterization of a major allergen of the house dust mite,
RT Dermatophagoides pteronyssinus, homologous with glutathione S-
RT transferase.";
RL Biochim. Biophys. Acta 1219:521-528(1994).
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S75286; AAB32224.1; -; mRNA.
DR PIR; S50146; S50146.
DR PDB; 4Q5Q; X-ray; 1.93 A; A/B=1-219.
DR PDBsum; 4Q5Q; -.
DR AlphaFoldDB; P46419; -.
DR SMR; P46419; -.
DR Allergome; 322; Der p 8.
DR Allergome; 3269; Der p 8.0101.
DR BRENDA; 2.5.1.18; 1873.
DR Proteomes; UP000515146; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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 3D-structure; Allergen; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..219
FT /note="Glutathione S-transferase"
FT /id="PRO_0000185839"
FT DOMAIN 2..89
FT /note="GST N-terminal"
FT DOMAIN 91..207
FT /note="GST C-terminal"
FT BINDING 8..9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 44..47
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 51
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 60..61
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 73..74
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 92..116
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 121..143
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 157..171
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:4Q5Q"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4Q5Q"
SQ SEQUENCE 219 AA; 25590 MW; EC4A739CD40FC4B4 CRC64;
MSQPILGYWD IRGYAQPIRL LLTYSGVDFV DKRYQIGPAP DFDRSEWLNE KFNLGLDFPN
LPYYIDGDMK MTQTFAILRY LGRKYKLNGS NDHEEIRISM AEQQTEDMMA AMIRVCYDAN
CDKLKPDYLK SLPDCLKLMS KFVGEHAFIA GANISYVDFN LYEYLCHVKV MVPEVFGQFE
NLKRYVERME SLPRVSDYIK KQQPKTFNAP TSKWNASYA
