GSTA3_CHICK
ID GSTA3_CHICK Reviewed; 229 AA.
AC P26697;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Glutathione S-transferase 3;
DE EC=2.5.1.18;
DE AltName: Full=GST class-alpha;
DE AltName: Full=GST-CL3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=1339283; DOI=10.1042/bj2810545;
RA Chang L.-H., Fan J.-Y., Liu L.-F., Tsai S.-P., Tam M.F.;
RT "Cloning and expression of a chick liver glutathione S-transferase CL 3
RT subunit with the use of a baculovirus expression system.";
RL Biochem. J. 281:545-551(1992).
CC -!- FUNCTION: Catalyzes the conjugation of GSH to a wide variety of
CC electrophilic alkylating agents. Also involved in the metabolism of
CC lipid hydroperoxides, prostaglandins and leukotriene A4 and in binding
CC of non-substrate hydrophobic ligands such as bile acids, a number of
CC drugs and thyroid hormones. This GST does not exhibit peroxidase
CC activity.
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:0000250|UniProtKB:Q16772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:Q16772};
CC -!- SUBUNIT: Homodimer or heterodimer (with a subunit from group CL-4).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: The variations were found from AA sequencing and imply
CC there are multiple forms of CL-3.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; M38219; AAA62731.1; -; mRNA.
DR PIR; S19734; S19734.
DR RefSeq; NP_990743.1; NM_205412.1.
DR PDB; 1VF1; X-ray; 1.77 A; A=1-229.
DR PDB; 1VF2; X-ray; 2.15 A; A/B=1-229.
DR PDB; 1VF3; X-ray; 2.15 A; A/B=1-229.
DR PDB; 1VF4; X-ray; 2.45 A; A=1-229.
DR PDBsum; 1VF1; -.
DR PDBsum; 1VF2; -.
DR PDBsum; 1VF3; -.
DR PDBsum; 1VF4; -.
DR AlphaFoldDB; P26697; -.
DR SMR; P26697; -.
DR STRING; 9031.ENSGALP00000026283; -.
DR PaxDb; P26697; -.
DR GeneID; 396380; -.
DR KEGG; gga:396380; -.
DR VEuPathDB; HostDB:LOC396380; -.
DR eggNOG; KOG1695; Eukaryota.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P26697; -.
DR SABIO-RK; P26697; -.
DR EvolutionaryTrace; P26697; -.
DR PRO; PR:P26697; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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; IPR003080; GST_alpha.
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 PRINTS; PR01266; GSTRNSFRASEA.
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; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..229
FT /note="Glutathione S-transferase 3"
FT /id="PRO_0000185800"
FT DOMAIN 3..83
FT /note="GST N-terminal"
FT DOMAIN 85..207
FT /note="GST C-terminal"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0007744|PDB:1VF1, ECO:0007744|PDB:1VF2,
FT ECO:0007744|PDB:1VF3"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0007744|PDB:1VF1, ECO:0007744|PDB:1VF2,
FT ECO:0007744|PDB:1VF3"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0007744|PDB:1VF1, ECO:0007744|PDB:1VF2,
FT ECO:0007744|PDB:1VF3"
FT MOD_RES 2
FT /note="Blocked amino end (Ala)"
FT VARIANT 45
FT /note="L -> V"
FT VARIANT 47
FT /note="S -> A"
FT VARIANT 49
FT /note="I -> F"
FT VARIANT 49
FT /note="I -> V"
FT VARIANT 52
FT /note="F -> R"
FT VARIANT 129..130
FT /note="TS -> AN"
FT VARIANT 135..136
FT /note="AY -> VF"
FT VARIANT 155
FT /note="W -> R"
FT VARIANT 158..159
FT /note="IH -> VV"
FT VARIANT 163
FT /note="A -> T"
FT VARIANT 166
FT /note="M -> A"
FT VARIANT 168
FT /note="E -> V"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:1VF1"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:1VF1"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:1VF1"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1VF1"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 86..104
FT /evidence="ECO:0007829|PDB:1VF1"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1VF3"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 114..130
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:1VF1"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:1VF1"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:1VF1"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:1VF1"
SQ SEQUENCE 229 AA; 26326 MW; EA30D949034BD8DB CRC64;
MAAKPVLYYF NGRGKMESIR WLLAAAGVEF EEVFLETREQ YEKLLQSGIL MFQQVPMVEI
DGMKLVQTRA ILNYIAGKYN LYGKDLKERA LIDMYVGGTD DLMGFLLSFP FLSAEDKVKQ
CAFVVEKATS RYFPAYEKVL KDHGQDFLVG NRLSWADIHL LEAILMVEEK KSDALSGFPL
LQAFKKRISS IPTIKKFLAP GSKRKPISDD KYVETVRRVL RMYYDVKPH
