ID A0A1A6H5H7_NEOLE Unreviewed; 210 AA.
AC A0A1A6H5H7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU368105};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU368105};
DE AltName: Full=GST class-pi {ECO:0000256|RuleBase:RU368105};
GN ORFNames=A6R68_12525 {ECO:0000313|EMBL:OBS72857.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS72857.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS72857.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS72857.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS72857.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|RuleBase:RU368105}.
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:0000256|RuleBase:RU368105};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368105}.
CC Mitochondrion {ECO:0000256|RuleBase:RU368105}. Nucleus
CC {ECO:0000256|RuleBase:RU368105}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family.
CC {ECO:0000256|ARBA:ARBA00007297, ECO:0000256|RuleBase:RU368105}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS72857.1}.
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DR EMBL; LZPO01055072; OBS72857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6H5H7; -.
DR STRING; 56216.A0A1A6H5H7; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd03076; GST_N_Pi; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF264; GLUTATHIONE S-TRANSFERASE; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368105};
KW Mitochondrion {ECO:0000256|RuleBase:RU368105};
KW Nucleus {ECO:0000256|RuleBase:RU368105};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW Transferase {ECO:0000256|RuleBase:RU368105}.
FT DOMAIN 2..81
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 83..204
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 210 AA; 24059 MW; C68958B0ED4F9512 CRC64;
MPPYTIVYFP SRGRCEVIRM LLADQGQSWK EEVVTLDAWG QDTLKASCLF GQLPKFQDGD
LTLYQSNAIL RHLGRSFGLY GKDQREAALV DMVNDGLEDL IRHRGQLFLR NYEEAKAQCL
KELPGHLKPF ETVLAQNKGG QSFIVGDQIS FADYRLLDFL LNHELLFPGY LNDYPLLSAY
VERLRARPKL KAFLDSPEHV NRPISSRLKI
//
