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Database: UniProt
Entry: A0A452ERH0_CAPHI
LinkDB: A0A452ERH0_CAPHI
Original site: A0A452ERH0_CAPHI 
ID   A0A452ERH0_CAPHI        Unreviewed;       211 AA.
AC   A0A452ERH0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
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   Name=LOC102184041 {ECO:0000313|Ensembl:ENSCHIP00000014777.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000014777.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000014777.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000014777.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   EMBL; LWLT01000026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A452ERH0; -.
DR   STRING; 9925.ENSCHIP00000014777; -.
DR   Ensembl; ENSCHIT00000022576.1; ENSCHIP00000014777.1; ENSCHIG00000015669.1.
DR   GeneTree; ENSGT00940000164125; -.
DR   Proteomes; UP000291000; Chromosome 29.
DR   Bgee; ENSCHIG00000015669; Expressed in descending colon and 17 other cell types or tissues.
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; 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:SF248; 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; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 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|RuleBase:RU368105};
KW   Mitochondrion {ECO:0000256|RuleBase:RU368105};
KW   Nucleus {ECO:0000256|RuleBase:RU368105};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW   Transferase {ECO:0000256|RuleBase:RU368105}.
FT   DOMAIN          2..81
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          83..205
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   211 AA;  23784 MW;  A3D051D00FAE19E6 CRC64;
     VPPYTIVYFP TRGRCEALRM LLADQDQSWK EEVVTKESWL QGPLKASCLY GQLPKFQDGD
     LTLYQSNAIL RHLGRSFGLY GTDEREAALV DMVNDGLEDL RRRCSHLIHH KAGAQGWAQY
     VRELPAHLKP FETLLSQNQG GQAFIVGNQI SFADYNLLDL LLNHQVLVPG CLDPFPLLSA
     YVARLSARPK LKAFLASPEH VNRPIFGSRK I
//
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