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Database: UniProt
Entry: A0A452EKG7_CAPHI
LinkDB: A0A452EKG7_CAPHI
Original site: A0A452EKG7_CAPHI 
ID   A0A452EKG7_CAPHI        Unreviewed;       210 AA.
AC   A0A452EKG7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=LOC100861197 {ECO:0000313|Ensembl:ENSCHIP00000012372.1};
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:ENSCHIP00000012372.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000012372.1, 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:ENSCHIP00000012372.1}
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; A0A452EKG7; -.
DR   SMR; A0A452EKG7; -.
DR   Ensembl; ENSCHIT00000020162.1; ENSCHIP00000012372.1; ENSCHIG00000014133.1.
DR   GeneTree; ENSGT00940000163435; -.
DR   Proteomes; UP000291000; Chromosome 29.
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; cd03210; GST_C_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:SF255; GLUTATHIONE S-TRANSFERASE P; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01268; GSTRNSFRASEP.
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|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..204
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   210 AA;  23462 MW;  1292D46D8B37BC03 CRC64;
     LPTLIAPFSP PPGRCEAMRM LLADQDQSWK EEVVAMQSWL QGPLKASCLY GQLPKFQDGD
     LTLYQSNAIL RHLGRTLGLY GKDQREAALV DMVNDGVEDL RCKYVSLIYT NYEAGKEDYV
     KALPQHLKPF ETLLSQNKGG QAFIVGDQIS FADYNLLDLL RIHQVLAPSC LDSFPLLSAY
     VARLNSRPKL KAFLASPEHV NRPINGNGKQ
//
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