ID B5XC10_SALSA Unreviewed; 207 AA.
AC B5XC10;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=GSTP1 {ECO:0000313|EMBL:ACI68380.1};
GN Synonyms=LOC106611534 {ECO:0000313|RefSeq:XP_014067301.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI68380.1};
RN [1] {ECO:0000313|EMBL:ACI68380.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI68380.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI68380.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI68380.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACI68380.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI68380.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:XP_014067301.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014067301.1};
RG RefSeq;
RL Submitted (NOV-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}.
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; BT048579; ACI68380.1; -; mRNA.
DR RefSeq; XP_014067301.1; XM_014211826.1.
DR STRING; 8030.ENSSSAP00000023183; -.
DR PaxDb; 8030-ENSSSAP00000023183; -.
DR Ensembl; ENSSSAT00000192588; ENSSSAP00000144111; ENSSSAG00000015545.
DR GeneID; 106611534; -.
DR KEGG; sasa:106611534; -.
DR OMA; YWHTIRN; -.
DR OrthoDB; 5302341at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR Bgee; ENSSSAG00000015545; Expressed in pharyngeal gill and 8 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 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:SF141; GLUTATHIONE S-TRANSFERASE P; 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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU368105};
KW Mitochondrion {ECO:0000256|RuleBase:RU368105};
KW Nucleus {ECO:0000256|RuleBase:RU368105};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|RuleBase:RU368105, ECO:0000313|EMBL:ACI68380.1}.
FT DOMAIN 1..80
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 82..201
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 207 AA; 23635 MW; 9174631511567403 CRC64;
MSLTLTYFPV RGRAEVIRVM LKDQGAEFDE KVITMEMWKE GTLKASCLFG QLPIFQDGDL
TLYQTNAIRR HLARKLGLYG KDQREAALID MMDEAIQDLL NKYIKLMFEK DDSGKERYLK
ALPTDLKPFE KTLSSNKGSF LVGDKISLAD YALVLLLIHH QVLSPPCLDA FPSLQSYLKR
LCARPNLHAY LHSDDFKNRP IIPGNRA
//
