GSTO1_PIG
ID GSTO1_PIG Reviewed; 241 AA.
AC Q9N1F5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glutathione S-transferase omega-1;
DE Short=GSTO-1;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P78417};
DE AltName: Full=Glutathione S-transferase omega 1-1;
DE Short=GSTO 1-1;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE EC=1.8.5.1 {ECO:0000250|UniProtKB:P78417};
DE AltName: Full=Monomethylarsonic acid reductase;
DE Short=MMA(V) reductase;
DE EC=1.20.4.2 {ECO:0000250|UniProtKB:P78417};
DE AltName: Full=S-(Phenacyl)glutathione reductase;
DE Short=SPG-R;
GN Name=GSTO1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-31; 58-83; 101-110;
RP 115-147; 149-160; 162-190; 201-228 AND 235-241, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=11485575; DOI=10.1042/0264-6021:3580257;
RA Rouimi P., Anglade P., Benzekri A., Costet P., Debrauwer L., Pineau T.,
RA Tulliez J.;
RT "Purification and characterization of a glutathione S-transferase Omega in
RT pig: evidence for two distinct organ-specific transcripts.";
RL Biochem. J. 358:257-262(2001).
CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase and
CC dehydroascorbate reductase activities. Has S-(phenacyl)glutathione
CC reductase activity. Has also glutathione S-transferase activity.
CC Participates in the biotransformation of inorganic arsenic and reduces
CC monomethylarsonic acid (MMA) and dimethylarsonic acid.
CC {ECO:0000250|UniProtKB:P78417}.
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:P78417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC Evidence={ECO:0000250|UniProtKB:P78417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC Evidence={ECO:0000250|UniProtKB:P78417};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11485575}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11485575}.
CC -!- TISSUE SPECIFICITY: Most abundant in the liver and skeletal muscle;
CC also expressed in heart, diaphragm, colon, thymus, kidney, lung,
CC ovaries, spleen, intestine and pancreas. {ECO:0000269|PubMed:11485575}.
CC -!- MASS SPECTROMETRY: Mass=27328; Mass_error=3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11485575};
CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000305}.
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; AF188838; AAF71994.2; -; mRNA.
DR RefSeq; NP_999215.1; NM_214050.2.
DR AlphaFoldDB; Q9N1F5; -.
DR SMR; Q9N1F5; -.
DR STRING; 9823.ENSSSCP00000011305; -.
DR PaxDb; Q9N1F5; -.
DR PeptideAtlas; Q9N1F5; -.
DR PRIDE; Q9N1F5; -.
DR Ensembl; ENSSSCT00000011607; ENSSSCP00000011305; ENSSSCG00000022351.
DR Ensembl; ENSSSCT00005012023; ENSSSCP00005007045; ENSSSCG00005007916.
DR Ensembl; ENSSSCT00015047497; ENSSSCP00015018811; ENSSSCG00015035687.
DR Ensembl; ENSSSCT00025094544; ENSSSCP00025041522; ENSSSCG00025068774.
DR Ensembl; ENSSSCT00030014022; ENSSSCP00030006281; ENSSSCG00030010226.
DR Ensembl; ENSSSCT00035026899; ENSSSCP00035010267; ENSSSCG00035020670.
DR Ensembl; ENSSSCT00040039734; ENSSSCP00040016647; ENSSSCG00040029505.
DR Ensembl; ENSSSCT00045030324; ENSSSCP00045021014; ENSSSCG00045017747.
DR Ensembl; ENSSSCT00050076822; ENSSSCP00050033094; ENSSSCG00050056308.
DR Ensembl; ENSSSCT00060079326; ENSSSCP00060034315; ENSSSCG00060058178.
DR Ensembl; ENSSSCT00065017932; ENSSSCP00065007312; ENSSSCG00065013486.
DR Ensembl; ENSSSCT00070020016; ENSSSCP00070016635; ENSSSCG00070010275.
DR GeneID; 397117; -.
DR KEGG; ssc:397117; -.
DR CTD; 9446; -.
DR eggNOG; KOG0406; Eukaryota.
DR GeneTree; ENSGT00940000155351; -.
DR HOGENOM; CLU_011226_9_2_1; -.
DR InParanoid; Q9N1F5; -.
DR OMA; ADHYSHR; -.
DR OrthoDB; 1225872at2759; -.
DR TreeFam; TF105325; -.
DR BRENDA; 2.5.1.18; 6170.
DR Reactome; R-SSC-156581; Methylation.
DR Reactome; R-SSC-156590; Glutathione conjugation.
DR Reactome; R-SSC-196836; Vitamin C (ascorbate) metabolism.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000022351; Expressed in liver and 43 other tissues.
DR ExpressionAtlas; Q9N1F5; baseline and differential.
DR Genevisible; Q9N1F5; SS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB.
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; IPR005442; GST_omega.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR PRINTS; PR01625; GSTRNSFRASEO.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
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 Acetylation; Cytoplasm; Direct protein sequencing; Oxidoreductase;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT CHAIN 2..241
FT /note="Glutathione S-transferase omega-1"
FT /id="PRO_0000185886"
FT DOMAIN 22..101
FT /note="GST N-terminal"
FT DOMAIN 106..225
FT /note="GST C-terminal"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 59
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 72
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 85..86
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT CONFLICT 139
FT /note="C -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 27419 MW; AA50EE81C70433A6 CRC64;
MSGGSARSLG KGSAPPGPVP EGLIRVYSMR FCPFAQRTLL VLNAKGIRHQ VININLKNKP
EWFFQKNPSG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMVFELS
SKVPPLLIRF IRRENEADCS GLKEELRKEF SKLEEVLTKK KTTYFGGSSL SMIDYLIWPW
FERLEALELN ECIDHTPKLK LWMAAMMKDP AVSALHIEPR DLRAFNDLYL QNSPEACDYG
L
