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Protein

Glutathione S-transferase omega-1

Gene

GSTO1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid (By similarity).By similarity

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.
Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321NucleophileBy similarity
Binding sitei59 – 591GlutathioneBy similarity
Binding sitei72 – 721Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 6170.
ReactomeiREACT_322613. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase omega-1 (EC:2.5.1.18)
Short name:
GSTO-1
Alternative name(s):
Glutathione S-transferase omega 1-1
Short name:
GSTO 1-1
Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
Monomethylarsonic acid reductase (EC:1.20.4.2)
Short name:
MMA(V) reductase
S-(Phenacyl)glutathione reductase
Short name:
SPG-R
Gene namesi
Name:GSTO1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Chromosome 14

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 241240Glutathione S-transferase omega-1PRO_0000185886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei57 – 571N6-acetyllysineBy similarity
Modified residuei143 – 1431N6-acetyllysineBy similarity
Modified residuei148 – 1481N6-acetyllysineBy similarity
Modified residuei152 – 1521N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9N1F5.

Expressioni

Tissue specificityi

Most abundant in the liver and skeletal muscle; also expressed in heart, diaphragm, colon, thymus, kidney, lung, ovaries, spleen, intestine and pancreas.1 Publication

Gene expression databases

GenevisibleiQ9N1F5. SS.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011305.

Structurei

3D structure databases

ProteinModelPortaliQ9N1F5.
SMRiQ9N1F5. Positions 5-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10180GST N-terminalAdd
BLAST
Domaini106 – 225120GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 862Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Omega family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
HOVERGENiHBG051853.
InParanoidiQ9N1F5.
KOiK00799.
OMAiYLDSFAM.
OrthoDBiEOG71CFNG.
TreeFamiTF105325.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSiPR01625. GSTRNSFRASEO.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9N1F5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGSARSLG KGSAPPGPVP EGLIRVYSMR FCPFAQRTLL VLNAKGIRHQ
60 70 80 90 100
VININLKNKP EWFFQKNPSG LVPVLENSQG QLIYESAITC EYLDEAYPGK
110 120 130 140 150
KLLPDDPYEK ACQKMVFELS SKVPPLLIRF IRRENEADCS GLKEELRKEF
160 170 180 190 200
SKLEEVLTKK KTTYFGGSSL SMIDYLIWPW FERLEALELN ECIDHTPKLK
210 220 230 240
LWMAAMMKDP AVSALHIEPR DLRAFNDLYL QNSPEACDYG L
Length:241
Mass (Da):27,419
Last modified:January 31, 2002 - v2
Checksum:iAA50EE81C70433A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391C → Y AA sequence (PubMed:11485575).Curated
Sequence conflicti158 – 1581T → Q AA sequence (PubMed:11485575).Curated

Mass spectrometryi

Molecular mass is 27328±3 Da from positions 2 - 241. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188838 mRNA. Translation: AAF71994.2.
RefSeqiNP_999215.1. NM_214050.1.
UniGeneiSsc.58505.

Genome annotation databases

EnsembliENSSSCT00000011607; ENSSSCP00000011305; ENSSSCG00000022351.
GeneIDi397117.
KEGGissc:397117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188838 mRNA. Translation: AAF71994.2.
RefSeqiNP_999215.1. NM_214050.1.
UniGeneiSsc.58505.

3D structure databases

ProteinModelPortaliQ9N1F5.
SMRiQ9N1F5. Positions 5-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011305.

Proteomic databases

PaxDbiQ9N1F5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000011607; ENSSSCP00000011305; ENSSSCG00000022351.
GeneIDi397117.
KEGGissc:397117.

Organism-specific databases

CTDi9446.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
HOVERGENiHBG051853.
InParanoidiQ9N1F5.
KOiK00799.
OMAiYLDSFAM.
OrthoDBiEOG71CFNG.
TreeFamiTF105325.

Enzyme and pathway databases

BRENDAi2.5.1.18. 6170.
ReactomeiREACT_322613. Glutathione conjugation.

Gene expression databases

GenevisibleiQ9N1F5. SS.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSiPR01625. GSTRNSFRASEO.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Purification and characterization of a glutathione S-transferase Omega in pig: evidence for two distinct organ-specific transcripts."
    Rouimi P., Anglade P., Benzekri A., Costet P., Debrauwer L., Pineau T., Tulliez J.
    Biochem. J. 358:257-262(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-31; 58-83; 101-110; 115-147; 149-160; 162-190; 201-228 AND 235-241, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY.
    Tissue: Liver.

Entry informationi

Entry nameiGSTO1_PIG
AccessioniPrimary (citable) accession number: Q9N1F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 31, 2002
Last modified: July 22, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.