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Q9N1F5 (GSTO1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase omega-1

Short name=GSTO-1
EC=2.5.1.18
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
Short name=MMA(V) reductase
EC=1.20.4.2
S-(Phenacyl)glutathione reductase
Short name=SPG-R
Gene names
Name:GSTO1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.

Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.

Subunit structure

Homodimer. Ref.1

Subcellular location

Cytoplasmcytosol Ref.1.

Tissue specificity

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

Sequence similarities

Belongs to the GST superfamily. Omega family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Mass spectrometry

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 241240Glutathione S-transferase omega-1
PRO_0000185886

Regions

Domain22 – 10180GST N-terminal
Domain106 – 225120GST C-terminal
Region85 – 862Glutathione binding By similarity

Sites

Active site321Nucleophile By similarity
Binding site591Glutathione By similarity
Binding site721Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue1431N6-acetyllysine By similarity
Modified residue1481N6-acetyllysine By similarity
Modified residue1521N6-acetyllysine By similarity

Experimental info

Sequence conflict1391C → Y AA sequence Ref.1
Sequence conflict1581T → Q AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9N1F5 [UniParc].

Last modified January 31, 2002. Version 2.
Checksum: AA50EE81C70433A6

FASTA24127,419
        10         20         30         40         50         60 
MSGGSARSLG KGSAPPGPVP EGLIRVYSMR FCPFAQRTLL VLNAKGIRHQ VININLKNKP 

        70         80         90        100        110        120 
EWFFQKNPSG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMVFELS 

       130        140        150        160        170        180 
SKVPPLLIRF IRRENEADCS GLKEELRKEF SKLEEVLTKK KTTYFGGSSL SMIDYLIWPW 

       190        200        210        220        230        240 
FERLEALELN ECIDHTPKLK LWMAAMMKDP AVSALHIEPR DLRAFNDLYL QNSPEACDYG 


L 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF188838 mRNA. Translation: AAF71994.2.
RefSeqNP_999215.1. NM_214050.1.
UniGeneSsc.58505.

3D structure databases

ProteinModelPortalQ9N1F5.
SMRQ9N1F5. Positions 5-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000011310.

Proteomic databases

PaxDbQ9N1F5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000011607; ENSSSCP00000011305; ENSSSCG00000022351.
GeneID397117.
KEGGssc:397117.

Organism-specific databases

CTD9446.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00390000005479.
HOGENOMHOG000006560.
HOVERGENHBG051853.
KOK00799.
OMAQPEIKFS.
OrthoDBEOG71CFNG.
TreeFamTF105325.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSPR01625. GSTRNSFRASEO.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSTO1_PIG
AccessionPrimary (citable) accession number: Q9N1F5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 31, 2002
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families