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Q9Z339

- GSTO1_RAT

UniProt

Q9Z339 - GSTO1_RAT

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Protein

Glutathione S-transferase omega-1

Gene

Gsto1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

  1. glutathione dehydrogenase (ascorbate) activity Source: RGD
  2. glutathione transferase activity Source: UniProtKB
  3. methylarsonate reductase activity Source: UniProtKB-EC
  4. oxidoreductase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to arsenic-containing substance Source: UniProtKB
  2. L-ascorbic acid biosynthetic process Source: RGD
  3. L-ascorbic acid metabolic process Source: UniProtKB
  4. xenobiotic catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi70952. Gsto1.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: RGD
  2. basement membrane Source: RGD
  3. cell body Source: RGD
  4. cytoplasm Source: RGD
  5. cytosol Source: RGD
  6. myelin sheath Source: RGD
  7. nuclear membrane Source: RGD
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_0000185887Add
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

PaxDbiQ9Z339.
PRIDEiQ9Z339.

2D gel databases

World-2DPAGE0004:Q9Z339.

PTM databases

PhosphoSiteiQ9Z339.

Expressioni

Gene expression databases

GenevestigatoriQ9Z339.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

MINTiMINT-4569802.

Structurei

3D structure databases

ProteinModelPortaliQ9Z339.
SMRiQ9Z339. Positions 5-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10180GST N-terminalAdd
BLAST
Domaini106 – 228123GST 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.
HOGENOMiHOG000006560.
HOVERGENiHBG051853.
InParanoidiQ9Z339.
PhylomeDBiQ9Z339.

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.

Q9Z339-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGASARSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE
60 70 80 90 100
IININLKNKP EWFFEKNPFG LVPVLENTQG HLITESVITC EYLDEAYPEK
110 120 130 140 150
KLFPDDPYEK ACQKMTFELF SKVPSLVTSF IRAKRKEDHP GIKEELKKEF
160 170 180 190 200
SKLEEAMANK RTAFFGGNSL SMIDYLIWPW FQRLEALELN ECIDHTPKLK
210 220 230 240
LWMATMQEDP VASSHFIDAK TYRDYLSLYL QDSPEACDYG L
Length:241
Mass (Da):27,669
Last modified:January 24, 2001 - v2
Checksum:i31EAC5A7CAF22BC6
GO

Sequence cautioni

The sequence BAA34217.1 differs from that shown. Reason: Frameshift at position 23. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008807 mRNA. Translation: BAA34217.1. Frameshift.
UniGeneiRn.25166.

Genome annotation databases

UCSCiRGD:70952. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008807 mRNA. Translation: BAA34217.1 . Frameshift.
UniGenei Rn.25166.

3D structure databases

ProteinModelPortali Q9Z339.
SMRi Q9Z339. Positions 5-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4569802.

PTM databases

PhosphoSitei Q9Z339.

2D gel databases

World-2DPAGE 0004:Q9Z339.

Proteomic databases

PaxDbi Q9Z339.
PRIDEi Q9Z339.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:70952. rat.

Organism-specific databases

RGDi 70952. Gsto1.

Phylogenomic databases

eggNOGi COG0625.
HOGENOMi HOG000006560.
HOVERGENi HBG051853.
InParanoidi Q9Z339.
PhylomeDBi Q9Z339.

Miscellaneous databases

PROi Q9Z339.

Gene expression databases

Genevestigatori Q9Z339.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view ]
PRINTSi PR01625. GSTRNSFRASEO.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase."
    Ishikawa T., Casini A.F., Nishikimi M.
    J. Biol. Chem. 273:28708-28712(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. Lubec G., Diao W., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 38-43 AND 123-132, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Hippocampus.
  3. "Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver."
    Maellaro E., Del Bello B., Sugherini L., Santucci A., Comporti M., Casini A.F.
    Biochem. J. 301:471-476(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Liver.

Entry informationi

Entry nameiGSTO1_RAT
AccessioniPrimary (citable) accession number: Q9Z339
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: October 1, 2014
This is version 104 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