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Protein

Glutathione S-transferase 3

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conjugation of GSH to a wide variety of electrophilic alkylating agents. Also involved in the metabolism of lipid hydroperoxides, prostaglandins and leukotriene A4 and in binding of non-substrate hydrophobic ligands such as bile acids, a number of drugs and thyroid hormones. This GST does not exhibit peroxidase activity.

Miscellaneous

The variations were found from AA sequencing and imply there are multiple forms of CL-3.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei9GlutathioneCombined sources1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

SABIO-RKP26697

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 3 (EC:2.5.1.18)
Alternative name(s):
GST class-alpha
GST-CL3
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001858002 – 229Glutathione S-transferase 3Add BLAST228

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2Blocked amino end (Ala)1

Proteomic databases

PaxDbiP26697
PRIDEiP26697

Interactioni

Subunit structurei

Homodimer or heterodimer (with a subunit from group CL-4).

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036177

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 9Combined sources4
Turni14 – 16Combined sources3
Helixi17 – 25Combined sources9
Beta strandi31 – 34Combined sources4
Helixi38 – 47Combined sources10
Beta strandi57 – 60Combined sources4
Beta strandi63 – 67Combined sources5
Helixi68 – 78Combined sources11
Helixi86 – 104Combined sources19
Turni105 – 107Combined sources3
Helixi109 – 111Combined sources3
Helixi114 – 130Combined sources17
Helixi132 – 143Combined sources12
Beta strandi146 – 149Combined sources4
Helixi155 – 170Combined sources16
Turni172 – 177Combined sources6
Helixi179 – 190Combined sources12
Helixi192 – 198Combined sources7
Helixi210 – 220Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VF1X-ray1.77A1-229[»]
1VF2X-ray2.15A/B1-229[»]
1VF3X-ray2.15A/B1-229[»]
1VF4X-ray2.45A1-229[»]
ProteinModelPortaliP26697
SMRiP26697
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26697

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 83GST N-terminalAdd BLAST81
Domaini85 – 207GST C-terminalAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 55Glutathione bindingCombined sources2
Regioni67 – 68Glutathione bindingCombined sources2

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.Curated

Phylogenomic databases

eggNOGiKOG1695 Eukaryota
ENOG4111VAU LUCA
HOGENOMiHOG000115734
HOVERGENiHBG053749
KOiK00799
PhylomeDBiP26697

Family and domain databases

InterProiView protein in InterPro
IPR010987 Glutathione-S-Trfase_C-like
IPR036282 Glutathione-S-Trfase_C_sf
IPR004045 Glutathione_S-Trfase_N
IPR003080 GST_alpha
IPR004046 GST_C
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF14497 GST_C_3, 1 hit
PF02798 GST_N, 1 hit
PRINTSiPR01266 GSTRNSFRASEA
SUPFAMiSSF47616 SSF47616, 1 hit
SSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS50405 GST_CTER, 1 hit
PS50404 GST_NTER, 1 hit

Sequencei

Sequence statusi: Complete.

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

P26697-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKPVLYYF NGRGKMESIR WLLAAAGVEF EEVFLETREQ YEKLLQSGIL
60 70 80 90 100
MFQQVPMVEI DGMKLVQTRA ILNYIAGKYN LYGKDLKERA LIDMYVGGTD
110 120 130 140 150
DLMGFLLSFP FLSAEDKVKQ CAFVVEKATS RYFPAYEKVL KDHGQDFLVG
160 170 180 190 200
NRLSWADIHL LEAILMVEEK KSDALSGFPL LQAFKKRISS IPTIKKFLAP
210 220
GSKRKPISDD KYVETVRRVL RMYYDVKPH
Length:229
Mass (Da):26,326
Last modified:January 23, 2007 - v2
Checksum:iEA30D949034BD8DB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti45L → V. 1
Natural varianti47S → A. 1
Natural varianti49I → F. 1
Natural varianti49I → V. 1
Natural varianti52F → R. 1
Natural varianti129 – 130TS → AN. 2
Natural varianti135 – 136AY → VF. 2
Natural varianti155W → R. 1
Natural varianti158 – 159IH → VV. 2
Natural varianti163A → T. 1
Natural varianti166M → A. 1
Natural varianti168E → V. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38219 mRNA Translation: AAA62731.1
PIRiS19734
RefSeqiNP_990743.1, NM_205412.1
UniGeneiGga.788

Genome annotation databases

GeneIDi396380
KEGGigga:396380

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiGSTA3_CHICK
AccessioniPrimary (citable) accession number: P26697
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 117 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health