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P26697

- GSTA3_CHICK

UniProt

P26697 - GSTA3_CHICK

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Protein

Glutathione S-transferase 3

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91Glutathione

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 229228Glutathione S-transferase 3PRO_0000185800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Ala)

Proteomic databases

PaxDbiP26697.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036177.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Turni14 – 163Combined sources
Helixi17 – 259Combined sources
Beta strandi31 – 344Combined sources
Helixi38 – 4710Combined sources
Beta strandi57 – 604Combined sources
Beta strandi63 – 675Combined sources
Helixi68 – 7811Combined sources
Helixi86 – 10419Combined sources
Turni105 – 1073Combined sources
Helixi109 – 1113Combined sources
Helixi114 – 13017Combined sources
Helixi132 – 14312Combined sources
Beta strandi146 – 1494Combined sources
Helixi155 – 17016Combined sources
Turni172 – 1776Combined sources
Helixi179 – 19012Combined sources
Helixi192 – 1987Combined sources
Helixi210 – 22011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VF1X-ray1.77A1-229[»]
1VF2X-ray2.15A/B1-229[»]
1VF3X-ray2.15A/B1-229[»]
1VF4X-ray2.45A1-229[»]
ProteinModelPortaliP26697.
SMRiP26697. Positions 2-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26697.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminalAdd
BLAST
Domaini85 – 207123GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 552Glutathione binding
Regioni67 – 682Glutathione binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG266414.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
KOiK00799.
PhylomeDBiP26697.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451L → V.
Natural varianti47 – 471S → A.
Natural varianti49 – 491I → F.
Natural varianti49 – 491I → V.
Natural varianti52 – 521F → R.
Natural varianti129 – 1302TS → AN.
Natural varianti135 – 1362AY → VF.
Natural varianti155 – 1551W → R.
Natural varianti158 – 1592IH → VV.
Natural varianti163 – 1631A → T.
Natural varianti166 – 1661M → A.
Natural varianti168 – 1681E → V.

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38219 mRNA. Translation: AAA62731.1 .
PIRi S19734.
RefSeqi NP_990743.1. NM_205412.1.
UniGenei Gga.788.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VF1 X-ray 1.77 A 1-229 [» ]
1VF2 X-ray 2.15 A/B 1-229 [» ]
1VF3 X-ray 2.15 A/B 1-229 [» ]
1VF4 X-ray 2.45 A 1-229 [» ]
ProteinModelPortali P26697.
SMRi P26697. Positions 2-228.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000036177.

Proteomic databases

PaxDbi P26697.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396380.
KEGGi gga:396380.

Phylogenomic databases

eggNOGi NOG266414.
HOGENOMi HOG000115734.
HOVERGENi HBG053749.
KOi K00799.
PhylomeDBi P26697.

Enzyme and pathway databases

SABIO-RK P26697.

Miscellaneous databases

EvolutionaryTracei P26697.
NextBioi 20816422.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01266. GSTRNSFRASEA.
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. "Cloning and expression of a chick liver glutathione S-transferase CL 3 subunit with the use of a baculovirus expression system."
    Chang L.-H., Fan J.-Y., Liu L.-F., Tsai S.-P., Tam M.F.
    Biochem. J. 281:545-551(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: White leghorn.
    Tissue: Liver.

Entry informationi

Entry nameiGSTA3_CHICK
AccessioniPrimary (citable) accession number: P26697
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3