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P26697

- GSTA3_CHICK

UniProt

P26697 - GSTA3_CHICK

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
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 – 94
    Turni14 – 163
    Helixi17 – 259
    Beta strandi31 – 344
    Helixi38 – 4710
    Beta strandi57 – 604
    Beta strandi63 – 675
    Helixi68 – 7811
    Helixi86 – 10419
    Turni105 – 1073
    Helixi109 – 1113
    Helixi114 – 13017
    Helixi132 – 14312
    Beta strandi146 – 1494
    Helixi155 – 17016
    Turni172 – 1776
    Helixi179 – 19012
    Helixi192 – 1987
    Helixi210 – 22011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    InParanoidiP26697.
    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

    MAAKPVLYYF NGRGKMESIR WLLAAAGVEF EEVFLETREQ YEKLLQSGIL    50
    MFQQVPMVEI DGMKLVQTRA ILNYIAGKYN LYGKDLKERA LIDMYVGGTD 100
    DLMGFLLSFP FLSAEDKVKQ CAFVVEKATS RYFPAYEKVL KDHGQDFLVG 150
    NRLSWADIHL LEAILMVEEK KSDALSGFPL LQAFKKRISS IPTIKKFLAP 200
    GSKRKPISDD KYVETVRRVL RMYYDVKPH 229
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    InParanoidi P26697.
    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: October 1, 2014
    This is version 99 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