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P80031

- GSTP1_PIG

UniProt

P80031 - GSTP1_PIG

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Protein
Glutathione S-transferase P
Gene
GSTP1
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Glutathione
Binding sitei13 – 131Glutathione
Binding sitei38 – 381Glutathione
Binding sitei42 – 421Glutathione By similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    SABIO-RKP80031.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase P (EC:2.5.1.18)
    Alternative name(s):
    GST P1-1
    GST class-pi
    Gene namesi
    Name:GSTP1
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity
    Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization By similarity.

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 207207Glutathione S-transferase P
    PRO_0000185905Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Phosphotyrosine; by EGFR By similarity
    Modified residuei100 – 1001N6-succinyllysine By similarity
    Modified residuei113 – 1131N6-succinyllysine By similarity
    Modified residuei125 – 1251N6-acetyllysine By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP80031.
    PRIDEiP80031.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CDK5 By similarity.2 Publications

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000013714.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75
    Beta strandi9 – 113
    Turni12 – 143
    Helixi15 – 239
    Beta strandi29 – 324
    Turni35 – 373
    Helixi38 – 414
    Helixi42 – 443
    Beta strandi52 – 554
    Beta strandi58 – 625
    Helixi63 – 7412
    Helixi81 – 10727
    Helixi109 – 13224
    Helixi135 – 1373
    Beta strandi141 – 1455
    Helixi148 – 16316
    Helixi167 – 1704
    Helixi172 – 18211
    Helixi185 – 1928
    Helixi194 – 1974

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GSRX-ray2.11A/B1-206[»]
    ProteinModelPortaliP80031.
    SMRiP80031. Positions 1-206.

    Miscellaneous databases

    EvolutionaryTraceiP80031.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7878GST N-terminal
    Add
    BLAST
    Domaini80 – 201122GST C-terminal
    Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 502Glutathione binding
    Regioni62 – 632Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Pi family.

    Phylogenomic databases

    eggNOGiNOG05174.
    HOGENOMiHOG000115733.
    HOVERGENiHBG108324.

    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.
    IPR003082. GST_pi.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01268. GSTRNSFRASEP.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P80031-1 [UniParc]FASTAAdd to Basket

    « Hide

    PPYTITYFPV RGRCEAMRML LADQDQSWKE EVVTMETWPP LKPSCLFRQL    50
    PKFQDGDLTL YQSNAILRHL GRSFGLYGKD QKEAALVDMV NDGVEDLRCK 100
    YATLIYTNYE AGKEKYVKEL PEHLKPFETL LSQNQGGQAF VVGSQISFAD 150
    YNLLDLLRIH QVLNPSCLDA FPLLSAYVAR LSARPKIKAF LASPEHVNRP 200
    INGNGKN 207
    Length:207
    Mass (Da):23,497
    Last modified:June 1, 1994 - v2
    Checksum:i2B638B60504BF4A0
    GO

    Sequence databases

    PIRiS13780.

    Cross-referencesi

    Sequence databases

    PIRi S13780.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GSR X-ray 2.11 A/B 1-206 [» ]
    ProteinModelPortali P80031.
    SMRi P80031. Positions 1-206.
    ModBasei Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000013714.

    Proteomic databases

    PaxDbi P80031.
    PRIDEi P80031.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG05174.
    HOGENOMi HOG000115733.
    HOVERGENi HBG108324.

    Enzyme and pathway databases

    SABIO-RK P80031.

    Miscellaneous databases

    EvolutionaryTracei P80031.

    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.
    IPR003082. GST_pi.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01268. GSTRNSFRASEP.
    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. "Class pi glutathione S-transferase from pig lung. Purification, biochemical characterization, primary structure and crystallization."
      Dirr H.W., Mann K., Huber R., Ladenstein R., Reinemer P.
      Eur. J. Biochem. 196:693-698(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Lung.
    2. Cited for: PROTEIN SEQUENCE OF 1-15.
      Tissue: Lens.
    3. "The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3-A resolution."
      Reinemer P., Dirr H.W., Ladenstein R., Schaeffer J., Gallay O., Huber R.
      EMBO J. 10:1997-2005(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE SULFONATE, SUBUNIT.
    4. "Refined crystal structure of porcine class Pi glutathione S-transferase (pGST P1-1) at 2.1-A resolution."
      Dirr H.W., Reinemer P., Huber R.
      J. Mol. Biol. 243:72-92(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

    Entry informationi

    Entry nameiGSTP1_PIG
    AccessioniPrimary (citable) accession number: P80031
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: June 1, 1994
    Last modified: March 19, 2014
    This is version 97 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

    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

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