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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: 3 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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Glutathione1 Publication
Binding sitei13 – 131Glutathione1 Publication
Binding sitei38 – 381Glutathione1 Publication
Binding sitei42 – 421GlutathioneBy similarity

GO - Molecular functioni

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

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Glutathione S-transferase PPRO_0000185905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Phosphotyrosine; by EGFRBy similarity
Modified residuei100 – 1001N6-succinyllysineBy similarity
Modified residuei113 – 1131N6-succinyllysineBy similarity
Modified residuei125 – 1251N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP80031.
PRIDEiP80031.

Interactioni

Subunit structurei

Homodimer. Interacts with CDK5 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013714.

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi9 – 113Combined sources
Turni12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi29 – 324Combined sources
Turni35 – 373Combined sources
Helixi38 – 414Combined sources
Helixi42 – 443Combined sources
Beta strandi52 – 554Combined sources
Beta strandi58 – 625Combined sources
Helixi63 – 7412Combined sources
Helixi81 – 10727Combined sources
Helixi109 – 13224Combined sources
Helixi135 – 1373Combined sources
Beta strandi141 – 1455Combined sources
Helixi148 – 16316Combined sources
Helixi167 – 1704Combined sources
Helixi172 – 18211Combined sources
Helixi185 – 1928Combined sources
Helixi194 – 1974Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GSRX-ray2.11A/B1-206[»]
ProteinModelPortaliP80031.
SMRiP80031. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80031.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG05174.
HOGENOMiHOG000115733.
HOVERGENiHBG108324.
InParanoidiP80031.

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

        10         20         30         40         50
PPYTITYFPV RGRCEAMRML LADQDQSWKE EVVTMETWPP LKPSCLFRQL
60 70 80 90 100
PKFQDGDLTL YQSNAILRHL GRSFGLYGKD QKEAALVDMV NDGVEDLRCK
110 120 130 140 150
YATLIYTNYE AGKEKYVKEL PEHLKPFETL LSQNQGGQAF VVGSQISFAD
160 170 180 190 200
YNLLDLLRIH QVLNPSCLDA FPLLSAYVAR LSARPKIKAF LASPEHVNRP

INGNGKN
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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.
InParanoidi P80031.

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: November 26, 2014
This is version 100 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