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P80031 (GSTP1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutathione S-transferase P
EC=2.5.1.18
Alternative name(s):
GST P1-1
GST class-pi
Gene names
Name:GSTP1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

Homodimer. Interacts with CDK5 By similarity. Ref.3 Ref.4

Subcellular location

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 motochondrial localization By similarity.

Sequence similarities

Belongs to the GST superfamily. Pi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Molecular functionTransferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Glutathione S-transferase P
PRO_0000185905

Regions

Domain1 – 7878GST N-terminal
Domain80 – 201122GST C-terminal
Region49 – 502Glutathione binding
Region62 – 632Glutathione binding

Sites

Binding site71Glutathione
Binding site131Glutathione
Binding site381Glutathione
Binding site421Glutathione By similarity

Amino acid modifications

Modified residue31Phosphotyrosine; by EGFR By similarity
Modified residue1061Phosphotyrosine By similarity
Modified residue1251N6-acetyllysine By similarity

Secondary structure

1 .................................... 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80031 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 2B638B60504BF4A0

FASTA20723,497
        10         20         30         40         50         60 
PPYTITYFPV RGRCEAMRML LADQDQSWKE EVVTMETWPP LKPSCLFRQL PKFQDGDLTL 

        70         80         90        100        110        120 
YQSNAILRHL GRSFGLYGKD QKEAALVDMV NDGVEDLRCK YATLIYTNYE AGKEKYVKEL 

       130        140        150        160        170        180 
PEHLKPFETL LSQNQGGQAF VVGSQISFAD YNLLDLLRIH QVLNPSCLDA FPLLSAYVAR 

       190        200 
LSARPKIKAF LASPEHVNRP INGNGKN

« Hide

References

[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]"Pig lens glutathione S-transferase belongs to class Pi enzyme."
Nishinaka T., Fujioka M., Nanjo H., Nishikawa J., Mizoguchi T., Terada T., Nishihara T.
Biochem. Biophys. Res. Commun. 176:966-971(1991) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

PIRS13780.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GSRX-ray2.11A/B1-206[»]
ProteinModelPortalP80031.
SMRP80031. Positions 1-206.
ModBaseSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000013714.

Proteomic databases

PaxDbP80031.
PRIDEP80031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG05174.
HOGENOMHOG000115733.
HOVERGENHBG108324.
OrthoDBEOG48SGTZ.

Enzyme and pathway databases

SABIO-RKP80031.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01268. GSTRNSFRASEP.
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80031.

Entry information

Entry nameGSTP1_PIG
AccessionPrimary (citable) accession number: P80031
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 1, 1994
Last modified: April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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