An official website of the United States government

Ggt5 - gamma-glutamyltransferase 5 (Norway rat)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-15
Description
Predicted to enable glutathione hydrolase activity; leukotriene-C(4) hydrolase; and peptidyltransferase activity. Predicted to be involved in several processes, including carboxylic acid metabolic process; glutathione catabolic process; and inflammatory response. Predicted to be active in plasma membrane. Orthologous to human GGT5 (gamma-glutamyltransferase 5).

1 Names and Identifiers

1.1 Synonyms

  • Ggta1
  • Ggtla1
  • glutathione hydrolase 5 proenzyme
  • GGL
  • GGT 5
  • GGT-rel
  • gamma-glutamyl leukotrienase
  • gamma-glutamyl transpeptidase-related enzyme
  • gamma-glutamyltransferase-like activity 1
  • gamma-glutamyltranspeptidase 5
  • leukotriene-C4 hydrolase

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Enzyme Commission (EC) Number

1.2.4 RGD ID

1.2.5 Wikidata

3 Proteins

3.1 Protein Function

Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione-S-conjugate. Converts leukotriene C4 (LTC4), a glutathione-S-conjugate, to leukotriene D4 (LTD4). Does not cleave gamma-glutamyl compounds such as gamma-glutamyl leucine. May also catalyze a transpeptidation reaction in addition to the hydrolysis reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Acts as a negative regulator of geranylgeranyl glutathione bioactivity by cleaving off its gamma-glutamyl group, playing a role in adaptive immune responses.

3.2 Protein 3D Structures

3.2.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

3.3 Protein Targets

4 Interactions and Pathways

4.1 Interactions

4.2 Pathways

5 Biochemical Reactions

6 Expression

7 Literature

7.1 Gene-Chemical Co-Occurrences in Literature

7.2 Gene-Gene Co-Occurrences in Literature

7.3 Gene-Disease Co-Occurrences in Literature

8 Patents

8.1 Gene-Chemical Co-Occurrences in Patents

8.2 Gene-Gene Co-Occurrences in Patents

8.3 Gene-Disease Co-Occurrences in Patents

9 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Alliance of Genome Resources
    LICENSE
    All annotations and data produced by Alliance members that are accessible from alliancegenome.org are distributed under a CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
    https://www.alliancegenome.org/privacy-warranty-licensing
  4. NCBI Gene Expression Omnibus (GEO)
  5. Rat Genome Database (RGD)
    LICENSE
    Creative Commons Attribution 4.0 International license (CC BY 4.0)
    https://creativecommons.org/licenses/by/4.0/
  6. STRING: functional protein association networks
  7. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  8. Wikidata
  9. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
  10. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
CONTENTS