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PLAAT3 - phospholipase A and acyltransferase 3 (human)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-26
Description
Enables N-acyltransferase activity; lipid binding activity; and phospholipase activity. Involved in N-acylphosphatidylethanolamine metabolic process. Predicted to be located in several cellular components, including lysosome; nuclear envelope; and peroxisome. Predicted to be active in cytoplasm. Biomarker of seminoma.

1 Names and Identifiers

1.1 Synonyms

  • AdPLA
  • FPLD9
  • H-REV107
  • H-REV107-1
  • HRASLS3
  • HREV107
  • HREV107-1
  • HREV107-3
  • HRSL3
  • PLA2G16
  • PLAAT-3
  • Ca-independent phospholipase A1/2
  • H-rev 107 protein homolog
  • HRAS-like suppressor 1
  • HRAS-like suppressor 3
  • adipose-specific PLA2
  • adipose-specific phospholipase A2
  • group XVI phospholipase A1/A2
  • group XVI phospholipase A2
  • phospholipase A/acyltransferase-3
  • phospholipase A2 group XVI
  • renal carcinoma antigen NY-REN-65

1.2 Other Identifiers

1.2.1 HGNC ID

1.2.2 Ensembl ID

1.2.3 Alliance Gene ID

1.2.4 Bgee Gene ID

1.2.5 Enzyme Commission (EC) Number

1.2.6 GlyCosmos Gene

1.2.7 KEGG Gene

1.2.8 MIM Number

1.2.9 Open Targets ID

1.2.10 PharmGKB ID

1.2.11 Pharos Target

1.2.12 VEuPathDB ID

1.2.13 Wikidata

3 Proteins

3.1 Protein Function

Exhibits both phospholipase A1/2 and acyltransferase activities (PMID: 19047760, PMID: 19615464, PMID: 22605381, PMID: 22825852, PMID: 26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PMID: 19047760, PMID: 19615464, PMID: 22605381, PMID: 22825852, PMID: 22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PMID: 19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PMID: 19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PMID: 19047760, PMID: 19615464, PMID: 22605381, PMID: 22825852). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PMID: 22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).

(Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PMID: 28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PMID: 28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PMID: 28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PMID: 28077878). The lipid-modifying enzyme activity is required for this process (PMID: 28077878).

3.2 Protein 3D Structures

3.2.1 PDB Structures

3.2.2 NCBI Protein Structures

3.2.3 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 Chemicals and Bioactivities

4.1 Tested Compounds

5 BioAssays

5.1 Small-Molecule BioAssays

5.2 RNAi BioAssays

6 Diseases and Phenotypes

6.1 KEGG Diseases

6.2 OMIM Phenotypes

6.3 MedGen Diseases

6.4 Gene-Disease Associations

7 Interactions and Pathways

7.1 Chemical-Gene Interactions

7.2 Interactions

7.3 Pathways

8 Biochemical Reactions

9 Expression

10 Target Development Level

11 Literature

11.1 Consolidated References

11.2 Gene-Chemical Co-Occurrences in Literature

11.3 Gene-Gene Co-Occurrences in Literature

11.4 Gene-Disease Co-Occurrences in Literature

12 Patents

13 Classification

13.1 Gene Family

13.2 Gene Ontology: Biological Process

13.3 Gene Ontology: Cellular Component

13.4 Gene Ontology: Molecular Function

13.5 ChEMBL Target Tree

13.6 Enzyme Classification

14 Information Sources

  1. NCBI Gene
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    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Alliance of Genome Resources
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    https://www.alliancegenome.org/privacy-warranty-licensing
  4. BioGRID
    LICENSE
    The MIT License (MIT); Copyright Mike Tyers Lab
    https://wiki.thebiogrid.org/doku.php/terms_and_conditions
  5. STRING: functional protein association networks
  6. Comparative Toxicogenomics Database (CTD)
    LICENSE
    It is to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of NC State University.
    http://ctdbase.org/about/legal.jsp
  7. GlyCosmos Glycoscience Portal
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    https://glycosmos.org/license
  8. HUGO Gene Nomenclature Committee (HGNC)
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    No restrictions are imposed on access to, or use of, the data provided by the HGNC, which are provided to enhance knowledge and encourage progress in the scientific community.
    https://www.genenames.org/about/
  9. KEGG
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    https://www.kegg.jp/kegg/legal.html
  10. NCBI Gene Expression Omnibus (GEO)
  11. NCBI MedGen
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    https://www.ncbi.nlm.nih.gov/home/about/policies/
  12. NCBI Structure
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    https://www.ncbi.nlm.nih.gov/home/about/policies/
  13. Online Mendelian Inheritance in Man (OMIM)
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    https://omim.org/help/copyright
  14. Open Targets
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    https://platform-docs.opentargets.org/licence
  15. PharmGKB
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    https://www.pharmgkb.org/page/policies
  16. Pharos
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    Data accessed from Pharos and TCRD is publicly available from the primary sources listed above. Please respect their individual licenses regarding proper use and redistribution.
    https://pharos.nih.gov/about
  17. RCSB Protein Data Bank (RCSB PDB)
    LICENSE
    Data files contained in the PDB archive (ftp://ftp.wwpdb.org) are free of all copyright restrictions and made fully and freely available for both non-commercial and commercial use. Users of the data should attribute the original authors of that structural data.
    https://www.rcsb.org/pages/policies
  18. Swiss Institute of Bioinformatics Bgee
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    Creative Commons Zero license (CC0)
    https://www.bgee.org/about/
  19. UniProt
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    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
  20. VEuPathDB: The Eukaryotic Pathogen, Vector and Host Informatics Resource
    LICENSE
    All data on VEuPathDB websites are provided freely for public use.
    https://veupathdb.org/veupathdb/app/static-content/about.html
  21. Wikidata
  22. ChEMBL
    LICENSE
    Access to the web interface of ChEMBL is made under the EBI's Terms of Use (http://www.ebi.ac.uk/Information/termsofuse.html). The ChEMBL data is made available on a Creative Commons Attribution-Share Alike 3.0 Unported License (http://creativecommons.org/licenses/by-sa/3.0/).
    http://www.ebi.ac.uk/Information/termsofuse.html
  23. Swiss Institute of Bioinformatics ENZYME
    LICENSE
    Copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution (CC BY 4.0) License (https://creativecommons.org/licenses/by/4.0/).
    https://enzyme.expasy.org/enzyme.get
    Enzyme Classification
    https://enzyme.expasy.org/
  24. Gene Ontology (GO)
    LICENSE
    Gene Ontology Consortium data and data products are licensed under the Creative Commons Attribution 4.0 Unported License (https://creativecommons.org/licenses/by/4.0/legalcode)
    http://geneontology.org/docs/go-citation-policy/
  25. 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
  26. 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
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