Version 5.4
Mus musculus Protein: Lypla2
Summary
InnateDB Protein IDBP-197545.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Lypla2
Protein Name lysophospholipase 2
Synonyms LysoII;
Species Mus musculus
Ensembl Protein ENSMUSP00000064204
InnateDB Gene IDBG-197543 (Lypla2)
Protein Structure
UniProt Annotation
Function May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Deacylates GAP43 (By similarity). Has lysophospholipase activity. {ECO:0000250, ECO:0000269PubMed:10064901}.
Subcellular Localization Cytoplasm {ECO:0000305}.
Disease Associations
Tissue Specificity Ubiquitous; detected at low levels. {ECO:0000269PubMed:10064901}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
They are also associated with 8 interaction(s) predicted by orthology.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 8 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0016787 hydrolase activity
Biological Process
GO:0006631 fatty acid metabolic process
GO:0008152 metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:1347000
InterPro IPR003140 Phospholipase/carboxylesterase/thioesterase
IPR013094 Alpha/beta hydrolase fold-3
IPR029058 Alpha/Beta hydrolase fold
PFAM PF02230
PF07859
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9WTL7
PhosphoSite PhosphoSite-Q9WTL7
TrEMBL
UniProt Splice Variant
Entrez Gene 26394
UniGene Mm.34302
RefSeq NP_036072
MGI ID
MGI Symbol Lypla2
OMIM
CCDS CCDS18797
HPRD
IMGT
EMBL AB009653 AK003689 AK075590 AK089112 AK167478 BC068120
GenPept AAH68120 BAA76751 BAB22940 BAC35841 BAC40757 BAE39559

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca