Version 5.4
Mus musculus Protein: Ppapdc2
Summary
InnateDB Protein IDBP-156686.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ppapdc2
Protein Name phosphatidic acid phosphatase type 2 domain containing 2
Synonyms 4932443D16Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000047776
InnateDB Gene IDBG-156684 (Ppapdc2)
Protein Structure
UniProt Annotation
Function Phosphatase that dephosphorylates presqualene diphosphate (PSDP) into presqualene monophosphate (PSMP), suggesting that it may be indirectly involved in innate immunity. PSDP is a bioactive lipid that rapidly remodels to presqualene monophosphate PSMP upon cell activation. Displays diphosphate phosphatase activity with a substrate preference for PSDP > FDP > phosphatidic acid (By similarity). {ECO:0000250}.
Subcellular Localization Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
Biological Process
GO:0008150 biological_process
GO:0008152 metabolic process
Cellular Component
GO:0005575 cellular_component
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1921661
InterPro IPR000326 Phosphatidic acid phosphatase type 2/haloperoxidase
PFAM PF01569
PRINTS
PIRSF
SMART SM00014
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9D4F2
PhosphoSite PhosphoSite-Q9D4F2
TrEMBL
UniProt Splice Variant
Entrez Gene 74411
UniGene Mm.441887
RefSeq NP_083198
MGI ID
MGI Symbol Ppapdc2
OMIM
CCDS CCDS29728
HPRD
IMGT
EMBL AK016572 BC052412
GenPept AAH52412 BAB30313

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