Version 5.4
Mus musculus Protein: Smpd2
Summary
InnateDB Protein IDBP-146758.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Smpd2
Protein Name sphingomyelin phosphodiesterase 2, neutral
Synonyms AW108287; nSMase; nSMase1;
Species Mus musculus
Ensembl Protein ENSMUSP00000019965
InnateDB Gene IDBG-146756 (Smpd2)
Protein Structure
UniProt Annotation
Function Converts sphingomyelin to ceramide. Hydrolyze 1-acyl-2- lyso-sn-glycero-3-phosphocholine (lyso-PC) and 1-O-alkyl-2-lyso- sn-glycero-3-phosphocholine (lyso-platelet-activating factor). The physiological substrate seems to be Lyso-PAF (By similarity). {ECO:0000250}.
Subcellular Localization Membrane; Multi-pass membrane protein.
Disease Associations
Tissue Specificity Although widely expressed in all tissues examined, except the spleen, high enzymatic activity occurs only in the brain. {ECO:0000269PubMed:9520418}.
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:0004767 sphingomyelin phosphodiesterase activity
GO:0046872 metal ion binding
Biological Process
GO:0009612 response to mechanical stimulus
GO:0035556 intracellular signal transduction
GO:0046513 ceramide biosynthetic process
Cellular Component
GO:0005901 caveola
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1278330
InterPro IPR005135 Endonuclease/exonuclease/phosphatase
PFAM PF03372
PF14529
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O70572
PhosphoSite PhosphoSite-O70572
TrEMBL
UniProt Splice Variant
Entrez Gene 20598
UniGene Mm.452529
RefSeq NP_033239
MGI ID
MGI Symbol Smpd2
OMIM
CCDS CCDS23805
HPRD
IMGT
EMBL AJ222800 BC010978
GenPept AAH10978 CAA10994

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