Q965X7 · NAPE1_CAEEL
- ProteinN-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 1
- Genenape-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids356 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (PubMed:25423491).
NAEs are bioactive lipids that are involved in diverse physiological processes such as growth and lifespan (PubMed:21562563, PubMed:25423491).
NAEs are bioactive lipids that are involved in diverse physiological processes such as growth and lifespan (PubMed:21562563, PubMed:25423491).
Catalytic activity
- H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate + an N-acylethanolamine + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(N-hexadecanoyl)-ethanolamine + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineThis reaction proceeds in the forward direction.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamineThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 zinc divalent cations per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 144 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 146 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 147 | N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 148 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 149 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 217 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 248 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 286 | N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 308 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane-bounded organelle | |
Cellular Component | neuronal cell body | |
Molecular Function | N-acylphosphatidylethanolamine-specific phospholipase D activity | |
Molecular Function | zinc ion binding | |
Biological Process | N-acylethanolamine metabolic process | |
Biological Process | N-acylphosphatidylethanolamine metabolic process | |
Biological Process | phospholipid catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameN-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 1
- EC number
- Short namesNAPE-1
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ965X7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
No strong phenotype in the nape-1 deletion mutant, however its overexpression alters growth and lifespan when grown at 25 degrees Celsius compared to 15 degrees Celsius.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452742 | 1-356 | N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 1 | |||
Sequence: MSLPTTSSPLTNDQEFAKPVRNGKIFENPKSFTNWGGRPGLTNIFKLVLRETSHENLPSDKKVLDSTLPVHNITADDFHSESGLFATWLGHATVLVDLEGVKFVTDPVWADRASFTSFAGPKRYRPPPMKLEDLPDLDFAVVSHDHYDHLDADAVKRITNLNPQIKWFVPLGLKKWMKNQGIGADGSNTVTELNWGESSEFVKNGKTITIWCLPAQHSGQRGLSDHNHRLWSGWAVIGENRRFYFPGDTGFCDVEFKKIGEKLGPFDLAAIPIGAYEPRWFMKSHHINPDEAVEVHKLVRARNSIGIHWGTYPMGTTEYYLEPRDKLKELMDAREDLKDTSFVTVDMGEIWEASDR |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length356
- Mass (Da)40,319
- Last updated2001-12-01 v1
- ChecksumF3EE650FAEE98103
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284604 EMBL· GenBank· DDBJ | CCD74042.1 EMBL· GenBank· DDBJ | Genomic DNA |