A0A8M2BC81 · A0A8M2BC81_DANRE
- ProteinN-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Genenapepld
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids415 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
- 1-O-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H2O = 1-O-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineThis reaction proceeds in the forward direction.
- H2O + N,1,2-tri-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(9Z-octadecenoyl) ethanolamineThis reaction proceeds in the forward direction.
- H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-3-phosphate + an N-acylethanolamine + H+This reaction proceeds in the forward direction.
- H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineThis reaction proceeds in the forward direction.
- H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-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.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-butanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-butanoyl ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-decanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-decanoyl ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-dodecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-dodecanoylethanolamineThis reaction proceeds in the forward direction.
- H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamineThis reaction proceeds in the forward direction.
- H2O + N-hexanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-hexanoyl ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-octadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-octadecanoyl ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-octanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+ + N-octanoyl ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-tetradecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+ + N-tetradecanoylethanolamineThis 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 | 205 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 207 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 208 | N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 209 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 210 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 273 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 304 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 304 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 341 | N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 363 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | early endosome membrane | |
Cellular Component | Golgi membrane | |
Cellular Component | membrane-bounded organelle | |
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
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionA0A8M2BC81
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Early endosome membrane ; Peripheral membrane protein
Golgi apparatus membrane ; Peripheral membrane protein
Interaction
Subunit
Homodimer. Bile acids promote the assembly of inactive monomers into an active dimer and enable catalysis.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 164-364 | Metallo-beta-lactamase | ||||
Sequence: VLTDPIFSQRASPVAFMGPKRYRDPPCTIEQLPRLDAVVISHTHYDHLDAASVTALNSRFGSALHWFVPLGLAEWMQKTGCENVTELDWWVGSRIPGHDNVSFFCTPAQHWCKRTPVDDNKTLWGSWSIVGSHSRFFFAGDTGYCASFKEIGRHFGPFDLAAIPIGAYVPRGIMKSQHVDPEEAVQIHIDVQAKASLAIHW |
Sequence similarities
Belongs to the NAPE-PLD family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length415
- Mass (Da)46,185
- Last updated2022-08-03 v1
- Checksum194C8590FD6C03CC
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5TZE8 | Q5TZE8_DANRE | napepld | 416 | ||
A0A2R8RJ40 | A0A2R8RJ40_DANRE | napepld | 364 |
Keywords
- Technical term