A0A7J7TME8 · A0A7J7TME8_RHIFE
- ProteinN-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids371 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid. Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain. May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation. As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs.
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 + N-hexadecanoylethanolamine + H+This reaction proceeds in the forward direction.
- N,1,2-tri-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-(9Z-octadecenoyl) ethanolamine + 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N,1-diacyl-sn-glycero-3-phosphoethanolamine + H2O = an N-acylethanolamine + a 1-acyl-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + N-hexadecanoylethanolamine + H+This reaction proceeds in the forward direction.
- N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = N-hexadecanoylethanolamine + 1-hexadecanoyl-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + a 1,2-diacyl-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-butanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-butanoyl ethanolamine + 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-decanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-decanoyl ethanolamine + 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-dodecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-dodecanoylethanolamine + 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-hexadecanoylethanolamine + 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-hexanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-hexanoyl ethanolamine + 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-octadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-octadecanoyl ethanolamine + 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-octanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-octanoyl ethanolamine + 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H+This reaction proceeds in the forward direction.
- N-tetradecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-tetradecanoylethanolamine + 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H+This 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 | 185 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 187 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 188 | an N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 189 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 190 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 253 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 256 | deoxycholate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 260 | deoxycholate (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 284 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 284 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 321 | an N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 343 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 348 | deoxycholate (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | early endosome membrane | |
Cellular Component | Golgi membrane | |
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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yinpterochiroptera > Rhinolophoidea > Rhinolophidae > Rhinolophinae > Rhinolophus
Accessions
- Primary accessionA0A7J7TME8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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 compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-39 | Polar residues | ||||
Sequence: MDENESNQSLMTSSQYPKEAVRKRQNSARNSGGSDSSRL | ||||||
Region | 1-40 | Disordered | ||||
Sequence: MDENESNQSLMTSSQYPKEAVRKRQNSARNSGGSDSSRLS | ||||||
Domain | 144-344 | Metallo-beta-lactamase | ||||
Sequence: FLTDPIFSSRASPSQYMGPKRFRRPPCTISELPLIDAVLISHNHYDHLDYHSVVALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHIDVQTRKSVAIHW |
Sequence similarities
Belongs to the NAPE-PLD family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length371
- Mass (Da)42,849
- Last updated2021-04-07 v1
- ChecksumF7A5EF8F230A521B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-39 | Polar residues | ||||
Sequence: MDENESNQSLMTSSQYPKEAVRKRQNSARNSGGSDSSRL |