A0A8M2BC81 · A0A8M2BC81_DANRE

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-hexadecanoylethanolamine
    This 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) ethanolamine
    This 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-hexadecanoylethanolamine
    This reaction proceeds in the forward direction.
  • H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-hexadecanoyl-sn-glycero-3-phosphate + H+ + N-hexadecanoylethanolamine
    This 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)-ethanolamine
    This 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)-ethanolamine
    This 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)-ethanolamine
    This 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 ethanolamine
    This 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 ethanolamine
    This 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-dodecanoylethanolamine
    This 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-hexadecanoylethanolamine
    This 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 ethanolamine
    This 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 ethanolamine
    This 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 ethanolamine
    This 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-tetradecanoylethanolamine
    This reaction proceeds in the forward direction.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 zinc divalent cations per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site205Zn2+ 1 (UniProtKB | ChEBI)
Binding site207Zn2+ 1 (UniProtKB | ChEBI)
Binding site208N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI)
Binding site209Zn2+ 2 (UniProtKB | ChEBI)
Binding site210Zn2+ 2 (UniProtKB | ChEBI)
Binding site273Zn2+ 1 (UniProtKB | ChEBI)
Binding site304Zn2+ 2 (UniProtKB | ChEBI)
Binding site304Zn2+ 1 (UniProtKB | ChEBI)
Binding site341N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI)
Binding site363Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentearly endosome membrane
Cellular ComponentGolgi membrane
Cellular Componentmembrane-bounded organelle
Molecular FunctionN-acylphosphatidylethanolamine-specific phospholipase D activity
Molecular Functionzinc ion binding
Biological ProcessN-acylethanolamine metabolic process
Biological ProcessN-acylphosphatidylethanolamine metabolic process
Biological Processphospholipid catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
  • EC number

Gene names

    • Name
      napepld
    • Synonyms
      fc56b11
      , nape-pld
      , si:dkey-65m5.3
      , wu:fc56b11
      , zgc:158854

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    A0A8M2BC81

Proteomes

Organism-specific databases

Subcellular Location

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.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain164-364Metallo-beta-lactamase

Sequence similarities

Belongs to the NAPE-PLD family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    415
  • Mass (Da)
    46,185
  • Last updated
    2022-08-03 v1
  • Checksum
    194C8590FD6C03CC
MAAHTSGLLLGRLHQRRARALATLPKQTGASLRLAELTHRCLCSSAAGGVSMAEQPLVGASSSTPLDYRQEADVTCSRRDSQGRFVNPWSTWHFPSYTTVARLFLTEKNNSKIPSAKEALDRELPIVQPYFIQNPDQCGQTGTSVRATWLGHATVLVEMEGLLVLTDPIFSQRASPVAFMGPKRYRDPPCTIEQLPRLDAVVISHTHYDHLDAASVTALNSRFGSALHWFVPLGLAEWMQKTGCENVTELDWWVGSRIPGHDNVSFFCTPAQHWCKRTPVDDNKTLWGSWSIVGSHSRFFFAGDTGYCASFKEIGRHFGPFDLAAIPIGAYVPRGIMKSQHVDPEEAVQIHIDVQAKASLAIHWGTFPLSYEHYLEPPARLREAMVNLGLNPDDFFTLHHGESRMINLKDMHSSS

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q5TZE8Q5TZE8_DANREnapepld416
A0A2R8RJ40A0A2R8RJ40_DANREnapepld364

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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