A0A1A8HJ44 · A0A1A8HJ44_9TELE

  • Protein
    N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
  • Gene
    NAPEPLD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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-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 site190Zn2+ 1 (UniProtKB | ChEBI)
Binding site192Zn2+ 1 (UniProtKB | ChEBI)
Binding site194Zn2+ 2 (UniProtKB | ChEBI)
Binding site195Zn2+ 2 (UniProtKB | ChEBI)
Binding site258Zn2+ 1 (UniProtKB | ChEBI)
Binding site261deoxycholate (UniProtKB | ChEBI)
Binding site265deoxycholate (UniProtKB | ChEBI)
Binding site289Zn2+ 2 (UniProtKB | ChEBI)
Binding site289Zn2+ 1 (UniProtKB | ChEBI)
Binding site348Zn2+ 2 (UniProtKB | ChEBI)
Binding site353deoxycholate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentearly endosome membrane
Cellular ComponentGolgi membrane
Molecular FunctionN-acylphosphatidylethanolamine-specific phospholipase D activity
Molecular Functionzinc ion binding
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

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Atherinomorphae > Cyprinodontiformes > Nothobranchiidae > Nothobranchius

Accessions

  • Primary accession
    A0A1A8HJ44

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 compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-22Basic and acidic residues
Region1-46Disordered
Domain148-349Metallo-beta-lactamase

Sequence similarities

Belongs to the NAPE-PLD family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    400
  • Mass (Da)
    45,481
  • Last updated
    2016-10-05 v1
  • Checksum
    974813DCF6980691
MEKPSSSDRATPEEKTGLVEDNADPKGAEGGQTDAQTSRKSSSRSSRKSFRLDYRLEEEVTKSCLDKNGRWTNPWPTWRFPSYTMLLRFLLLEKNHSNVPTSKETLDSELPVMEPYFVRSPDLSDSRPGLRVTWLGHATVLVEMEGVNILTDPIFSQRASPFQFMGPKRYRGPPCSVEQLPRIDAVLISHSHFDHLDAGSVASLNARFGGELRWFVPLGLMDWLVKMGCENVMELDWWEENCVPGHDNVTFVCTPSQHWSKRTAWDDNKSLWGSWSVLGPSFRFFFAGDTGYCSSFQEIGRRFGPFDLAAIPIGAYQPRYVMRGQHVDPEEAVQIHQDLQAKQSVAIHWGTFALAYENYLEPPVRLREALEQKGLKPESFFTLHHGESRLIATCDADVFD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-22Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HAEB01001690
EMBL· GenBank· DDBJ
SBQ48198.1
EMBL· GenBank· DDBJ
Transcribed RNA
HAEC01016039
EMBL· GenBank· DDBJ
SBQ84260.1
EMBL· GenBank· DDBJ
Transcribed RNA

Similar Proteins

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