A0A7J7V479 · A0A7J7V479_MYOMY

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 zinc divalent cations per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site185Zn2+ 1 (UniProtKB | ChEBI)
Binding site187Zn2+ 1 (UniProtKB | ChEBI)
Binding site188an N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI)
Binding site189Zn2+ 2 (UniProtKB | ChEBI)
Binding site190Zn2+ 2 (UniProtKB | ChEBI)
Binding site253Zn2+ 1 (UniProtKB | ChEBI)
Binding site256deoxycholate (UniProtKB | ChEBI)
Binding site260deoxycholate (UniProtKB | ChEBI)
Binding site284Zn2+ 2 (UniProtKB | ChEBI)
Binding site284Zn2+ 1 (UniProtKB | ChEBI)
Binding site321an N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine (UniProtKB | ChEBI)
Binding site343Zn2+ 2 (UniProtKB | ChEBI)
Binding site348deoxycholate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentearly endosome membrane
Cellular ComponentGolgi membrane
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

    • ORF names
      mMyoMyo1_013672

Organism names

  • Taxonomic identifier
  • Strain
    • MMyoMyo1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yangochiroptera > Vespertilionidae > Myotis

Accessions

  • Primary accession
    A0A7J7V479

Proteomes

Organism-specific databases

Subcellular Location

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 bias1-18Polar residues
Region1-40Disordered
Domain144-344Metallo-beta-lactamase

Sequence similarities

Belongs to the NAPE-PLD family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    394
  • Mass (Da)
    45,503
  • Last updated
    2021-04-07 v1
  • Checksum
    4A8D2C4C6D677328
MDENESNQSLMTSSQYPKEVVRRRQHSARNSGGSTSSRFSRKSFKLDYRLEEDVTKSRRGKDGRFVNPWPTWKSLSIPNILRWLIMEKDHSSIPSSKEELDKELPVLKPYFINDPEAAGVSEAGLRVTWLGHAMVMVEMDELIFLTDPMFSSRASPSQYMGPKRFRQAPCSVGELPAIDAVLISHNHYDHLDYSSVVSLNERFGNDLRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLLDDNKALWGSWSVLGPWNRFFFAGDTGYCPVFEEIGRRFGPFDLAAIPIGAYAPRWFMKYQHVDPEEAVRIHIDVQAKKSVAIHWGTFALANEHYLEPPVKLSEALERYGLKNEDFFVLKHGESRYIHTSDESFE

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A7J7V4D7A0A7J7V4D7_MYOMYmMyoMyo1_013672662
A0A7J7V452A0A7J7V452_MYOMYmMyoMyo1_013672309

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABWUV010000011
EMBL· GenBank· DDBJ
KAF6319882.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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