A0A099ZUP7 · A0A099ZUP7_TINGU

Function

Catalytic activity

  • (9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate
    This reaction proceeds in the forward direction.
  • 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate
    This reaction proceeds in the forward direction.
  • H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate
    This reaction proceeds in the forward direction.
  • H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate
    This reaction proceeds in the forward direction.
  • H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate
    This reaction proceeds in the forward direction.
  • H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine
    This reaction proceeds in the forward direction.
  • a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.4 (UniProtKB | ENZYME | Rhea)
  • a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H+ + phosphate
    This reaction proceeds in the forward direction.
    EC:3.6.1.75 (UniProtKB | ENZYME | Rhea)
  • a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.106 (UniProtKB | ENZYME | Rhea)
  • an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate
    This reaction proceeds in the forward direction.

Pathway

Lipid metabolism; phospholipid metabolism.
Phospholipid metabolism.

GO annotations

AspectTerm
Cellular Componentapical plasma membrane
Cellular Componentcaveola
Molecular Functionlysophosphatidic acid phosphatase activity
Molecular Functionphosphatidate phosphatase activity
Biological Processphospholipid dephosphorylation
Biological Processphospholipid metabolic process
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phospholipid phosphatase 1
  • EC number
  • Alternative names
    • Lipid phosphate phosphohydrolase 1
    • PAP2-alpha
    • Phosphatidate phosphohydrolase type 2a
    • Phosphatidic acid phosphatase 2a

Gene names

    • ORF names
      N309_08666

Organism names

  • Taxonomic identifier
  • Strain
    • BGI_N309
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Palaeognathae > Tinamiformes > Tinamidae > Tinamus

Accessions

  • Primary accession
    A0A099ZUP7

Proteomes

Subcellular Location

Apical cell membrane
; Multi-pass membrane protein
Cell membrane
; Multi-pass membrane protein
Membrane raft
; Multi-pass membrane protein
Membrane, caveola
; Multi-pass membrane protein
Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane41-64Helical
Transmembrane76-94Helical
Transmembrane148-168Helical
Transmembrane180-199Helical
Transmembrane211-233Helical

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain85-226Phosphatidic acid phosphatase type 2/haloperoxidase
Region246-266Disordered
Compositional bias251-266Polar residues

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    266
  • Mass (Da)
    29,806
  • Last updated
    2015-01-07 v1
  • Checksum
    E7DCC4CCB204CC67
LLAGLPFAILNSRRIPFQRGVFCSDDSIRYPYKEDTISYKLLAGIIVPFCIIVIIVGETLSVSYNHLHSNSFVRNSYIATIYKAIGTFIFGAAASQSLTDIAKYSIGRLRPHFLAVCQPDWARINCTLGYVENFLCQGDKAKINEGRLSFYSGHSSFSMYCMLFLALYLQARMKGDWARLVRPTLQFALVAASIYVGLSRVSDYKHHWSDVLTGLIQGAVVAVLIVLYVSDFFKVRACTFQPKEDSHTTLHETPTNGNHFGSNHQP

Features

Showing features for non-terminal residue, compositional bias.

TypeIDPosition(s)Description
Non-terminal residue1
Compositional bias251-266Polar residues
Non-terminal residue266

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KL898626
EMBL· GenBank· DDBJ
KGL85531.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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