A0A7J7F7X3 · A0A7J7F7X3_DICBM

Function

function

Hydrolyzes the ester bond of the acyl group attached at the sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1-acyl-2-lysophosphatidylserines (lysophospholipase activity) in the pathway of phosphatidylserines acyl chain remodeling. Cleaves phosphatidylserines exposed on the outer leaflet of the plasma membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines, which in turn enhance mast cell activation and histamine production. Has no activity toward other glycerophospholipids including phosphatidylcholines, phosphatidylethanolamines, phosphatidic acids or phosphatidylinositols, or glycerolipids such as triolein.

Caution

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

Catalytic activity

  • 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = sn-glycero-3-phospho-L-serine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-L-serine + hexadecanoate + H+
    This reaction proceeds in the forward direction.
  • a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-glycero-3-phospho-L-serine + a fatty acid + H+
    This reaction proceeds in the forward direction.
    EC:3.1.1.111 (UniProtKB | ENZYME | Rhea)
  • a 1-acyl-sn-glycero-3-phospho-L-serine + H2O = sn-glycero-3-phospho-L-serine + a fatty acid + H+
    This reaction proceeds in the forward direction.
    EC:3.1.1.111 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site173Nucleophile
Active site197Charge relay system
Binding site211Ca2+ (UniProtKB | ChEBI)
Binding site213Ca2+ (UniProtKB | ChEBI)
Binding site216Ca2+ (UniProtKB | ChEBI)
Active site267Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular space
Molecular Functionlipoprotein lipase activity
Molecular Functionmetal ion binding
Biological Processfatty acid biosynthetic process
Biological Processtriglyceride catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phospholipase A1 member A
  • EC number

Gene names

    • ORF names
      HPG69_010420

Organism names

Accessions

  • Primary accession
    A0A7J7F7X3

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_502990558525-463Phospholipase A1 member A

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain17-343Lipase

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    463
  • Mass (Da)
    50,664
  • Last updated
    2021-04-07 v1
  • Checksum
    C0903F1F41450234
MPPGLWERRCWVWGLLLWLSVGNAGDAPPTQQPKCTDFQNANLLRGTNLKVQFLLFTPSDPSCGQLVEESSDIQNSGFNVTLGTKLIIHGFRALGTKPSWIGKFIGALLRAVDANVIAVDWVYGSSGAYFSAVENVVKLGLEISRFLRKLLVGAEELRVLGVSESSIHILGVSLGAHVGGMVGHFYKGQLGRITGLDPAGPEYTRASLEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQDQPGCPSFIHAGYSYLICDHMRAVHLYISALENSCPLMAFPCASYKAFLAGHCLDCFNPFLLSCPRIGLVEQDGVKIEPLPKEVRVYLLTSSKAPYCVHHSFVEFYLQEPRKKDTSIAVTFLSGNVTSSVKITIPRQQLQGKGVIAHPNPQCQINQVKLKLQASNRVWKKDRTTIVGTFCTAPLPVHDNKKMVCLPEPVNLQASVTVSHDLKITCV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACDTQ010001070
EMBL· GenBank· DDBJ
KAF5923988.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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