A0A7J8KEJ4 · A0A7J8KEJ4_ROUAE

Function

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-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + (9Z,12Z)-octadecadienoate + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
    EC:3.1.1.4 (UniProtKB | ENZYME | Rhea)

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site49Ca2+ (UniProtKB | ChEBI)
Binding site51Ca2+ (UniProtKB | ChEBI)
Active site67
Binding site68Ca2+ (UniProtKB | ChEBI)
Active site112

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent phospholipase A2 activity
Molecular Functionphospholipid binding
Biological Processarachidonic acid secretion
Biological Processlipid catabolic process
Biological Processnegative regulation of T cell proliferation
Biological Processphospholipid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phospholipase A2
  • EC number

Gene names

    • ORF names
      HJG63_015403

Organism names

Accessions

  • Primary accession
    A0A7J8KEJ4

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-20
ChainPRO_502995021121-148Phospholipase A2
Disulfide bond46↔141
Disulfide bond48↔64
Disulfide bond63↔118
Disulfide bond70↔111
Disulfide bond79↔104
Disulfide bond97↔109

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain21-142Phospholipase A2

Sequence similarities

Belongs to the phospholipase A2 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    148
  • Mass (Da)
    17,102
  • Last updated
    2021-04-07 v1
  • MD5 Checksum
    46877956A4485E88763E13096A2AB601
MELLHLYLLVVFAGVCPTQGGIQNLNKMVRHMTEKTPIISYWFYGCHCGLGGRGPPLDATDRCCHAHDCCYAHLRHHRCRIHTDLYSYNFSHGDIQCSDKGTWCEQELCACDKEVAFCLQRHLGSYKKELRFTRQFRPSRCKGKTPMC

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACASE010000001
EMBL· GenBank· DDBJ
KAF6507244.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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