Q9QUL3 · PA2GE_MOUSE

  • Protein
    Group IIE secretory phospholipase A2
  • Gene
    Pla2g2e
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids (PubMed:10531313, PubMed:11922621).
Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines (By similarity).
In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver (PubMed:24910243).
May act in an autocrine and paracrine manner (By similarity).
Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria (By similarity).
Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis (PubMed:27226633).
May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes. Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells (PubMed:11922621).

Catalytic activity

  • a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H+
  • 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H+ + hexadecanoate
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoglycerol + 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+
    This reaction proceeds in the forward direction.
    EC:3.1.1.4 (UniProtKB | ENZYME | Rhea)
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoate
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+
    This reaction proceeds in the forward direction.

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 2 Ca2+ ions per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site41Ca2+ 2 (UniProtKB | ChEBI)
Binding site43Ca2+ 2 (UniProtKB | ChEBI)
Binding site45Ca2+ 1 (UniProtKB | ChEBI)
Binding site45Ca2+ (UniProtKB | ChEBI)
Binding site47Ca2+ 1 (UniProtKB | ChEBI)
Binding site47Ca2+ (UniProtKB | ChEBI)
Binding site49Ca2+ 1 (UniProtKB | ChEBI)
Binding site49Ca2+ (UniProtKB | ChEBI)
Active site65
Binding site66Ca2+ 1 (UniProtKB | ChEBI)
Binding site66Ca2+ (UniProtKB | ChEBI)
Active site109
Binding site130Ca2+ 2 (UniProtKB | ChEBI)
Binding site132Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentextracellular region
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent phospholipase A2 activity
Molecular Functionphospholipid binding
Biological Processarachidonic acid secretion
Biological Processinflammatory response
Biological Processlipid catabolic process
Biological Processlow-density lipoprotein particle remodeling
Biological Processnegative regulation of T cell proliferation
Biological Processphosphatidylcholine metabolic process
Biological Processphosphatidylglycerol metabolic process
Biological Processphospholipid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Group IIE secretory phospholipase A2
  • EC number
  • Short names
    GIIE sPLA2; sPLA2-IIE
  • Alternative names
    • Phosphatidylcholine 2-acylhydrolase 2E

Gene names

    • Name
      Pla2g2e

Organism names

  • Taxonomic identifier
  • Strain
    • BALB/cJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9QUL3

Proteomes

Organism-specific databases

Subcellular Location

Secreted
Cytoplasm
Note: Through binding to heparan sulfate proteoglycan, may be localized to cytoplasmic compartments enriched in anionic phospholipids.

Keywords

Phenotypes & Variants

Disruption phenotype

Mutant mice show abnormal hair follicle ultrastructure characterized by defects in the companion layer, the inner root sheath (IRS) and hair shaft. Mutant IRS cells have large cytoplasmic cysts and pyknotic nuclei and are devoid of keratohyalin granules, whereas the cuticle is abnormally dissociated from the hair cortex and medulla, indicative of impaired hair follicle development (PubMed:27226633).
Mutant mice are protected from obesity and hyperlipidemia in response to high-fat diet (PubMed:24910243).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000002275820-142Group IIE secretory phospholipase A2
Disulfide bond44↔135
Disulfide bond46↔62
Disulfide bond61↔115
Disulfide bond67↔142
Disulfide bond68↔108
Disulfide bond77↔101
Disulfide bond95↔106

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in skin and uterus, and at lower levels in various other tissues (PubMed:10531313, PubMed:10681567, PubMed:11922621, PubMed:27226633).
Expressed in hair follicles, specifically localized in companion cells of the outer root sheath and cuticular cells of the inner root sheath in hair follicles during anagen (PubMed:27226633).
Expressed in white and brown adipose tissue (PubMed:24910243).

Induction

Up-regulated in thymus, small intestine, brain, heart, testis, kidney and lung upon endotoxin challenge (PubMed:10681567, PubMed:11922621).
Detected in alveolar macrophage-like cells upon endotoxin challenge (PubMed:10681567).
Up-regulated in white and brown adipocytes upon high-fat diet (PubMed:24910243).
Up-regulated in ear epidermis in response to topical dermatitis agent 2,4-dinitrobenzene (DNFB) (PubMed:11922621).

Developmental stage

Expressed abundantly in hair follicles during the anagen phase. Low expression is observed before birth, then follows hair cycle progression: up-regulated markedly during P5-P15 (anagen phase), declining to nearly the basal level during P20-P25 (catagen and telogen) and then increasing again at P30 (next anagen).

Gene expression databases

Interaction

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the phospholipase A2 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    142
  • Mass (Da)
    15,943
  • Last updated
    2000-05-01 v1
  • Checksum
    8B0E3CC710A1F946
MKPPIALACLCLLVPLAGGNLVQFGVMIERMTGKPALQYNDYGCYCGVGGSHWPVDETDWCCHAHDCCYGRLEKLGCDPKLEKYLFSITRDNIFCAGRTACQRHTCECDKRAALCFRHNLNTYNRKYAHYPNKLCTGPTPPC

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A2APQ4A2APQ4_MOUSEPla2g2e80

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF166098
EMBL· GenBank· DDBJ
AAF04499.1
EMBL· GenBank· DDBJ
mRNA
AF112984
EMBL· GenBank· DDBJ
AAF22290.1
EMBL· GenBank· DDBJ
mRNA
BC027524
EMBL· GenBank· DDBJ
AAH27524.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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