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Protein

Group IIF secretory phospholipase A2

Gene

Pla2g2f

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May play a role in lipid mediator production in inflammatory conditions, by providing arachidonic acid to downstream cyclooxygenases and lipoxygenases. Phospholipase A2, which catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:10531313). Hydrolyzes phosphatidylethanolamine more efficiently than phosphatidylcholine, with only a modest preference for arachidonic acid versus linoelic acid at the sn-2 position. Comparable activity toward 1-palmitoyl-2-oleoyl-phosphatidylserine vesicles to that toward 1-palmitoyl-2-oleoyl-phosphatidylglycerol (PubMed:11877435). Prefers phosphatidylglycerol compared to phosphatidylcholine (PubMed:10531313).2 Publications

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

pH dependencei

Optimum pH is 6.0-7.0.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi47Calcium; via carbonyl oxygenBy similarity1
Metal bindingi49Calcium; via carbonyl oxygenBy similarity1
Metal bindingi51Calcium; via carbonyl oxygenBy similarity1
Active sitei67PROSITE-ProRule annotation1
Metal bindingi68CalciumBy similarity1
Active sitei114PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • arachidonic acid secretion Source: InterPro
  • innate immune response Source: UniProtKB-KW
  • lipid catabolic process Source: UniProtKB-KW
  • negative regulation of T cell proliferation Source: MGI
  • phospholipid metabolic process Source: MGI

Keywordsi

Molecular functionHydrolase
Biological processImmunity, Innate immunity, Lipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1482788 Acyl chain remodelling of PC
R-MMU-1482801 Acyl chain remodelling of PS
R-MMU-1482839 Acyl chain remodelling of PE
R-MMU-1482922 Acyl chain remodelling of PI
R-MMU-1482925 Acyl chain remodelling of PG
R-MMU-1483166 Synthesis of PA

Names & Taxonomyi

Protein namesi
Recommended name:
Group IIF secretory phospholipase A2 (EC:3.1.1.4)
Short name:
GIIF sPLA2
Short name:
sPLA2-IIF
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase 2F
Gene namesi
Name:Pla2g2f
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1349661 Pla2g2f

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49G → S: Loss of catalytic activity. 1 Publication1
Mutagenesisi157C → S: No effect on lipase activity toward 1-palmitoyl-2-arachidonoyl-phosphatidylethanolamine (2-AA-PE). 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5361

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000002276021 – 168Group IIF secretory phospholipase A2Add BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 138By similarity
Disulfide bondi48 ↔ 64By similarity
Disulfide bondi63 ↔ 120By similarity
Disulfide bondi69 ↔ 145By similarity
Disulfide bondi70 ↔ 113By similarity
Disulfide bondi79 ↔ 106By similarity
Glycosylationi92N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi98 ↔ 111By similarity
Glycosylationi102N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi144N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9QZT4
PRIDEiQ9QZT4

PTM databases

iPTMnetiQ9QZT4
PhosphoSitePlusiQ9QZT4

Expressioni

Tissue specificityi

Strongly expressed in testis.1 Publication

Developmental stagei

Strongly expressed during embryogenesis.1 Publication

Inductioni

Strongly up-regulated by lipopolysaccharide (LPS) in brain, heart, liver, colon and testis.1 Publication

Gene expression databases

BgeeiENSMUSG00000028749
CleanExiMM_PLA2G2F
GenevisibleiQ9QZT4 MM

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030526

Chemistry databases

BindingDBiQ9QZT4

Structurei

3D structure databases

ProteinModelPortaliQ9QZT4
SMRiQ9QZT4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni139 – 168Required for localization on the plasma membrane1 PublicationAdd BLAST30

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4087 Eukaryota
ENOG411283D LUCA
GeneTreeiENSGT00760000119160
HOGENOMiHOG000231749
HOVERGENiHBG008137
InParanoidiQ9QZT4
KOiK01047
OMAiYCQGPTP
OrthoDBiEOG091G0UZ3
PhylomeDBiQ9QZT4
TreeFamiTF319283

Family and domain databases

CDDicd00125 PLA2c, 1 hit
Gene3Di1.20.90.10, 1 hit
InterProiView protein in InterPro
IPR001211 PLipase_A2
IPR016090 PLipase_A2_dom
IPR036444 PLipase_A2_dom_sf
IPR033113 PLipase_A2_His_AS
PANTHERiPTHR11716 PTHR11716, 1 hit
PfamiView protein in Pfam
PF00068 Phospholip_A2_1, 1 hit
PRINTSiPR00389 PHPHLIPASEA2
SMARTiView protein in SMART
SM00085 PA2c, 1 hit
SUPFAMiSSF48619 SSF48619, 1 hit
PROSITEiView protein in PROSITE
PS00118 PA2_HIS, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QZT4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKKFFAIAVL AGSVVTTAHS SLLNLKSMVE AITHRNSILS FVGYGCYCGL
60 70 80 90 100
GGRGHPMDEV DWCCHAHDCC YEKLFEQGCR PYVDHYDHRI ENGTMIVCTE
110 120 130 140 150
LNETECDKQT CECDKSLTLC LKDHPYRNKY RGYFNVYCQG PTPNCSIYDP
160
YPEEVTCGHG LPATPVST
Length:168
Mass (Da):18,880
Last modified:May 1, 2000 - v1
Checksum:i9E15FB6AC0F5450C
GO
Isoform 2 (identifier: Q9QZT4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MADGAQANPKGFRKKALVKHSTGRKSPSLRASPSKTSRSSLGM

Note: No signal peptide could be predicted in this isoform, challenging its subcellular location within the secretory pathway and hence the formation of disulfide bonds, which are required for its activity. Gene prediction based on EST data. No experimental available.Curated
Show »
Length:210
Mass (Da):23,259
Checksum:i5AC55CD96F68FC28
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0375251M → MADGAQANPKGFRKKALVKH STGRKSPSLRASPSKTSRSS LGM in isoform 2. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF166099 mRNA Translation: AAF04500.2
AK029254 mRNA Translation: BAC26357.1
AL844178 Genomic DNA Translation: CAM21862.1
BC125567 mRNA Translation: AAI25568.1
CCDSiCCDS18832.1 [Q9QZT4-2]
RefSeqiNP_036175.2, NM_012045.4 [Q9QZT4-2]
UniGeneiMm.331989

Genome annotation databases

EnsembliENSMUST00000030526; ENSMUSP00000030526; ENSMUSG00000028749 [Q9QZT4-2]
GeneIDi26971
KEGGimmu:26971
UCSCiuc008vlf.2 mouse [Q9QZT4-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiPA2GF_MOUSE
AccessioniPrimary (citable) accession number: Q9QZT4
Secondary accession number(s): Q8CE14
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 1, 2000
Last modified: April 25, 2018
This is version 133 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health