Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytosolic phospholipase A2

Gene

Pla2g4a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulationi

Stimulated by agonists such as ATP, EGF, thrombin and bradykinin as well as by cytosolic Ca2+.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi40Calcium 1By similarity1
Metal bindingi40Calcium 2By similarity1
Metal bindingi41Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi43Calcium 1By similarity1
Metal bindingi43Calcium 2By similarity1
Metal bindingi65Calcium 1By similarity1
Metal bindingi93Calcium 2By similarity1
Metal bindingi94Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi95Calcium 2By similarity1
Active sitei228NucleophileBy similarity1
Active sitei548Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

  • arachidonic acid secretion Source: UniProtKB
  • cellular response to antibiotic Source: MGI
  • icosanoid biosynthetic process Source: MGI
  • phospholipid catabolic process Source: InterPro
  • regulation of cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.4. 3474.
ReactomeiR-MMU-111995. phospho-PLA2 pathway.
R-MMU-1482788. Acyl chain remodelling of PC.
R-MMU-1482798. Acyl chain remodeling of CL.
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-1483115. Hydrolysis of LPC.
R-MMU-1483166. Synthesis of PA.
R-MMU-2142753. Arachidonic acid metabolism.
R-MMU-418592. ADP signalling through P2Y purinoceptor 1.
R-MMU-432142. Platelet sensitization by LDL.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
SABIO-RKP47713.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic phospholipase A2
Short name:
cPLA2
Alternative name(s):
Phospholipase A2 group IVA
Including the following 2 domains:
Phospholipase A2 (EC:3.1.1.4)
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Lysophospholipase (EC:3.1.1.5)
Gene namesi
Name:Pla2g4a
Synonyms:Cpla2, Pla2g4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1195256. Pla2g4a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: MGI
  • Golgi apparatus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2907.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001872631 – 748Cytosolic phospholipase A2Add BLAST748

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineBy similarity1
Modified residuei268PhosphothreonineBy similarity1
Modified residuei434PhosphoserineBy similarity1
Modified residuei435PhosphoserineCombined sources1
Modified residuei437PhosphoserineCombined sources1
Modified residuei505Phosphoserine; by MAPKCombined sources1 Publication1
Modified residuei515PhosphoserineBy similarity1
Modified residuei726PhosphoserineCombined sources1 Publication1
Modified residuei728PhosphoserineCombined sources1

Post-translational modificationi

Activated by phosphorylation at both Ser-505 and Ser-726.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP47713.
PeptideAtlasiP47713.
PRIDEiP47713.

PTM databases

iPTMnetiP47713.
PhosphoSitePlusiP47713.
SwissPalmiP47713.

Miscellaneous databases

PMAP-CutDBP47713.

Expressioni

Gene expression databases

BgeeiENSMUSG00000056220.
ExpressionAtlasiP47713. baseline and differential.
GenevisibleiP47713. MM.

Interactioni

Protein-protein interaction databases

BioGridi202222. 6 interactors.
IntActiP47713. 14 interactors.
MINTiMINT-4106449.
STRINGi10090.ENSMUSP00000070868.

Chemistry databases

BindingDBiP47713.

Structurei

3D structure databases

ProteinModelPortaliP47713.
SMRiP47713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 106C2PROSITE-ProRule annotationAdd BLAST102
Domaini140 – 739PLA2cPROSITE-ProRule annotationAdd BLAST600

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 178Phospholipid bindingCuratedAdd BLAST178

Domaini

The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca2+ (By similarity).By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PLA2c domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1012. Eukaryota.
KOG1325. Eukaryota.
ENOG410XR72. LUCA.
GeneTreeiENSGT00550000074489.
HOGENOMiHOG000115420.
HOVERGENiHBG053479.
InParanoidiP47713.
KOiK16342.
OMAiRFSMALC.
OrthoDBiEOG091G0276.
PhylomeDBiP47713.
TreeFamiTF325228.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47713-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGTFGDMLD TPDPYVELFI
60 70 80 90 100
STTPDSRKRT RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE
110 120 130 140 150
TLGTATFPVS SMKVGEKKEV PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL
160 170 180 190 200
CDQEKTFRQQ RKENIKENMK KLLGPKKSEG LYSTRDVPVV AILGSGGGFR
210 220 230 240 250
AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH PDFPEKGPEE
260 270 280 290 300
INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
310 320 330 340 350
ETLIQNRMSM TLSSLKEKVN AARCPLPLFT CLHVKPDVSE LMFADWVEFS
360 370 380 390 400
PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL
410 420 430 440 450
FNRVLGVSGS QNKGSTMEEE LENITAKHIV SNDSSDSDDE AQGPKGTENE
460 470 480 490 500
EAEKEYQSDN QASWVHRMLM ALVSDSALFN TREGRAGKVH NFMLGLNLNT
510 520 530 540 550
SYPLSPLRDF SSQDSFDDEL DAAVADPDEF ERIYEPLDVK SKKIHVVDSG
560 570 580 590 600
LTFNLPYPLI LRPQRGVDLI ISFDFSARPS DTSPPFKELL LAEKWAKMNK
610 620 630 640 650
LPFPKIDPYV FDREGLKECY VFKPKNPDVE KDCPTIIHFV LANINFRKYK
660 670 680 690 700
APGVLRETKE EKEIADFDIF DDPESPFSTF NFQYPNQAFK RLHDLMYFNT
710 720 730 740
LNNIDVIKDA IVESIEYRRQ NPSRCSVSLS NVEARKFFNK EFLSKPTV
Length:748
Mass (Da):85,222
Last modified:February 1, 1996 - v1
Checksum:i49D12BBB2911492A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M72394 mRNA. Translation: AAB00796.1.
BC003816 mRNA. Translation: AAH03816.1.
CCDSiCCDS15352.1.
PIRiB39898.
RefSeqiNP_032895.1. NM_008869.4.
UniGeneiMm.4186.

Genome annotation databases

EnsembliENSMUST00000070200; ENSMUSP00000070868; ENSMUSG00000056220.
GeneIDi18783.
KEGGimmu:18783.
UCSCiuc007cxt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M72394 mRNA. Translation: AAB00796.1.
BC003816 mRNA. Translation: AAH03816.1.
CCDSiCCDS15352.1.
PIRiB39898.
RefSeqiNP_032895.1. NM_008869.4.
UniGeneiMm.4186.

3D structure databases

ProteinModelPortaliP47713.
SMRiP47713.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202222. 6 interactors.
IntActiP47713. 14 interactors.
MINTiMINT-4106449.
STRINGi10090.ENSMUSP00000070868.

Chemistry databases

BindingDBiP47713.
ChEMBLiCHEMBL2907.

PTM databases

iPTMnetiP47713.
PhosphoSitePlusiP47713.
SwissPalmiP47713.

Proteomic databases

PaxDbiP47713.
PeptideAtlasiP47713.
PRIDEiP47713.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070200; ENSMUSP00000070868; ENSMUSG00000056220.
GeneIDi18783.
KEGGimmu:18783.
UCSCiuc007cxt.2. mouse.

Organism-specific databases

CTDi5321.
MGIiMGI:1195256. Pla2g4a.

Phylogenomic databases

eggNOGiKOG1012. Eukaryota.
KOG1325. Eukaryota.
ENOG410XR72. LUCA.
GeneTreeiENSGT00550000074489.
HOGENOMiHOG000115420.
HOVERGENiHBG053479.
InParanoidiP47713.
KOiK16342.
OMAiRFSMALC.
OrthoDBiEOG091G0276.
PhylomeDBiP47713.
TreeFamiTF325228.

Enzyme and pathway databases

BRENDAi3.1.1.4. 3474.
ReactomeiR-MMU-111995. phospho-PLA2 pathway.
R-MMU-1482788. Acyl chain remodelling of PC.
R-MMU-1482798. Acyl chain remodeling of CL.
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-1483115. Hydrolysis of LPC.
R-MMU-1483166. Synthesis of PA.
R-MMU-2142753. Arachidonic acid metabolism.
R-MMU-418592. ADP signalling through P2Y purinoceptor 1.
R-MMU-432142. Platelet sensitization by LDL.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
SABIO-RKP47713.

Miscellaneous databases

PMAP-CutDBP47713.
PROiP47713.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000056220.
ExpressionAtlasiP47713. baseline and differential.
GenevisibleiP47713. MM.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA24A_MOUSE
AccessioniPrimary (citable) accession number: P47713
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.