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P47713 (PA24A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic phospholipase A2

Short name=cPLA2
Alternative name(s):
Phospholipase A2 group IVA

Including the following 2 domains:

  1. Phospholipase A2
    EC=3.1.1.4
    Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
  2. Lysophospholipase
    EC=3.1.1.5
Gene names
Name:Pla2g4a
Synonyms:Cpla2, Pla2g4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length748 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulation

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

Subcellular location

Cytoplasm. Cytoplasmic vesicle. Note: Translocates to membrane vesicles in a calcium-dependent fashion.

Domain

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.

Post-translational modification

Activated by phosphorylation at both Ser-505 and Ser-726.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PLA2c domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCytoplasm
Cytoplasmic vesicle
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid secretion

Inferred from direct assay PubMed 10946309. Source: UniProtKB

cellular response to antibiotic

Inferred from direct assay PubMed 17293613. Source: MGI

icosanoid biosynthetic process

Inferred from mutant phenotype PubMed 17293613. Source: MGI

phospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of cell proliferation

Inferred from genetic interaction PubMed 10969066. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 17293613. Source: MGI

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 10946309. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 17293613. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-dependent phospholipase A2 activity

Inferred from electronic annotation. Source: Ensembl

calcium-dependent phospholipid binding

Inferred from sequence or structural similarity. Source: UniProtKB

lysophospholipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phospholipase A2 activity

Inferred from direct assay PubMed 10946309. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 748748Cytosolic phospholipase A2
PRO_0000187263

Regions

Domain5 – 106102C2
Domain140 – 739600PLA2c
Region1 – 178178Phospholipid binding Probable

Sites

Active site2281Nucleophile By similarity
Active site5481Proton acceptor By similarity
Metal binding401Calcium 1 By similarity
Metal binding401Calcium 2 By similarity
Metal binding411Calcium 1; via carbonyl oxygen By similarity
Metal binding431Calcium 1 By similarity
Metal binding431Calcium 2 By similarity
Metal binding651Calcium 1 By similarity
Metal binding931Calcium 2 By similarity
Metal binding941Calcium 2; via carbonyl oxygen By similarity
Metal binding951Calcium 2 By similarity

Amino acid modifications

Modified residue2681Phosphothreonine By similarity
Modified residue4371Phosphoserine Ref.5
Modified residue5051Phosphoserine; by MAPK Ref.3
Modified residue7261Phosphoserine Ref.3
Modified residue7281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P47713 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 49D12BBB2911492A

FASTA74885,222
        10         20         30         40         50         60 
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGTFGDMLD TPDPYVELFI STTPDSRKRT 

        70         80         90        100        110        120 
RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFPVS SMKVGEKKEV 

       130        140        150        160        170        180 
PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKENIKENMK KLLGPKKSEG 

       190        200        210        220        230        240 
LYSTRDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH 

       250        260        270        280        290        300 
PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG 

       310        320        330        340        350        360 
ETLIQNRMSM TLSSLKEKVN AARCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG 

       370        380        390        400        410        420 
TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QNKGSTMEEE 

       430        440        450        460        470        480 
LENITAKHIV SNDSSDSDDE AQGPKGTENE EAEKEYQSDN QASWVHRMLM ALVSDSALFN 

       490        500        510        520        530        540 
TREGRAGKVH NFMLGLNLNT SYPLSPLRDF SSQDSFDDEL DAAVADPDEF ERIYEPLDVK 

       550        560        570        580        590        600 
SKKIHVVDSG LTFNLPYPLI LRPQRGVDLI ISFDFSARPS DTSPPFKELL LAEKWAKMNK 

       610        620        630        640        650        660 
LPFPKIDPYV FDREGLKECY VFKPKNPDVE KDCPTIIHFV LANINFRKYK APGVLRETKE 

       670        680        690        700        710        720 
EKEIADFDIF DDPESPFSTF NFQYPNQAFK RLHDLMYFNT LNNIDVIKDA IVESIEYRRQ 

       730        740 
NPSRCSVSLS NVEARKFFNK EFLSKPTV 

« Hide

References

« Hide 'large scale' references
[1]"A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP."
Clark J.D., Lin L.-L., Kriz R.W., Ramesha C.S., Sultzman L.A., Lin A.Y., Milona N., Knopf J.L.
Cell 65:1043-1051(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[3]"Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases."
Hefner Y., Boersch-Haubold A.G., Murakami M., Wilde J.I., Pasquet S., Schieltz D., Ghomashchi F., Yates J.R. III, Armstrong C.G., Paterson A., Cohen P., Fukunaga R., Hunter T., Kudo I., Watson S.P., Gelb M.H.
J. Biol. Chem. 275:37542-37551(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-505 AND SER-726, ACTIVATION.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M72394 mRNA. Translation: AAB00796.1.
BC003816 mRNA. Translation: AAH03816.1.
PIRB39898.
RefSeqNP_032895.1. NM_008869.3.
UniGeneMm.4186.

3D structure databases

ProteinModelPortalP47713.
SMRP47713. Positions 13-720.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202222. 6 interactions.
IntActP47713. 13 interactions.
MINTMINT-4106449.

Chemistry

BindingDBP47713.
ChEMBLCHEMBL2907.

PTM databases

PhosphoSiteP47713.

Proteomic databases

PaxDbP47713.
PRIDEP47713.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070200; ENSMUSP00000070868; ENSMUSG00000056220.
GeneID18783.
KEGGmmu:18783.
UCSCuc007cxt.1. mouse.

Organism-specific databases

CTD5321.
MGIMGI:1195256. Pla2g4a.

Phylogenomic databases

eggNOGNOG257248.
HOGENOMHOG000115420.
HOVERGENHBG053479.
InParanoidP47713.
KOK16342.
OMAETLIHNR.
OrthoDBEOG73V6JM.
PhylomeDBP47713.
TreeFamTF325228.

Enzyme and pathway databases

BRENDA3.1.1.4. 3474.
SABIO-RKP47713.

Gene expression databases

ArrayExpressP47713.
BgeeP47713.
GenevestigatorP47713.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295044.
PMAP-CutDBP47713.
PROP47713.
SOURCESearch...

Entry information

Entry namePA24A_MOUSE
AccessionPrimary (citable) accession number: P47713
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot