Cytosolic phospholipase A2 - Mus musculus (Mouse)

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P47713 (PA24A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Pla2g4a
Synonyms:	Cpla2, Pla2g4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	748 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Cellular component	Cytoplasm Cytoplasmic vesicle
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	arachidonic 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_component	Golgi 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_function	calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB calcium-dependent phospholipid binding Inferred from sequence or structural similarity. Source: UniProtKB lysophospholipase activity Inferred from electronic annotation. Source: EC phospholipase A2 activity Inferred from direct assay PubMed 10946309. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 748

748

Cytosolic phospholipase A2

PRO_0000187263

Regions

Domain

5 – 106

102

Domain

140 – 739

600

PLA2c

Region

1 – 178

178

Phospholipid binding Probable

Sites

Active site

228

Nucleophile By similarity

Active site

548

Proton acceptor By similarity

Metal binding

Calcium 1 By similarity

Metal binding

Calcium 2 By similarity

Metal binding

Calcium 1; via carbonyl oxygen By similarity

Metal binding

Calcium 1 By similarity

Metal binding

Calcium 2 By similarity

Metal binding

Calcium 1 By similarity

Metal binding

Calcium 2 By similarity

Metal binding

Calcium 2; via carbonyl oxygen By similarity

Metal binding

Calcium 2 By similarity

Amino acid modifications

Modified residue

268

Phosphothreonine By similarity

Modified residue

437

Phosphoserine Ref.5 Ref.6

Modified residue

505

Phosphoserine; by MAPK Ref.3

Modified residue

726

Phosphoserine Ref.3 Ref.4

Modified residue

728

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P47713 [UniParc].

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

FASTA

748

85,222

        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' referencesShow '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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-726, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, MASS SPECTROMETRY. Tissue: Melanoma.
[6]	"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, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M72394 mRNA. Translation: AAB00796.1. BC003816 mRNA. Translation: AAH03816.1.
IPI	IPI00111169.
PIR	B39898.
RefSeq	NP_032895.1. NM_008869.3.
UniGene	Mm.4186.
3D structure databases
ProteinModelPortal	P47713.
SMR	P47713. Positions 13-720.
ModBase	Search...
Protein-protein interaction databases
IntAct	P47713. 12 interactions.
PTM databases
PhosphoSite	P47713.
Proteomic databases
PaxDb	P47713.
PRIDE	P47713.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000070200; ENSMUSP00000070868; ENSMUSG00000056220.
GeneID	18783.
KEGG	mmu:18783.
Organism-specific databases
CTD	5321.
MGI	MGI:1195256. Pla2g4a.
Phylogenomic databases
eggNOG	NOG257248.
HOGENOM	HOG000115420.
HOVERGEN	HBG053479.
InParanoid	P47713.
KO	K16342.
OMA	ETLIHNR.
OrthoDB	EOG4Z62MZ.
Enzyme and pathway databases
BRENDA	3.1.1.4. 3474.
SABIO-RK	P47713.
Gene expression databases
ArrayExpress	P47713.
Bgee	P47713.
Genevestigator	P47713.
GermOnline	ENSMUSG00000056220. Mus musculus.
Family and domain databases
InterPro	IPR016035. Acyl_Trfase/lysoPLipase. IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR002642. LysoPLipase_cat_dom. [Graphical view]
Pfam	PF00168. C2. 1 hit. PF01735. PLA2_B. 1 hit. [Graphical view]
SMART	SM00239. C2. 1 hit. SM00022. PLAc. 1 hit. [Graphical view]
SUPFAM	SSF52151. Acyl_Trfase/lysoPlipase. 1 hit. SSF49562. C2_CaLB. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS51210. PLA2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P47713.
ChEMBL	CHEMBL2907.
NextBio	295044.
PMAP-CutDB	P47713.
SOURCE	Search...

Entry information

Entry name

PA24A_MOUSE

Accession

Primary (citable) accession number: P47713

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents