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P50393 (PA24A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity. Cytoplasmic vesicle By similarity. Note: Translocates to membrane vesicles in a calcium-dependent fashion By similarity.

Tissue specificity

In brain tissue, expressed in low levels in olfactory mitral and granule cells, in hippocampal pyramidal cells and in dentate and cerebellar granule cells.

Induction

Levels of rat CPLA2 are increased in dentate granule cells during ischemia.

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-727 By similarity.

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_processaging

Inferred from expression pattern PubMed 15368358. Source: RGD

arachidonic acid metabolic process

Inferred from mutant phenotype PubMed 16603549. Source: RGD

decidualization

Inferred from mutant phenotype PubMed 10050766. Source: RGD

luteolysis

Inferred from expression pattern PubMed 11444430. Source: RGD

ovulation from ovarian follicle

Inferred from mutant phenotype PubMed 10189070. Source: RGD

phospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 15486059. Source: RGD

positive regulation of bone mineralization

Inferred from expression pattern PubMed 10807497. Source: RGD

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 17060404. Source: RGD

positive regulation of fever generation

Inferred from expression pattern PubMed 16933973. Source: RGD

positive regulation of inflammatory response

Inferred from mutant phenotype PubMed 17305324. Source: RGD

positive regulation of prostaglandin biosynthetic process

Inferred from mutant phenotype PubMed 16203828. Source: RGD

positive regulation of vesicle fusion

Inferred from mutant phenotype PubMed 17148545. Source: RGD

response to calcium ion

Inferred from mutant phenotype PubMed 16828086. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 10092307. Source: RGD

response to heat

Inferred from expression pattern PubMed 17483741. Source: RGD

response to hormone

Inferred from expression pattern PubMed 15368358. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 16864412. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 17093905. Source: RGD

response to methylmercury

Inferred from expression pattern PubMed 15019302. Source: RGD

response to organic substance

Inferred from mutant phenotype PubMed 17093080. Source: RGD

response to organonitrogen compound

Inferred from expression pattern PubMed 16603213. Source: RGD

response to vitamin D

Inferred from expression pattern PubMed 15225789. Source: RGD

surfactant homeostasis

Inferred from mutant phenotype PubMed 10025671. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15486059. Source: RGD

cytosol

Inferred from direct assay PubMed 12490538. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 1642464. Source: RGD

nucleus

Inferred from direct assay PubMed 15368358. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 15486059. Source: RGD

zymogen granule

Inferred from direct assay PubMed 17148545. Source: RGD

   Molecular_functioncalcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-dependent phospholipase A2 activity

Inferred from direct assay PubMed 8148815. Source: RGD

calcium-dependent phospholipid binding

Inferred from sequence or structural similarity. Source: UniProtKB

lysophospholipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phospholipase A2 activity

Traceable author statement PubMed 12051686. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 752752Cytosolic phospholipase A2
PRO_0000187264

Regions

Domain5 – 106102C2
Domain140 – 740601PLA2c
Region1 – 178178Phospholipid binding Probable

Sites

Active site2281Nucleophile By similarity
Active site5491Proton 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 By similarity
Modified residue5051Phosphoserine; by MAPK By similarity
Modified residue7271Phosphoserine By similarity
Modified residue7291Phosphoserine By similarity

Experimental info

Sequence conflict1391C → S in AAC21591. Ref.3
Sequence conflict1591R → Q in AAC21591. Ref.3
Sequence conflict2871Q → L in AAC21591. Ref.3
Sequence conflict308 – 3103MST → IVP in AAC21591. Ref.3
Sequence conflict4101S → L in AAC21591. Ref.3
Sequence conflict4891E → V in AAC21591. Ref.3
Sequence conflict6351P → T in AAC21591. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P50393 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C68F71BB05FBF732

FASTA75285,707
        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 CDQEKTFRRQ RKENIKENMK KLLGPKKSEG 

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

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

       310        320        330        340        350        360 
ETLIQNRMST TLSSLKEKVS AARCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG 

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

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

       490        500        510        520        530        540 
TREGRAGKEH NFMLGLNLNT SYPLSPLRDF SPQDSFDDDE LDAAVADPDE FERIYEPLDV 

       550        560        570        580        590        600 
KSKKIHVVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDTSPPFKEL LLAEKWAKMN 

       610        620        630        640        650        660 
KLPFPKIDPY VFDREGLKEC YVFKPKNPDV EKDCPTIIHF VLANINFRKY KAPGVLRETK 

       670        680        690        700        710        720 
EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMYFN TLNNIDVIKD AIVESIEYRR 

       730        740        750 
QNPSRCSVSL SNVEARKFFN KEFLSKPTAE SI 

« Hide

References

[1]"Molecular cloning of rat cDNA for cytosolic phospholipase A2 and the increased gene expression in the dentate gyrus following transient forebrain ischemia."
Owada Y., Tominaga T., Yoshimoto T., Kondo H.
Brain Res. Mol. Brain Res. 25:364-368(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]Erratum
Owada Y., Tominaga T., Yoshimoto T., Kondo H.
Brain Res. Mol. Brain Res. 27:355-355(1994) [PubMed] [Europe PMC] [Abstract]
[3]"Cloning and expression of a group IV cytosolic Ca2+-dependent phospholipase A2 from rat pancreatic islets. Comparison of the expressed activity with that of an islet group VI cytosolic Ca2+-independent phospholipase A2."
Ma Z., Ramanadham S., Hu Z., Turk J.
Biochim. Biophys. Acta 1391:384-400(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Pancreatic islet.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S77829 mRNA. Translation: AAB33847.1.
U38376 mRNA. Translation: AAC21591.1.
UniGeneRn.10162.

3D structure databases

ProteinModelPortalP50393.
SMRP50393. Positions 13-721.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000003630.

PTM databases

PhosphoSiteP50393.

Proteomic databases

PRIDEP50393.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:67366. rat.

Organism-specific databases

RGD67366. Pla2g4a.

Phylogenomic databases

eggNOGNOG257248.
HOGENOMHOG000115420.
HOVERGENHBG053479.
InParanoidP50393.
PhylomeDBP50393.

Gene expression databases

GenevestigatorP50393.

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

PROP50393.

Entry information

Entry namePA24A_RAT
AccessionPrimary (citable) accession number: P50393
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 108 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