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A4IFJ5 (PA24A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length749 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 By similarity.

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+ By similarity.

Subunit structure

Interacts with KAT5 By similarity.

Subcellular location

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

Tissue specificity

Detected in granulosa cells after stimulation with chorionic gonadotropin (at protein level). Ref.1

Developmental stage

Highly expressed in granulosa cells of ovulatory follicles. Detected at low levels in granulosa cells during the rest of the estrous cycle.

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_processarachidonic acid secretion

Inferred from electronic annotation. Source: Ensembl

cellular response to antibiotic

Inferred from electronic annotation. Source: Ensembl

icosanoid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   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 sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 749749Cytosolic phospholipase A2
PRO_0000345133

Regions

Domain5 – 106102C2
Domain140 – 740601PLA2c
Region1 – 178178Phospholipid binding By similarity

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 conflict5811S → G in AAR17479. Ref.1

Sequences

Sequence LengthMass (Da)Tools
A4IFJ5 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: C44BF7E4C40959BF

FASTA74985,350
        10         20         30         40         50         60 
MSFIDPYQHI IVEHHYSHKF TVVVLRATKV TKGTFGDMLD TPDPYVELFI SSTPDSRKRT 

        70         80         90        100        110        120 
RHFNNDINPV WNETFEFILD PNQENILEIT LMDANYVMDE TLGTTTFPIS SMKVGEKKQV 

       130        140        150        160        170        180 
PFIFNQVTEM ILEMSLEVCS SPDLRFSMAL CDQEKAFRQQ RKENIKENMK KLLGPKNSEG 

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

       250        260        270        280        290        300 
PDFPEKGPEE INKELMKNVS HNPLLLLTPQ KIKRYVESLW RKKSSGQPVT FTDIFGMLIG 

       310        320        330        340        350        360 
ETLIHNRMNT TLSSLKEKVN TGQCPLPLFT CLHVKPDVSE LMFADWVEFS PFEIGMAKYG 

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

       430        440        450        460        470        480 
LENITAKHIV SNDSSDSDDE SQGPKGTEHE EAEREYQNDN QASWVQRMLM ALVSDSALFN 

       490        500        510        520        530        540 
TREGRAGKVH NFMLGLNLNT SYPMSPLRDF TMQESLDEDE LDAAVADPDE FEQIYEPLDV 

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

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

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

       730        740 
QNPSRCSVSL SSVEARRFFN KEFLSKPTA 

« Hide

References

« Hide 'large scale' references
[1]"Expression of phospholipase A2 group IVA (PLA2G4A) is upregulated by human chorionic gonadotropin in bovine granulosa cells of ovulatory follicles."
Diouf M.N., Sayasith K., Lefebvre R., Silversides D.W., Sirois J., Lussier J.G.
Biol. Reprod. 74:1096-1103(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Tissue: Follicular cell.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY363688 mRNA. Translation: AAR17479.1.
BC134610 mRNA. Translation: AAI34611.1.
RefSeqNP_001069332.1. NM_001075864.1.
UniGeneBt.69446.

3D structure databases

ProteinModelPortalA4IFJ5.
SMRA4IFJ5. Positions 13-721.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000017685.

Chemistry

ChEMBLCHEMBL2304401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017685; ENSBTAP00000017685; ENSBTAG00000013298.
GeneID525072.
KEGGbta:525072.

Organism-specific databases

CTD5321.

Phylogenomic databases

eggNOGNOG257248.
GeneTreeENSGT00550000074489.
HOGENOMHOG000115420.
HOVERGENHBG053479.
InParanoidA4IFJ5.
KOK16342.
OMAETLIHNR.
OrthoDBEOG73V6JM.
TreeFamTF325228.

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

NextBio20874091.

Entry information

Entry namePA24A_BOVIN
AccessionPrimary (citable) accession number: A4IFJ5
Secondary accession number(s): Q1XD55
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 49 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