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P49147 (PA24A_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

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

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 on a serine residue By similarity.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PLA2c domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 748748Cytosolic phospholipase A2
PRO_0000187266

Regions

Domain5 – 106102C2
Domain138 – 740603PLA2c
Region1 – 178178Phospholipid binding

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 residue5051Phosphoserine; by MAPK By similarity

Sequences

Sequence LengthMass (Da)Tools
P49147 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 996A5256CA032F75

FASTA74884,979
        10         20         30         40         50         60 
MSFIDPYQHI VVEHQYSHVF TVTVRKATNV TKGAIGDMLD TPDPYVELFI PSAPDCRKRT 

        70         80         90        100        110        120 
KHFNNDVNPV WNETFEFILD PNQDNVLEVT LMDANYVMDE TLGMATFPIS SLKLGEKKEV 

       130        140        150        160        170        180 
QLTFNNVTEM TLELSLEVCS STDLRFSMAL CDEEKKFRQQ RKDNIMQSMK SFLGEENSKN 

       190        200        210        220        230        240 
LTTSRDVPVI AVLGSGGGFR AMVGFAGVMK ALYESGVLDC ATYIAGLSGS TWYMSTLYSH 

       250        260        270        280        290        300 
PDFPEKGPKE INQELMNSVS HNPLLLLTPQ KVKRYIEALW NKKSSGQPVT FTDIFGMLIG 

       310        320        330        340        350        360 
ETLIHNRMDT TLSDMKEKVS EAQCALPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG 

       370        380        390        400        410        420 
TFMSPDLFGS KFFMGTVVKK YSENPLHFLM GVWGSAFSIL FNRVLGVSNS QNKGPTMEEE 

       430        440        450        460        470        480 
LENIRLKHLV SNDSSDSEDE SQHPKGTENS EANEEYQNSS QESWVQRMLM ALVGDSALFN 

       490        500        510        520        530        540 
TREGRAGKVH NFMLGLNLNS CYPLSPLADL LTQESVEEDE LDAAVADPDE FERIYEPLDV 

       550        560        570        580        590        600 
KSKKIHIVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEI LLAEKWAKMN 

       610        620        630        640        650        660 
KLPFPKIDPN VFDREGLKEC YVFKPKDTSS EKDCPTIIHF VLANINFRKY KAPGLPRESK 

       670        680        690        700        710        720 
EEKDFADFDI FDDPNTPFST FNFQYPNEAF KRLHDLMEFN TLNNLDVIKQ AMMESIEYRK 

       730        740 
ENPSRCSVSL SSVEARRFFN KNNLNNHT 

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References

[1]"Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain."
Nalefski E.A., Sultzman L.A., Martin D.M., Kriz R.W., Towler P.S., Knopf J.L., Clark J.D.
J. Biol. Chem. 269:18239-18249(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10329 mRNA. Translation: AAA53228.1.
PIRI50699.
RefSeqNP_990754.1. NM_205423.1.
UniGeneGga.3723.

3D structure databases

ProteinModelPortalP49147.
SMRP49147. Positions 13-721.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000038517.

Proteomic databases

PaxDbP49147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000008121; ENSGALP00000008107; ENSGALG00000005065.
GeneID396394.
KEGGgga:396394.

Organism-specific databases

CTD5321.

Phylogenomic databases

eggNOGNOG257248.
GeneTreeENSGT00550000074489.
HOGENOMHOG000115420.
HOVERGENHBG053479.
KOK16342.
OrthoDBEOG73V6JM.
PhylomeDBP49147.

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

NextBio20816436.
PROP49147.

Entry information

Entry namePA24A_CHICK
AccessionPrimary (citable) accession number: P49147
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 96 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