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Q5R8A5 (PA24A_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length749 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 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 749749Cytosolic phospholipase A2
PRO_0000345134

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

Sequences

Sequence LengthMass (Da)Tools
Q5R8A5 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 70C1D0C9E983BBD4

FASTA74985,168
        10         20         30         40         50         60 
MSFIDPYQHI IVEHQYSHKF TVVVLCATKV TKGAFGDMLD TPDPYVELFI STTPDSRKRT 

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

       130        140        150        160        170        180 
PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG 

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

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

       310        320        330        340        350        360 
ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG 

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

       430        440        450        460        470        480 
LENITTKHIV SNDSSDSDDE SHEPKGTENE DAGSDYQSDN QASWIHRMIM ALVSDSALFN 

       490        500        510        520        530        540 
TREGRAGKVH NFMLGLNLNT SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV 

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

       610        620        630        640        650        660 
KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY KAPGVPRETE 

       670        680        690        700        710        720 
EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN TLNNIDVIKE AMVESIEYRR 

       730        740 
QNPSRCSVSL SNVEARRFFN KEFLSKPKA 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859848 mRNA. Translation: CAH92005.1.
RefSeqNP_001126164.1. NM_001132692.1.
UniGenePab.12757.

3D structure databases

ProteinModelPortalQ5R8A5.
SMRQ5R8A5. Positions 13-721.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173125.
KEGGpon:100173125.

Organism-specific databases

CTD5321.

Phylogenomic databases

HOGENOMHOG000115420.
HOVERGENHBG053479.
InParanoidQ5R8A5.
KOK16342.

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...

Entry information

Entry namePA24A_PONAB
AccessionPrimary (citable) accession number: Q5R8A5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 48 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