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P50392 (PA24A_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length741 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.

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 – 741741Cytosolic phospholipase A2
PRO_0000187265

Regions

Domain1 – 100100C2
Domain132 – 729598PLA2c
Region1 – 172172Phospholipid binding Probable

Sites

Active site2231Nucleophile By similarity
Active site5401Proton acceptor By similarity
Metal binding341Calcium 1 By similarity
Metal binding341Calcium 2 By similarity
Metal binding351Calcium 1; via carbonyl oxygen By similarity
Metal binding371Calcium 1 By similarity
Metal binding371Calcium 2 By similarity
Metal binding591Calcium 1 By similarity
Metal binding871Calcium 2 By similarity
Metal binding881Calcium 2; via carbonyl oxygen By similarity
Metal binding891Calcium 2 By similarity

Amino acid modifications

Modified residue4981Phosphoserine; by MAPK By similarity

Sequences

Sequence LengthMass (Da)Tools
P50392 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 34896B1A8364A9D4

FASTA74183,809
        10         20         30         40         50         60 
MSNIIVEHQY SHRLKLTVVR AENVTKGAFG DLLDTPDPYV ELSVPTTPES RKRTRHINND 

        70         80         90        100        110        120 
INPKWNETFE FILDPNQSNV LEVTLMDANY VMDETLGTAK YSLSKLKVAQ MEHVTLSIGK 

       130        140        150        160        170        180 
TTKVFLDLLL EVCASTDLRF SMTLCDQEKL FMQTRRDRVM LSIKKLLKME NPRFLPSSPR 

       190        200        210        220        230        240 
EVPTIAILGS GGGFRAMVGF SGVMKALYES GVFDCATYVA GLSGSTWYMS MLYSHPEFPA 

       250        260        270        280        290        300 
KGPGDINKEL MNRVSNNPLK LLLPQNINRY VKALWKKKSA GQPVTFTDIF GMLIGETLIP 

       310        320        330        340        350        360 
GRMNIKLSSL KGKINEGQSP LPLFTCLHVK PDVSELMFAD WVEFSPYEIG MAKYGTFMSP 

       370        380        390        400        410        420 
GLFGSKFFMG SVVKQYEENP LHFLMGVWGS AFSILFNRVL GVKETTSSST MEEELEQIKP 

       430        440        450        460        470        480 
EHIVGDDSAD NEEETQRGGT ESADAEDERQ RHAQASWVQR MLTSIMGDTT LFTTREGRAG 

       490        500        510        520        530        540 
KVHNFMLGLN LNSTLPFSPF SGITHQTSLE EEVDAVTDPD EFERIYEPLD VKSKKIHVVD 

       550        560        570        580        590        600 
SGLTFNLPYP LILRCQRGVD LIISFDFSAR PSDSSPPFKE LLLAEKWARM NKLPFPKIDS 

       610        620        630        640        650        660 
KVFDREGLKE CYVFKPAKGD KNCPTIIHFV LANINFRNFK APGVPRDSDK DIEFGDFDIF 

       670        680        690        700        710        720 
DEPASPYSTF NFKYNNQAFK RLHDLMEFNT LNNIEVIKEA IKDSILLRRE NPARCSVSLS 

       730        740 
LSEIENKKFL KRDNSIAKRP T 

« Hide

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].
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10330 mRNA. Translation: AAA53229.1.
PIRB54908.
RefSeqNP_571370.1. NM_131295.2.
UniGeneDr.20961.

3D structure databases

ProteinModelPortalP50392.
SMRP50392. Positions 7-710.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000038013.

Proteomic databases

PRIDEP50392.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID30554.
KEGGdre:30554.

Organism-specific databases

CTD30554.
ZFINZDB-GENE-990415-45. cpla2.

Phylogenomic databases

eggNOGNOG257248.
HOGENOMHOG000115420.
HOVERGENHBG053479.
KOK16342.
PhylomeDBP50392.

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

NextBio20806930.
PROP50392.

Entry information

Entry namePA24A_DANRE
AccessionPrimary (citable) accession number: P50392
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 107 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