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Protein

Cytosolic phospholipase A2

Gene

pla2g4a

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulationi

Stimulated by agonists such as ATP, EGF, thrombin and bradykinin as well as by cytosolic Ca2+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Calcium 1By similarity
Metal bindingi34 – 341Calcium 2By similarity
Metal bindingi35 – 351Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi37 – 371Calcium 1By similarity
Metal bindingi37 – 371Calcium 2By similarity
Metal bindingi59 – 591Calcium 1By similarity
Metal bindingi87 – 871Calcium 2By similarity
Metal bindingi88 – 881Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi89 – 891Calcium 2By similarity
Active sitei223 – 2231NucleophileBy similarity
Active sitei540 – 5401Proton acceptorBy similarity

GO - Molecular functioni

  1. lysophospholipase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. phospholipase A2 activity Source: UniProtKB-EC

GO - Biological processi

  1. ovarian follicle development Source: ZFIN
  2. phospholipid catabolic process Source: InterPro
  3. response to wounding Source: ZFIN
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic phospholipase A2
Short name:
cPLA2
Alternative name(s):
Phospholipase A2 group IVA
Including the following 2 domains:
Phospholipase A2 (EC:3.1.1.4)
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Lysophospholipase (EC:3.1.1.5)
Gene namesi
Name:pla2g4a
Synonyms:cpla2, pla2g4
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-990415-45. pla2g4aa.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 741741Cytosolic phospholipase A2PRO_0000187265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei498 – 4981Phosphoserine; by MAPKBy similarity

Post-translational modificationi

Activated by phosphorylation on a serine residue.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP50392.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000038013.

Structurei

3D structure databases

ProteinModelPortaliP50392.
SMRiP50392. Positions 7-710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 100100C2PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 729598PLA2cPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 172172Phospholipid bindingCuratedAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PLA2c domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG257248.
HOGENOMiHOG000115420.
HOVERGENiHBG053479.
InParanoidiP50392.
KOiK16342.
PhylomeDBiP50392.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50392-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNIIVEHQY SHRLKLTVVR AENVTKGAFG DLLDTPDPYV ELSVPTTPES
60 70 80 90 100
RKRTRHINND INPKWNETFE FILDPNQSNV LEVTLMDANY VMDETLGTAK
110 120 130 140 150
YSLSKLKVAQ MEHVTLSIGK TTKVFLDLLL EVCASTDLRF SMTLCDQEKL
160 170 180 190 200
FMQTRRDRVM LSIKKLLKME NPRFLPSSPR EVPTIAILGS GGGFRAMVGF
210 220 230 240 250
SGVMKALYES GVFDCATYVA GLSGSTWYMS MLYSHPEFPA KGPGDINKEL
260 270 280 290 300
MNRVSNNPLK LLLPQNINRY VKALWKKKSA GQPVTFTDIF GMLIGETLIP
310 320 330 340 350
GRMNIKLSSL KGKINEGQSP LPLFTCLHVK PDVSELMFAD WVEFSPYEIG
360 370 380 390 400
MAKYGTFMSP GLFGSKFFMG SVVKQYEENP LHFLMGVWGS AFSILFNRVL
410 420 430 440 450
GVKETTSSST MEEELEQIKP EHIVGDDSAD NEEETQRGGT ESADAEDERQ
460 470 480 490 500
RHAQASWVQR MLTSIMGDTT LFTTREGRAG KVHNFMLGLN LNSTLPFSPF
510 520 530 540 550
SGITHQTSLE EEVDAVTDPD EFERIYEPLD VKSKKIHVVD SGLTFNLPYP
560 570 580 590 600
LILRCQRGVD LIISFDFSAR PSDSSPPFKE LLLAEKWARM NKLPFPKIDS
610 620 630 640 650
KVFDREGLKE CYVFKPAKGD KNCPTIIHFV LANINFRNFK APGVPRDSDK
660 670 680 690 700
DIEFGDFDIF DEPASPYSTF NFKYNNQAFK RLHDLMEFNT LNNIEVIKEA
710 720 730 740
IKDSILLRRE NPARCSVSLS LSEIENKKFL KRDNSIAKRP T
Length:741
Mass (Da):83,809
Last modified:September 30, 1996 - v1
Checksum:i34896B1A8364A9D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10330 mRNA. Translation: AAA53229.1.
PIRiB54908.
RefSeqiNP_571370.1. NM_131295.2.
UniGeneiDr.20961.

Genome annotation databases

GeneIDi30554.
KEGGidre:30554.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10330 mRNA. Translation: AAA53229.1.
PIRiB54908.
RefSeqiNP_571370.1. NM_131295.2.
UniGeneiDr.20961.

3D structure databases

ProteinModelPortaliP50392.
SMRiP50392. Positions 7-710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000038013.

Proteomic databases

PRIDEiP50392.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi30554.
KEGGidre:30554.

Organism-specific databases

CTDi30554.
ZFINiZDB-GENE-990415-45. pla2g4aa.

Phylogenomic databases

eggNOGiNOG257248.
HOGENOMiHOG000115420.
HOVERGENiHBG053479.
InParanoidiP50392.
KOiK16342.
PhylomeDBiP50392.

Miscellaneous databases

NextBioi20806930.
PROiP50392.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR000008. C2_dom.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiPA24A_DANRE
AccessioniPrimary (citable) accession number: P50392
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: September 30, 1996
Last modified: January 6, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.