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Protein

Cytosolic phospholipase A2

Gene

PLA2G4A

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

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+.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Calcium 1By similarity
Metal bindingi40 – 401Calcium 2By similarity
Metal bindingi41 – 411Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi43 – 431Calcium 1By similarity
Metal bindingi43 – 431Calcium 2By similarity
Metal bindingi65 – 651Calcium 1By similarity
Metal bindingi93 – 931Calcium 2By similarity
Metal bindingi94 – 941Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi95 – 951Calcium 2By similarity
Active sitei228 – 2281NucleophileBy similarity
Active sitei548 – 5481Proton acceptorBy similarity

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. lysophospholipase activity Source: UniProtKB-EC
  4. phospholipase A2 activity Source: UniProtKB-EC

GO - Biological processi

  1. phospholipid catabolic process Source: InterPro
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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

  1. Cytoplasm By similarity
  2. Cytoplasmic vesicle By similarity

  3. 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 – 748748Cytosolic phospholipase A2PRO_0000345135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei268 – 2681PhosphothreonineBy similarity
Modified residuei437 – 4371PhosphoserineBy similarity
Modified residuei505 – 5051Phosphoserine; by MAPKBy similarity
Modified residuei726 – 7261PhosphoserineBy similarity
Modified residuei728 – 7281PhosphoserineBy similarity

Post-translational modificationi

Activated by phosphorylation at both Ser-505 and Ser-726.By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with KAT5.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000012590.

Structurei

3D structure databases

ProteinModelPortaliQ9TT38.
SMRiQ9TT38. Positions 13-720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 106102C2PROSITE-ProRule annotationAdd
BLAST
Domaini138 – 739602PLA2cPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 178178Phospholipid bindingBy similarityAdd
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.
InParanoidiQ9TT38.
KOiK16342.

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.

Q9TT38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI
60 70 80 90 100
ATTPDSRKRT RHFNNDINPV WNEAFEFILD PNQGNVLEIT LMDANYVMDE
110 120 130 140 150
TLGTATFPVS SMKVGEKKEV PFIFNQVTEM ILEMSLEVCS SPDLRFSMAL
160 170 180 190 200
CDQEKAFRQQ RKENIKENMR KLLGPKKSEG LYSTRDVPVV AILGSGGGFR
210 220 230 240 250
AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH PDFPEKGPQE
260 270 280 290 300
INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
310 320 330 340 350
ETLIHNRMHT TLSSLKEKVS SAQCPLPLFT CLHVKPDVSE LMFADWVEFS
360 370 380 390 400
PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL
410 420 430 440 450
FNRVLGVSGS HNKGSTMEEE LENITAKHIV SNDSSDSDDE SQEPKGTEGE
460 470 480 490 500
DAEREYQNDH QASWVHRMLM ALVSDSALFN TREGRAGKVH NFMLGLNLNT
510 520 530 540 550
SYPLSPLRDF TQESFDDDEL DAAVADPDEF ERIYEPLDVK SKKIHVVDSG
560 570 580 590 600
LTFNLPYPLI LRPQRGVDLI ISFDFSARPS DTSPPFKELL LAEKWAKMNK
610 620 630 640 650
LPFPKIDPYV FDREGLKECY VFKPKNPDVE KDCPIIIHFV LANINFRKYK
660 670 680 690 700
SPGVPRETKE EKEIADFDIF DDPESPFSTF NFQYPNQAFK RLHDLMYFNT
710 720 730 740
LNNIDVIKDA MVESIEYRRQ NPSRCSVSLS NVEARRFFNK EFLSKPTA
Length:748
Mass (Da):85,235
Last modified:May 1, 2000 - v1
Checksum:i7661A3EFC41FF668
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF204923 mRNA. Translation: AAF15299.1.
RefSeqiNP_001075541.1. NM_001082072.1.
UniGeneiOcu.2401.

Genome annotation databases

GeneIDi100008748.
KEGGiocu:100008748.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF204923 mRNA. Translation: AAF15299.1.
RefSeqiNP_001075541.1. NM_001082072.1.
UniGeneiOcu.2401.

3D structure databases

ProteinModelPortaliQ9TT38.
SMRiQ9TT38. Positions 13-720.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000012590.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008748.
KEGGiocu:100008748.

Organism-specific databases

CTDi5321.

Phylogenomic databases

eggNOGiNOG257248.
HOGENOMiHOG000115420.
HOVERGENiHBG053479.
InParanoidiQ9TT38.
KOiK16342.

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. "Molecular cloning of cDNA coding for phospholipase A2."
    Al-Khalili O.K., Eaton D.C.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: New Zealand white.
    Tissue: Heart.

Entry informationi

Entry nameiPA24A_RABIT
AccessioniPrimary (citable) accession number: Q9TT38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: May 1, 2000
Last modified: March 4, 2015
This is version 70 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.