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Q9TT38 (PA24A_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length748 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-726 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_0000345135

Regions

Domain5 – 106102C2
Domain138 – 739602PLA2c
Region1 – 178178Phospholipid binding By similarity

Sites

Active site2281Nucleophile By similarity
Active site5481Proton 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 residue7261Phosphoserine By similarity
Modified residue7281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9TT38 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7661A3EFC41FF668

FASTA74885,235
        10         20         30         40         50         60 
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI ATTPDSRKRT 

        70         80         90        100        110        120 
RHFNNDINPV WNEAFEFILD PNQGNVLEIT LMDANYVMDE TLGTATFPVS SMKVGEKKEV 

       130        140        150        160        170        180 
PFIFNQVTEM ILEMSLEVCS SPDLRFSMAL CDQEKAFRQQ RKENIKENMR KLLGPKKSEG 

       190        200        210        220        230        240 
LYSTRDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH 

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

       310        320        330        340        350        360 
ETLIHNRMHT TLSSLKEKVS SAQCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG 

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

       430        440        450        460        470        480 
LENITAKHIV SNDSSDSDDE SQEPKGTEGE DAEREYQNDH QASWVHRMLM ALVSDSALFN 

       490        500        510        520        530        540 
TREGRAGKVH NFMLGLNLNT SYPLSPLRDF TQESFDDDEL DAAVADPDEF ERIYEPLDVK 

       550        560        570        580        590        600 
SKKIHVVDSG LTFNLPYPLI LRPQRGVDLI ISFDFSARPS DTSPPFKELL LAEKWAKMNK 

       610        620        630        640        650        660 
LPFPKIDPYV FDREGLKECY VFKPKNPDVE KDCPIIIHFV LANINFRKYK SPGVPRETKE 

       670        680        690        700        710        720 
EKEIADFDIF DDPESPFSTF NFQYPNQAFK RLHDLMYFNT LNNIDVIKDA MVESIEYRRQ 

       730        740 
NPSRCSVSLS NVEARRFFNK EFLSKPTA 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF204923 mRNA. Translation: AAF15299.1.
RefSeqNP_001075541.1. NM_001082072.1.
UniGeneOcu.2401.

3D structure databases

ProteinModelPortalQ9TT38.
SMRQ9TT38. Positions 13-720.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000012590.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008748.

Phylogenomic databases

eggNOGNOG257248.
HOGENOMHOG000115420.
HOVERGENHBG053479.

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_RABIT
AccessionPrimary (citable) accession number: Q9TT38
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 65 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