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Protein

Phospholipase A2

Gene

Pla2g1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Calcium; via carbonyl oxygenBy similarity1
Metal bindingi52Calcium; via carbonyl oxygenBy similarity1
Metal bindingi54Calcium; via carbonyl oxygenBy similarity1
Active sitei701
Metal bindingi71CalciumBy similarity1
Active sitei1211

GO - Molecular functioni

  • calcium-dependent phospholipase A2 activity Source: RGD
  • calcium ion binding Source: Ensembl
  • phospholipase A2 activity Source: BHF-UCL
  • receptor binding Source: BHF-UCL

GO - Biological processi

  • antibacterial humoral response Source: Ensembl
  • arachidonic acid secretion Source: InterPro
  • cellular response to insulin stimulus Source: BHF-UCL
  • defense response to Gram-positive bacterium Source: Ensembl
  • fatty acid biosynthetic process Source: BHF-UCL
  • glucose transport Source: BHF-UCL
  • innate immune response in mucosa Source: Ensembl
  • multicellular organism lipid catabolic process Source: Ensembl
  • phosphatidylcholine metabolic process Source: Ensembl
  • phospholipid metabolic process Source: RGD
  • positive regulation of DNA replication Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-1482788. Acyl chain remodelling of PC.
R-RNO-1482801. Acyl chain remodelling of PS.
R-RNO-1482839. Acyl chain remodelling of PE.
R-RNO-1482922. Acyl chain remodelling of PI.
R-RNO-1482925. Acyl chain remodelling of PG.
R-RNO-1483166. Synthesis of PA.

Chemistry databases

SwissLipidsiSLP:000001183.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A2 (EC:3.1.1.4)
Alternative name(s):
Group IB phospholipase A2
Phosphatidylcholine 2-acylhydrolase 1B
Gene namesi
Name:Pla2g1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi61949. Pla2g1b.

Subcellular locationi

  • Secreted

  • Note: secreted from pancreatic acinar cells in its inactive form.By similarity

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • extracellular space Source: Ensembl
  • secretory granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5016.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15Add BLAST15
PropeptideiPRO_000002274716 – 22Activation peptide1 Publication7
ChainiPRO_000002274823 – 146Phospholipase A2Add BLAST124

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33 ↔ 99By similarity
Disulfide bondi49 ↔ 146By similarity
Disulfide bondi51 ↔ 67By similarity
Disulfide bondi66 ↔ 127By similarity
Disulfide bondi73 ↔ 120By similarity
Disulfide bondi83 ↔ 113By similarity
Disulfide bondi106 ↔ 118By similarity

Post-translational modificationi

Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically (By similarity).By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Zymogen

Proteomic databases

PaxDbiP04055.
PRIDEiP04055.

Expressioni

Gene expression databases

BgeeiENSRNOG00000001153.
GenevisibleiP04055. RN.

Interactioni

Subunit structurei

Monomer or homodimer. The inactive pro-form is a homotrimer (By similarity).By similarity

GO - Molecular functioni

  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001525.

Chemistry databases

BindingDBiP04055.

Structurei

3D structure databases

ProteinModelPortaliP04055.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP04055.
KOiK01047.
OMAiWQFRKMI.
OrthoDBiEOG091G0UZ3.
PhylomeDBiP04055.
TreeFamiTF319283.

Family and domain databases

CDDicd00125. PLA2c. 1 hit.
Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04055-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLLLAALL TAGVTAHSIS TRAVWQFRNM IKCTIPGSDP LREYNNYGCY
60 70 80 90 100
CGLGGSGTPV DDLDRCCQTH DHCYNQAKKL ESCKFLIDNP YTNTYSYKCS
110 120 130 140
GNVITCSDKN NDCESFICNC DRQAAICFSK VPYNKEYKDL DTKKHC
Length:146
Mass (Da):16,424
Last modified:November 1, 1986 - v1
Checksum:i7EC4F7A491B913D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00036 mRNA. Translation: BAA00024.1.
PIRiA92008. PSRT.
RefSeqiNP_113773.1. NM_031585.1.
XP_017453797.1. XM_017598308.1.
UniGeneiRn.4283.

Genome annotation databases

EnsembliENSRNOT00000001525; ENSRNOP00000001525; ENSRNOG00000001153.
GeneIDi29526.
KEGGirno:29526.
UCSCiRGD:61949. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00036 mRNA. Translation: BAA00024.1.
PIRiA92008. PSRT.
RefSeqiNP_113773.1. NM_031585.1.
XP_017453797.1. XM_017598308.1.
UniGeneiRn.4283.

3D structure databases

ProteinModelPortaliP04055.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001525.

Chemistry databases

BindingDBiP04055.
ChEMBLiCHEMBL5016.
SwissLipidsiSLP:000001183.

Proteomic databases

PaxDbiP04055.
PRIDEiP04055.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001525; ENSRNOP00000001525; ENSRNOG00000001153.
GeneIDi29526.
KEGGirno:29526.
UCSCiRGD:61949. rat.

Organism-specific databases

CTDi5319.
RGDi61949. Pla2g1b.

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiP04055.
KOiK01047.
OMAiWQFRKMI.
OrthoDBiEOG091G0UZ3.
PhylomeDBiP04055.
TreeFamiTF319283.

Enzyme and pathway databases

ReactomeiR-RNO-1482788. Acyl chain remodelling of PC.
R-RNO-1482801. Acyl chain remodelling of PS.
R-RNO-1482839. Acyl chain remodelling of PE.
R-RNO-1482922. Acyl chain remodelling of PI.
R-RNO-1482925. Acyl chain remodelling of PG.
R-RNO-1483166. Synthesis of PA.

Miscellaneous databases

PROiP04055.

Gene expression databases

BgeeiENSRNOG00000001153.
GenevisibleiP04055. RN.

Family and domain databases

CDDicd00125. PLA2c. 1 hit.
Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA21B_RAT
AccessioniPrimary (citable) accession number: P04055
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: November 30, 2016
This is version 138 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.