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Protein

Phospholipase A2

Gene

Pla2g1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism
LigandCalcium, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi61949 Pla2g1b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

  • signaling receptor binding Source: BHF-UCL

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001525

Chemistry databases

BindingDBiP04055

Structurei

3D structure databases

ProteinModelPortaliP04055
SMRiP04055
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
InterProiView protein in InterPro
IPR001211 PLipase_A2
IPR033112 PLipase_A2_Asp_AS
IPR016090 PLipase_A2_dom
IPR036444 PLipase_A2_dom_sf
IPR033113 PLipase_A2_His_AS
PANTHERiPTHR11716 PTHR11716, 1 hit
PfamiView protein in Pfam
PF00068 Phospholip_A2_1, 1 hit
PRINTSiPR00389 PHPHLIPASEA2
SMARTiView protein in SMART
SM00085 PA2c, 1 hit
SUPFAMiSSF48619 SSF48619, 1 hit
PROSITEiView protein in PROSITE
PS00119 PA2_ASP, 1 hit
PS00118 PA2_HIS, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPA21B_RAT
AccessioniPrimary (citable) accession number: P04055
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: May 23, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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