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P04055 (PA21B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. 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:
Phospholipase A2

EC=3.1.1.4
Alternative name(s):
Group IB phospholipase A2
Phosphatidylcholine 2-acylhydrolase 1B
Gene names
Name:Pla2g1b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

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

Subcellular location

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

Post-translational modification

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

Sequence similarities

Belongs to the phospholipase A2 family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMAutocatalytic cleavage
Disulfide bond
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to insulin stimulus

Inferred from sequence or structural similarity PubMed 1918029. Source: BHF-UCL

fatty acid biosynthetic process

Inferred from direct assay PubMed 1918029. Source: BHF-UCL

glucose transport

Inferred from sequence or structural similarity PubMed 1918029. Source: BHF-UCL

multicellular organismal lipid catabolic process

Inferred from electronic annotation. Source: Compara

phosphatidylcholine metabolic process

Inferred from electronic annotation. Source: Compara

phospholipid metabolic process

Inferred from direct assay PubMed 9487151. Source: RGD

positive regulation of DNA replication

Inferred from direct assay PubMed 1918029. Source: BHF-UCL

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Compara

secretory granule

Inferred from direct assay PubMed 9487151. Source: RGD

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipase A2 activity

Inferred from direct assay PubMed 9487151. Source: RGD

cell surface binding

Inferred from direct assay PubMed 1918029. Source: BHF-UCL

receptor binding

Inferred from direct assay PubMed 1918029. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Propeptide16 – 227Activation peptide
PRO_0000022747
Chain23 – 146124Phospholipase A2
PRO_0000022748

Sites

Active site701
Active site1211
Metal binding501Calcium; via carbonyl oxygen By similarity
Metal binding521Calcium; via carbonyl oxygen By similarity
Metal binding541Calcium; via carbonyl oxygen By similarity
Metal binding711Calcium By similarity

Amino acid modifications

Disulfide bond33 ↔ 99 By similarity
Disulfide bond49 ↔ 146 By similarity
Disulfide bond51 ↔ 67 By similarity
Disulfide bond66 ↔ 127 By similarity
Disulfide bond73 ↔ 120 By similarity
Disulfide bond83 ↔ 113 By similarity
Disulfide bond106 ↔ 118 By similarity

Sequences

Sequence LengthMass (Da)Tools
P04055 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 7EC4F7A491B913D0

FASTA14616,424
        10         20         30         40         50         60 
MKLLLLAALL TAGVTAHSIS TRAVWQFRNM IKCTIPGSDP LREYNNYGCY CGLGGSGTPV 

        70         80         90        100        110        120 
DDLDRCCQTH DHCYNQAKKL ESCKFLIDNP YTNTYSYKCS GNVITCSDKN NDCESFICNC 

       130        140 
DRQAAICFSK VPYNKEYKDL DTKKHC 

« Hide

References

[1]"Dog and rat pancreatic phospholipases A2: complete amino acid sequences deduced from complementary DNAs."
Ohara O., Tamaki M., Nakamura E., Tsuruta Y., Fujii Y., Shin M., Teraoka H., Okamoto M.
J. Biochem. 99:733-739(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Presence of pancreatic-type phospholipase A2 mRNA in rat gastric mucosa and lung."
Sakata T., Nakamura E., Tsuruta Y., Tamaki M., Teraoka H., Tojo H., Ono T., Okamoto M.
Biochim. Biophys. Acta 1007:124-126(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Rat pancreatic phospholipase A2: purification, characterization, and N-terminal amino acid sequence."
Ono T., Tojo H., Inoue K., Kagamiyama H., Yamano T., Okamoto M.
J. Biochem. 96:785-792(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-54.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00036 mRNA. Translation: BAA00024.1.
IPIIPI00192334.
PIRPSRT. A92008.
RefSeqNP_113773.1. NM_031585.1.
UniGeneRn.4283.

3D structure databases

ProteinModelPortalP04055.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000001525.

Proteomic databases

PaxDbP04055.
PRIDEP04055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001525; ENSRNOP00000001525; ENSRNOG00000001153.
GeneID29526.
KEGGrno:29526.
UCSCRGD:61949. rat.

Organism-specific databases

CTD5319.
RGD61949. Pla2g1b.

Phylogenomic databases

eggNOGNOG290764.
GeneTreeENSGT00690000101719.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidP04055.
KOK01047.
OMANKECEAF.
OrthoDBEOG4GHZQJ.

Gene expression databases

GenevestigatorP04055.
GermOnlineENSRNOG00000001153. Rattus norvegicus.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERPTHR11716. PTHR11716. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. PhospholipaseA2. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP04055.
ChEMBLCHEMBL5016.
NextBio609488.

Entry information

Entry namePA21B_RAT
AccessionPrimary (citable) accession number: P04055
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: May 1, 2013
This is version 111 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