P04055 (PA21B_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 111.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Phospholipase A2 EC=3.1.1.4 Alternative name(s): Group IB phospholipase A2 Phosphatidylcholine 2-acylhydrolase 1B | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 146 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 15 | 15 | |||||||||
| Propeptide | 16 – 22 | 7 | Activation peptide | PRO_0000022747 | |||||||
| Chain | 23 – 146 | 124 | Phospholipase A2 | PRO_0000022748 | |||||||
Sites | |||||||||||
| Active site | 70 | 1 | |||||||||
| Active site | 121 | 1 | |||||||||
| Metal binding | 50 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 52 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 54 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 71 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 33 ↔ 99 | By similarity | |||||||||
| Disulfide bond | 49 ↔ 146 | By similarity | |||||||||
| Disulfide bond | 51 ↔ 67 | By similarity | |||||||||
| Disulfide bond | 66 ↔ 127 | By similarity | |||||||||
| Disulfide bond | 73 ↔ 120 | By similarity | |||||||||
| Disulfide bond | 83 ↔ 113 | By similarity | |||||||||
| Disulfide bond | 106 ↔ 118 | By similarity | |||||||||
Sequences
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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. |
| IPI | IPI00192334. |
| PIR | PSRT. A92008. |
| RefSeq | NP_113773.1. NM_031585.1. |
| UniGene | Rn.4283. |
3D structure databases | |
| ProteinModelPortal | P04055. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000001525. |
Proteomic databases | |
| PaxDb | P04055. |
| PRIDE | P04055. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000001525; ENSRNOP00000001525; ENSRNOG00000001153. |
| GeneID | 29526. |
| KEGG | rno:29526. |
| UCSC | RGD:61949. rat. |
Organism-specific databases | |
| CTD | 5319. |
| RGD | 61949. Pla2g1b. |
Phylogenomic databases | |
| eggNOG | NOG290764. |
| GeneTree | ENSGT00690000101719. |
| HOGENOM | HOG000231749. |
| HOVERGEN | HBG008137. |
| InParanoid | P04055. |
| KO | K01047. |
| OMA | NKECEAF. |
| OrthoDB | EOG4GHZQJ. |
Gene expression databases | |
| Genevestigator | P04055. |
| GermOnline | ENSRNOG00000001153. Rattus norvegicus. |
Family and domain databases | |
| Gene3D | 1.20.90.10. 1 hit. |
| InterPro | IPR001211. PLipase_A2. IPR013090. PLipase_A2_AS. IPR016090. PLipase_A2_dom. [Graphical view] |
| PANTHER | PTHR11716. PTHR11716. 1 hit. |
| Pfam | PF00068. Phospholip_A2_1. 1 hit. [Graphical view] |
| PRINTS | PR00389. PHPHLIPASEA2. |
| SMART | SM00085. PA2c. 1 hit. [Graphical view] |
| SUPFAM | SSF48619. PhospholipaseA2. 1 hit. |
| PROSITE | PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | P04055. |
| ChEMBL | CHEMBL5016. |
| NextBio | 609488. |
Entry information
| Entry name | PA21B_RAT | ||||||||
| Accession | Primary (citable) accession number: P04055 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
