Reviewed,
UniProtKB/Swiss-Prot P04055 (PA21B_RAT)
Last modified
February 9, 2010.
Version 87.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Phospholipase A2 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase 1B Group IB phospholipase A2 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| 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. |
| Catalytic activity | Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the phospholipase A2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellular response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB fatty acid biosynthetic processInferred from direct assay. Source: UniProtKB glucose transportInferred from sequence or structural similarity. Source: UniProtKB positive regulation of DNA replicationInferred from direct assay. Source: UniProtKB |
| Cellular component | secretory granule Inferred from direct assay. Source: RGD |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-dependent phospholipase A2 activityInferred from direct assay. Source: RGD cell surface bindingInferred from direct assay. Source: UniProtKB receptor bindingInferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
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: 3754861] [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: 2909239] [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: 6501264] [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. |
| UniGene | Rn.4283 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P04055. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000001525; ENSRNOP00000001525; ENSRNOG00000001153; Rattus norvegicus. [Genome view] |
| GeneID | 29526. |
| KEGG | rno:29526. |
| UCSC | NM_031585. rat. |
Organism-specific databases | |
| CTD | 29526. |
| RGD | 61949. Pla2g1b. |
Phylogenomic databases | |
| eggNOG | roNOG16901. |
| HOVERGEN | P04055. |
| InParanoid | P04055. |
| OMA | AKKLDSC. |
| OrthoDB | EOG98GZPW. |
| PhylomeDB | P04055. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.4. 248. |
Gene expression databases | |
| ArrayExpress | P04055. |
| Genevestigator | P04055. |
| GermOnline | ENSRNOG00000001153. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR016090. Phospholipase_A2. IPR013090. Phospholipase_A2_AS. IPR001211. Phospholipase_A2_euk. [Graphical view] |
| Gene3D | G3DSA:1.20.90.10. Phospholipase_A2. 1 hit. |
| PANTHER | PTHR11716. Phospholipase_A2. 1 hit. |
| Pfam | PF00068. Phospholip_A2_1. 1 hit. [Graphical view] |
| PRINTS | PR00389. PHPHLIPASEA2. |
| SMART | SM00085. PA2c. 1 hit. [Graphical view] |
| PROSITE | PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 609488. |
Entry information
| Entry name | PA21B_RAT | ||||||||
| Accession | Primary (citable) accession number: P04055 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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