Reviewed,
UniProtKB/Swiss-Prot P00594 (PA21B_HORSE)
Last modified
June 16, 2009.
Version 68.
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 Group IB phospholipase A2 Cleaved into the following chain: 1- Recommended name: Phospholipase A2 isoform 2 | ||
| Gene names |
| ||
| Organism | Equus caballus (Horse) | ||
| Taxonomic identifier | 9796 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus |
Protein attributes
| Sequence length | 132 AA. |
| Sequence status | Fragment. |
| 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 |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase A2 activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 7 | 7 | Removed by trypsin Ref.2 | PRO_0000022737 | |||||||
| Chain | 8 – 132 | 125 | Phospholipase A2 Ref.2 Ref.3 | PRO_0000022738 | |||||||
| Chain | 10 – 132 | 123 | Phospholipase A2 isoform 2 | PRO_0000045893 | |||||||
Sites | |||||||||||
| Active site | 55 | 1 | By similarity | ||||||||
| Active site | 106 | 1 | By similarity | ||||||||
| Metal binding | 35 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 37 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 39 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 56 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 18 ↔ 84 | By similarity | |||||||||
| Disulfide bond | 34 ↔ 131 | By similarity | |||||||||
| Disulfide bond | 36 ↔ 52 | By similarity | |||||||||
| Disulfide bond | 51 ↔ 112 | By similarity | |||||||||
| Disulfide bond | 58 ↔ 105 | By similarity | |||||||||
| Disulfide bond | 68 ↔ 98 | By similarity | |||||||||
| Disulfide bond | 91 ↔ 103 | By similarity | |||||||||
Experimental info | |||||||||||
| Non-terminal residue | 1 | 1 | |||||||||
Sequences
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References
| [1] | "Isolation and properties of prophospholipase A2 and phospholipase A2 from horse pancreas and horse pancreatic juice." Evenberg A., Meyer H., Verheij H.M., de Haas G.H. Biochim. Biophys. Acta 491:265-274(1977) [PubMed: 849461] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7. Tissue: Pancreas. |
| [2] | "Amino acid sequence of phospholipase A2 from horse pancreas." Evenberg A., Meyer H., Gaastra W., Verheij H.M., de Haas G.H. J. Biol. Chem. 252:1189-1196(1977) [PubMed: 838712] [Abstract] Cited for: PROTEIN SEQUENCE OF 8-132, ACTIVE SITE. Tissue: Pancreas. |
| [3] | "The complete primary structure of phospholipase A2 from human pancreas." Verheij H.M., Westerman J., Sternby B., de Haas G.H. Biochim. Biophys. Acta 747:93-99(1983) [PubMed: 6349696] [Abstract] Cited for: SEQUENCE REVISION TO 131-132. |
Cross-references
Sequence databases | |
|---|---|
| PIR | PSHOA. A90615. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HN4 based on UniProtKB P00592. |
| SMR | P00594. Positions 1-126. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSECAG00000009152. Equus caballus. [Contig view] |
Phylogenomic databases | |
| HOVERGEN | P00594. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.4. 1464. |
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. |
| ProDom | PD000303. PhospholipaseA2. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00085. PA2c. 1 hit. [Graphical view] |
| PROSITE | PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PA21B_HORSE | ||||||||
| Accession | Primary (citable) accession number: P00594 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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