Reviewed,
UniProtKB/Swiss-Prot P06596 (PA21B_CANFA)
Last modified
June 16, 2009.
Version 79.
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 | ||
| Gene names |
| ||
| Organism | Canis familiaris (Dog) | ||
| Taxonomic identifier | 9615 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis |
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 transcript 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 |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 15 | 15 | |||||||||
| Propeptide | 16 – 22 | 7 | PRO_0000022733 | ||||||||
| Chain | 23 – 146 | 124 | Phospholipase A2 | PRO_0000022734 | |||||||
Sites | |||||||||||
| Active site | 70 | 1 | By similarity | ||||||||
| Active site | 121 | 1 | By similarity | ||||||||
| 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] | "Isolation and sequence of the canine pancreatic phospholipase A2 gene." Kerfelec B., Laforge K.S., Vasiloudes P., Puigserver A., Scheele G.A. Eur. J. Biochem. 190:299-304(1990) [PubMed: 2142076] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Primary structures of canine pancreatic lipase and phospholipase A2 messenger RNAs." Kerfelec B., Laforge K.S., Puigserver A., Scheele G.A. Pancreas 1:430-437(1986) [PubMed: 3562437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| D00035 mRNA. Translation: BAA00023.1. M35301 mRNA. Translation: AAA30883.1. | |
| PIR | PSDG. S11316. |
| RefSeq | NP_001003320.1. |
| UniGene | Cfa.40293 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HN4 based on UniProtKB P00592. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSCAFG00000010263. Canis familiaris. [Contig view] |
| GeneID | 404011. |
| KEGG | cfa:404011. |
Phylogenomic databases | |
| HOVERGEN | P06596. |
| OMA | P06596. AKKLDSC. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.4. 463. |
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_CANFA | ||||||||
| Accession | Primary (citable) accession number: P06596 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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