Reviewed,
UniProtKB/Swiss-Prot P0CAS5 (PA215_CRODU)
Last modified
September 22, 2009.
Version 4.
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 F15 EC=3.1.1.4 Alternative name(s): CdtF15 Phosphatidylcholine 2-acylhydrolase |
| Organism | Crotalus durissus terrificus (South American rattlesnake) |
| Taxonomic identifier | 8732 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus |
Protein attributes
| Sequence length | 122 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. Shows moderate neurotoxic activity in isolated mouse phrenic nerve diaphragm but shows high neurotoxic activity in a chick biventrer cervis preparation. Also shows a high bactericidal effect against both Gram-negative and Gram-positive bacteria. Ref.1 |
| Catalytic activity | Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. |
| Cofactor | Binds 1 calcium ion per subunit. Ref.1 |
| Enzyme regulation | Activated by heparin. Inhibited by its chaperone crotapotin. Ref.1 |
| Subunit structure | When this PA2 is associated with crotapotin (F5 or F7), it forms the crotoxin protein. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Sequence similarities | Belongs to the phospholipase A2 family. Group II subfamily. |
| Biophysicochemical properties | Kinetic parameters: KM=38.5 mM for 4-nitro-3-(octanoyloxy)benzoic acid Vmax=8.5 nmol/min/mg enzyme pH dependence: Optimum pH is 8.5. Temperature dependence: Optimum temperature is 18 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Secreted |
| Ligand | Calcium Metal-binding |
| Molecular function | Antibiotic Antimicrobial Hydrolase Neurotoxin Toxin |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW pathogenesisInferred 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 122 | 122 | Phospholipase A2 F15 | PRO_0000376922 | |||||||
Sites | |||||||||||
| Active site | 47 | 1 | By similarity | ||||||||
| Active site | 89 | 1 | By similarity | ||||||||
| Metal binding | 27 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 29 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 31 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 48 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 26 ↔ 115 | By similarity | |||||||||
| Disulfide bond | 28 ↔ 44 | By similarity | |||||||||
| Disulfide bond | 43 ↔ 95 | By similarity | |||||||||
| Disulfide bond | 49 ↔ 122 | By similarity | |||||||||
| Disulfide bond | 50 ↔ 88 | By similarity | |||||||||
| Disulfide bond | 57 ↔ 81 | By similarity | |||||||||
| Disulfide bond | 75 ↔ 86 | By similarity | |||||||||
Sequences
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References
| [1] | "Structural, enzymatic and biological properties of new PLA(2) isoform from Crotalus durissus terrificus venom." Toyama M.H., de Oliveira D.G., Beriam L.O.S., Novello J.C., Rodrigues-Simioni L., Marangoni S. Toxicon 41:1033-1038(2003) [PubMed: 12875878] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Venom. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
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... |
Entry information
| Entry name | PA215_CRODU | ||||||||
| Accession | Primary (citable) accession number: P0CAS5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||
