P20249 (PA2A_GLOBL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 83.
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: Acidic phospholipase A2 Short name=PA2-II Short name=svPLA2 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase |
| Organism | Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi) |
| Taxonomic identifier | 242054 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Gloydius![]() |
Protein attributes
| Sequence length | 122 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | PLA2 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. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Miscellaneous | Is not neurotoxic. |
| Sequence similarities | Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation Lipid metabolism |
| 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: InterPro 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 | Acidic phospholipase A2 | PRO_0000161596 | |||||||
Sites | |||||||||||
| Active site | 47 | 1 | |||||||||
| Active site | 89 | 1 | |||||||||
| Metal binding | 27 | 1 | Calcium; via carbonyl oxygen | ||||||||
| Metal binding | 29 | 1 | Calcium; via carbonyl oxygen | ||||||||
| Metal binding | 30 | 1 | Calcium; via carbonyl oxygen | ||||||||
| Metal binding | 48 | 1 | Calcium | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 26 ↔ 115 | ||||||||||
| Disulfide bond | 28 ↔ 44 | ||||||||||
| Disulfide bond | 43 ↔ 95 | ||||||||||
| Disulfide bond | 49 ↔ 122 | ||||||||||
| Disulfide bond | 50 ↔ 88 | ||||||||||
| Disulfide bond | 57 ↔ 81 | ||||||||||
| Disulfide bond | 75 ↔ 86 | ||||||||||
Sequences
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References
| [1] | "Revised amino acid sequence, crystallization, and preliminary X-ray diffraction analysis of acidic phospholipase A2 from the venom of Agkistrodon halys blomhoffii." Tomoo K., Ohishi H., Ishida T., Inoue M., Ikeda K., Aoki Y., Samejima Y. J. Biol. Chem. 264:3636-3638(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom. |
| [2] | "Complete amino acid sequence of phospholipase A2-II isolated from Agkistrodon halys blomhoffii venom." Samejima Y., Iwanaga S., Suzuki T. FEBS Lett. 47:348-351(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE. Tissue: Venom. |
| [3] | "Structure of acidic phospholipase A2 for the venom of Agkistrodon halys blomhoffii at 2.8-A resolution." Tomoo K., Ohishi H., Doi M., Ishida T., Inoue M., Ikeda K., Hata Y., Samejima Y. Biochem. Biophys. Res. Commun. 184:137-143(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P20249. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG008137. |
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... |
Entry information
| Entry name | PA2A_GLOBL | ||||||||
| Accession | Primary (citable) accession number: P20249 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
