P24294 (PA2A2_ERIMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 76.
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 PLA-2 Short name=svPLA2 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase |
| Organism | Eristicophis macmahoni (Leaf-nosed viper) |
| Taxonomic identifier | 110227 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Eristicophis![]() |
Protein attributes
| Sequence length | 121 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 By similarity. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| 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 – 121 | 121 | Acidic phospholipase A2 PLA-2 | PRO_0000161646 | |||||||
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 ↔ 121 | 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] | "Purification and characterization of two highly different group II phospholipase A2 isozymes from a single viperid (Eristocophis macmahoni) venom." Siddiqi A.R., Zaidi Z.H., Joernvall H. Eur. J. Biochem. 201:675-679(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S17861. |
3D structure databases | |
| ProteinModelPortal | P24294. |
| SMR | P24294. Positions 1-121. |
| 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 | PA2A2_ERIMA | ||||||||
| Accession | Primary (citable) accession number: P24294 | ||||||||
| 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
