Reviewed,
UniProtKB/Swiss-Prot Q9W7J4 (PA21B_PSETE)
Last modified
January 19, 2010.
Version 53.
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 1 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase Pt-PLA1 |
| Organism | Pseudonaja textilis (Eastern brown snake) |
| Taxonomic identifier | 8673 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Pseudonaja |
Protein attributes
| Sequence length | 154 AA. |
| Sequence status | Complete. |
| 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. Shows moderate PA2 activity and exhibits procoagulant property. Ref.1 |
| Catalytic activity | Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. |
| Subunit structure | Monomer. |
| Subcellular location | Secreted By similarity. |
| Tissue specificity | Expressed by the venom gland. |
| Sequence similarities | Belongs to the phospholipase A2 family. Group I subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Blood coagulation Lipid degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic processInferred 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 – 19 | 19 | Potential | ||||||||
| Propeptide | 20 – 27 | 8 | PRO_0000022948 | ||||||||
| Chain | 28 – 154 | 127 | Phospholipase A2 1 | PRO_0000022949 | |||||||
Sites | |||||||||||
| Active site | 75 | 1 | By similarity | ||||||||
| Active site | 126 | 1 | By similarity | ||||||||
| Metal binding | 55 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 57 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 58 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 76 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 38 ↔ 104 | By similarity | |||||||||
| Disulfide bond | 54 ↔ 153 | By similarity | |||||||||
| Disulfide bond | 56 ↔ 72 | By similarity | |||||||||
| Disulfide bond | 71 ↔ 132 | By similarity | |||||||||
| Disulfide bond | 78 ↔ 125 | By similarity | |||||||||
| Disulfide bond | 88 ↔ 118 | By similarity | |||||||||
| Disulfide bond | 111 ↔ 123 | By similarity | |||||||||
Sequences
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References
| [1] | "Group IB phospholipase A2 from Pseudonaja textilis." Armugam A., Gong N.L., Li X.J., Siew P.Y., Chai S.C., Nair R., Jeyaseelan K. Arch. Biochem. Biophys. 421:10-20(2004) [PubMed: 14678780] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-39, FUNCTION. Tissue: Venom and Venom gland. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF082983 mRNA. Translation: AAD40975.1. AY027494 Genomic DNA. Translation: AAK15775.1. |
3D structure databases | |
| SMR | Q9W7J4. Positions 29-145. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q9W7J4. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.4. 274617. |
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 | PA21B_PSETE | ||||||||
| Accession | Primary (citable) accession number: Q9W7J4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


