Reviewed,
UniProtKB/Swiss-Prot P19000 (PA21B_LATLA)
Last modified
June 16, 2009.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Phospholipase A2 P'513 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase |
| Organism | Laticauda laticaudata (Blue-ringed sea krait) |
| Taxonomic identifier | 8630 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Laticaudinae › Laticauda |
Protein attributes
| Sequence length | 145 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. |
| Subunit structure | In contrast to the pancreatic enzymes, the molecules of venom phospholipases A2 are dimers of identical chains; the monomers appear to be inactive. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Sequence similarities | Belongs to the phospholipase A2 family. Group I subfamily. |
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 – 21 | 21 | Potential | ||||||||
| Propeptide | 22 – 27 | 6 | PRO_0000022886 | ||||||||
| Chain | 28 – 145 | 118 | Phospholipase A2 P'513 | PRO_0000022887 | |||||||
Sites | |||||||||||
| Active site | 75 | 1 | By similarity | ||||||||
| Active site | 119 | 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 | 59 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 76 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 38 ↔ 98 | By similarity | |||||||||
| Disulfide bond | 54 ↔ 144 | By similarity | |||||||||
| Disulfide bond | 56 ↔ 72 | By similarity | |||||||||
| Disulfide bond | 71 ↔ 125 | By similarity | |||||||||
| Disulfide bond | 78 ↔ 118 | By similarity | |||||||||
| Disulfide bond | 87 ↔ 111 | By similarity | |||||||||
| Disulfide bond | 105 ↔ 116 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Sequence of a cDNA encoding a snake venom phospholipase A2." Guignery Frelat G., Ducancel F., Menez A., Boulain J.-C. Nucleic Acids Res. 15:5892-5892(1987) [PubMed: 3615209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland. |
Cross-references
Sequence databases | |
|---|---|
| Y00377 mRNA. Translation: CAA68449.1. | |
| PIR | A27099. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AE7 based on UniProtKB P00608. |
| SMR | P19000. Positions 28-145. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P19000. |
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. |
| 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_LATLA | ||||||||
| Accession | Primary (citable) accession number: P19000 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


