P00611 (PA2A1_PSSEM) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
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 1 Short name=svPLA2 EC=3.1.1.4 Alternative name(s): GL5-1 Phosphatidylcholine 2-acylhydrolase Phospholipase A2 isozyme I |
| Organism | Pseudolaticauda semifasciata (Black-banded sea krait) (Laticauda semifasciata) |
| Taxonomic identifier | 8631 [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 protein level |
General annotation (Comments)
| Function | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides By similarity. |
| Catalytic activity | Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. |
| Cofactor | Binds 1 calcium ion By similarity. |
| Subunit structure | Monomer. Ref.2 |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Sequence similarities | Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation Lipid metabolism |
| 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 | 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | ||||||||
| Propeptide | 22 – 27 | 6 | PRO_0000022896 | ||||||||
| Chain | 28 – 145 | 118 | Acidic phospholipase A2 1 | PRO_0000022897 | |||||||
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 | ||||||||
| Site | 91 | 1 | Specific activity reduced 20-fold by modification | ||||||||
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 | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 39 – 40 | 2 | VN → NV AA sequence Ref.2 | ||||||||
| Sequence conflict | 77 | 1 | D → N AA sequence Ref.2 | ||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "A comparative analysis of invaded sequences from group IA phospholipase A(2) genes provides evidence about the divergence period of genes groups and snake families." Fujimi T.J., Tsuchiya T., Tamiya T. Toxicon 40:873-884(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver. |
| [2] | "Amino acid sequences of three phospholipases A I, III and IV from the venom of the sea snake Laticauda semifasciata." Nishida S., Kim H.S., Tamiya N. Biochem. J. 207:589-594(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-145, SUBUNIT. Tissue: Venom. |
| [3] | "Correction of amino acid sequence of phospholipase A2 I from the venom of Laticauda semifasciata (Erabu sea snake)." Takasaki C., Kuramochi H., Shimazu T., Tamiya N. Toxicon 26:747-749(1988) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 97-107. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB062440 Genomic DNA. Translation: BAB72247.1. |
| PIR | PSLT1E. A94325. |
3D structure databases | |
| ProteinModelPortal | P00611. |
| SMR | P00611. Positions 28-145. |
| 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 | PA2A1_PSSEM | ||||||||
| Accession | Primary (citable) accession number: P00611 Secondary accession number(s): Q9I848 | ||||||||
| 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
