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P04056 (PA2BB_PSEAU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Basic phospholipase A2 PA-11
Short name=svPLA2
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismPseudechis australis (Mulga snake) (King brown snake)
Taxonomic identifier8670 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Pseudechis

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

LD50 is 0.24 mg/kg by intravenous injection.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipase A2 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 118118Basic phospholipase A2 PA-11
PRO_0000161686

Sites

Active site481 By similarity
Active site921 By similarity
Metal binding281Calcium; via carbonyl oxygen By similarity
Metal binding301Calcium; via carbonyl oxygen By similarity
Metal binding321Calcium; via carbonyl oxygen By similarity
Metal binding491Calcium By similarity

Amino acid modifications

Disulfide bond11 ↔ 71 By similarity
Disulfide bond27 ↔ 117 By similarity
Disulfide bond29 ↔ 45 By similarity
Disulfide bond44 ↔ 98 By similarity
Disulfide bond51 ↔ 91 By similarity
Disulfide bond60 ↔ 84 By similarity
Disulfide bond78 ↔ 89 By similarity

Secondary structure

1 ....................... 118
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04056 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: F7C90529BB12D5A1

FASTA11812,966
        10         20         30         40         50         60 
NLIQFGNMIQ CANKGSRPSL DYADYGCYCG WGGSGTPVDE LDRCCQVHDN CYEQAGKKGC 

        70         80         90        100        110 
FPKLTLYSWK CTGNVPTCNS KPGCKSFVCA CDAAAAKCFA KAPYKKENYN IDTKKRCK

« Hide

References

[1]"Amino acid sequences of phospholipases A2 from the venom of an Australian elapid snake (king brown snake, Pseudechis australis)."
Nishida S., Terashima M., Tamiya N.
Toxicon 23:87-104(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.

Cross-references

Sequence databases

PIRPSSNK1. A00747.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3V9MX-ray1.56A/B1-118[»]
ProteinModelPortalP04056.
SMRP04056. Positions 1-118.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008137.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERPTHR11716. PTHR11716. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. PhospholipaseA2. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA2BB_PSEAU
AccessionPrimary (citable) accession number: P04056
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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