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P04056 (PA21B_PSEAU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospholipase A2 isozyme PA-11
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

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.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

LD50 is 0.24 mg/kg by intravenous injection.

Miscellaneous

There are many protein components with phospholipase A2 activity in the Mulga snake venom and some of them are myotoxic.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termDirect 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 – 118118Phospholipase A2 isozyme 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

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: 3887651] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRPSSNK1. A00747.

3D structure databases

ProteinModelPortalP04056.
SMRP04056. Positions 1-118.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008137.

Family and domain databases

InterProIPR016090. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR001211. PLipase_A2_euk.
[Graphical view]
Gene3DG3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHERPTHR11716. Phospholipase_A2. 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 namePA21B_PSEAU
AccessionPrimary (citable) accession number: P04056
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: October 19, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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