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Q9DF52 (PA2K_BUNCE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 71. 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:
Phospholipase A2 KPA2
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismBungarus caeruleus (Indian krait)
Taxonomic identifier132961 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. The protein shows anticoagulant and neurotoxic activities.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Neurotoxin
Presynaptic neurotoxin
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentother organism presynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Signal peptide1 – 1919 Potential
Propeptide20 – 278 By similarity
PRO_0000022827
Chain28 – 145118Phospholipase A2 KPA2
PRO_0000022828

Sites

Active site501
Active site731
Active site1191
Metal binding531Calcium; via carbonyl oxygen
Metal binding551Calcium; via carbonyl oxygen
Metal binding571Calcium; via carbonyl oxygen
Metal binding741Calcium

Amino acid modifications

Disulfide bond38 ↔ 97 Ref.1
Disulfide bond52 ↔ 144 Ref.1
Disulfide bond54 ↔ 70 Ref.1
Disulfide bond69 ↔ 125 Ref.1
Disulfide bond76 ↔ 118 Ref.1
Disulfide bond86 ↔ 111 Ref.1
Disulfide bond104 ↔ 116 Ref.1

Secondary structure

1 .................... 145
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9DF52 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 4CE49BD226AF3317

FASTA14515,765
        10         20         30         40         50         60 
MYPAHLLVLV AVCVSLLGAA NIPPQPLNLI QFKNMIQCAG TRPWTAYVNY GCYCGKGGSG 

        70         80         90        100        110        120 
TPVDELDRCC YTHDNCYNEA EKIPGCNPNI KTYSYTCTEP NLTCTDTADT CARFLCDCDR 

       130        140 
TAAICFASAP YNSNNVMISS STNCQ

« Hide

References

[1]"Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites."
Singh G., Gourinath S., Sharma S., Paramasivam M., Srinivasan A., Singh T.P.
J. Mol. Biol. 307:1049-1059(2001) [PubMed: 11286555] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT, DISULFIDE BOND.
Tissue: Venom and Venom gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF297663 mRNA. Translation: AAG13412.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPYX-ray2.45A28-145[»]
1FE5X-ray2.45A28-145[»]
1PO8X-ray2.71A34-137[»]
ProteinModelPortalQ9DF52.
SMRQ9DF52. Positions 28-145.
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.
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 namePA2K_BUNCE
AccessionPrimary (citable) accession number: Q9DF52
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
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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