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Reviewed, UniProtKB/Swiss-Prot Q8JFG0 (PA21B_VIPAP)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phospholipase A2, B chain
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    Vaspin chain B
OrganismVipera aspis aspis (Aspic viper)
Taxonomic identifier194601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Vipera

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Protein attributes

Sequence length138 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

The vaspin complex shows postsynaptic neurotoxicity, while the isolated vaspin B chain is a presynaptic neurotoxin By similarity.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Heterodimer of a weakly toxic basic protein having phospholipase A2 activity (B chain) and a nontoxic acidic protein functioning as its inhibitor (A chain).

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 By similarity
Chain17 – 138122Phospholipase A2, B chain
PRO_0000022968

Sites

Active site631 By similarity
Active site1051 By similarity
Metal binding431Calcium; via carbonyl oxygen By similarity
Metal binding451Calcium; via carbonyl oxygen By similarity
Metal binding471Calcium; via carbonyl oxygen By similarity
Metal binding641Calcium By similarity

Amino acid modifications

Disulfide bond42 ↔ 131 By similarity
Disulfide bond44 ↔ 60 By similarity
Disulfide bond59 ↔ 111 By similarity
Disulfide bond65 ↔ 138 By similarity
Disulfide bond66 ↔ 104 By similarity
Disulfide bond73 ↔ 97 By similarity
Disulfide bond91 ↔ 102 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8JFG0-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 28C749D504D1EA3E

FASTA13815,610
        10         20         30         40         50         60 
MRILWIVAVC LIGVEGNLFQ FAKMINGKLG AFSVWNYISY GCYCGWGGQG TPKDATDRCC 

        70         80         90        100        110        120 
FVHDCCYGRV RGCNPKLAIY SYSFKKGNIV CGKNNGCLRD ICECDRVAAN CFHQNKNTYN 

       130 
KNYRFLSSSR CRQTSEQC

« Hide

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References

[1]"Toxicity evolution of Vipera aspis aspis venom: identification and molecular modeling of a novel phospholipase A(2) heterodimer neurotoxin."
Jan V., Maroun R.C., Robbe-Vincent A., De Haro L., Choumet V.
FEBS Lett. 527:263-268(2002) [PubMed: 12220671] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Sequences and structural organization of phospholipase A2 genes from Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom. Identification of the origin of a new viper population based on ammodytin I1 heterogeneity."
Guillemin I., Bouchier C., Garrigues T., Wisner A., Choumet V.
Eur. J. Biochem. 270:2697-2706(2003) [PubMed: 12823540] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.

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Cross-references

Sequence databases

AJ459807 mRNA. Translation: CAD30850.1.
AY243576 Genomic DNA. Translation: AAO86504.1.

3D structure databases

HSSPHSSP built from PDB template 1JLT based on UniProtKB P14420.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ8JFG0.

Enzyme and pathway databases

BRENDA3.1.1.4. 294521.

Family and domain databases

InterProIPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_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.
ProDomPD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePA21B_VIPAP
AccessionPrimary (citable) accession number: Q8JFG0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents