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Reviewed, UniProtKB/Swiss-Prot P51972 (PA21_AGKPI)

Last modified November 25, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Phospholipase A2
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    APP-D-49
OrganismAgkistrodon piscivorus piscivorus (Eastern cottonmouth)
Taxonomic identifier8716 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeAgkistrodon

Protein attributes

Sequence length123 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 + H(2)O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer or homodimer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

Acylation causes dimerization.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily.

Ontologies

Keywords

   Biological processLipid degradation
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processlipid catabolic process

Inferred from electronic annotation. Source: InterPro

phospholipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 123123Phospholipase A2
PRO_0000161605

Sites

Active site471 By similarity
Active site891 By similarity
Metal binding271Calcium; via carbonyl oxygen
Metal binding291Calcium; via carbonyl oxygen
Metal binding311Calcium; via carbonyl oxygen
Metal binding481Calcium

Amino acid modifications

Lipidation71N6-palmitoyl lysine
Lipidation101N6-palmitoyl lysine
Disulfide bond26 ↔ 116
Disulfide bond28 ↔ 44
Disulfide bond43 ↔ 95
Disulfide bond49 ↔ 123
Disulfide bond50 ↔ 88
Disulfide bond57 ↔ 81
Disulfide bond75 ↔ 86

Secondary structure

........................ 123
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51972-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: C39986552D990D72

FASTA12313,989
        10         20         30         40         50         60 
NLFQFEKLIK KMTGKSGMLW YSAYGCYCGW GGQGRPKDAT DRCCFVHDCC YGKVTGCNPK 

        70         80         90        100        110        120 
MDIYTYSVDN GNIVCGGTNP CKKQICECDR AAAICFRDNL KTYDSKTYWK YPKKNCKEES 


EPC 

« Hide

References

[1]"An examination of structural interactions presumed to be of importance in the stabilization of phospholipase A2 dimers based upon comparative protein sequence analysis of a monomeric and dimeric enzyme from the venom of Agkistrodon p. piscivorus."
Welches W., Reardon I.M., Heinrikson R.L.
J. Protein Chem. 12:187-193(1993) [PubMed: 8489705] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"The chemical basis for interfacial activation of monomeric phospholipases A2. Autocatalytic derivatization of the enzyme by acyl transfer from substrate."
Cho W., Tomasselli A.G., Heinrikson R.L., Kezdy F.J.
J. Biol. Chem. 263:11237-11241(1988) [PubMed: 3403524] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-23, PALMITOYLATION AT LYS-7 AND LYS-10.
Tissue: Venom.
[3]"A new class of phospholipases A2 with lysine in place of aspartate 49. Functional consequences for calcium and substrate binding."
Maraganore J.M., Merutka G., Cho W., Welches W., Kezdy F.J., Heinrikson R.L.
J. Biol. Chem. 259:13839-13843(1984) [PubMed: 6438084] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Venom.
[4]"Structural aspects of interfacial adsorption. A crystallographic and site-directed mutagenesis study of the phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus."
Han S.K., Yoon E.T., Scott D.L., Sigler P.B., Cho W.
J. Biol. Chem. 272:3573-3582(1997) [PubMed: 9013608] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Tissue: Venom.

Cross-references

Sequence databases

PIRB53872.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1VAPX-ray1.60A/B1-123[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP51972.

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...

Other Resources

LinkHubP51972.

Entry information

Entry namePA21_AGKPI
AccessionPrimary (citable) accession number: P51972
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: November 25, 2008
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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