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P51972 (PA2B1_AGKPI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Basic phospholipase A2 APP-D49

Short name=svPLA2
EC=3.1.1.4
Alternative name(s):
App-dimer
Phosphatidylcholine 2-acylhydrolase
OrganismAgkistrodon piscivorus piscivorus (Eastern cottonmouth)
Taxonomic identifier8716 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeAgkistrodon

Protein attributes

Sequence length123 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. Ref.3

Catalytic activity

Phosphatidylcholine + H2O = 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. D49 sub-subfamily.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Lipoprotein
Palmitate
   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 – 123123Basic phospholipase A2 APP-D49
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 Ref.2
Lipidation101N6-palmitoyl lysine Ref.2
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Tissue: Venom.

Cross-references

Sequence databases

PIRB53872.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VAPX-ray1.60A/B1-123[»]
ProteinModelPortalP51972.
SMRP51972. Positions 1-123.
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...

Other

EvolutionaryTraceP51972.

Entry information

Entry namePA2B1_AGKPI
AccessionPrimary (citable) accession number: P51972
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: May 1, 2013
This is version 85 of the entry and version 2 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