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P00608 (PA22_NOTSC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. 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
EC=3.1.1.4
Alternative name(s):
Notexin
Phosphatidylcholine 2-acylhydrolase
OrganismNotechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
Taxonomic identifier70142 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Notechis

Protein attributes

Sequence length119 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. Inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Acts presynaptically. Is directly toxic to skeletal muscle upon local application in vivo (dystrophic effect).

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

LD50 is 0.025 mg/kg by intravenous injection.

Miscellaneous

Activity and lethal neurotoxicity are lost upon modification with p-bromophenacyl bromide.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 119119Phospholipase A2
PRO_0000161675

Sites

Active site481 Ref.3 Ref.5
Active site931 Ref.3
Metal binding281Calcium; via carbonyl oxygen
Metal binding301Calcium; via carbonyl oxygen
Metal binding321Calcium; via carbonyl oxygen
Metal binding491Calcium

Amino acid modifications

Disulfide bond11 ↔ 71
Disulfide bond27 ↔ 118
Disulfide bond29 ↔ 45
Disulfide bond44 ↔ 99
Disulfide bond51 ↔ 92
Disulfide bond60 ↔ 85
Disulfide bond78 ↔ 90

Natural variations

Natural variant161K → R in variant S.

Secondary structure

1 ...................... 119
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00608 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 23D8BF780221D852

FASTA11913,593
        10         20         30         40         50         60 
NLVQFSYLIQ CANHGKRPTW HYMDYGCYCG AGGSGTPVDE LDRCCKIHDD CYDEAGKKGC 

        70         80         90        100        110 
FPKMSAYDYY CGENGPYCRN IKKKCLRFVC DCDVEAAFCF AKAPYNNANW NIDTKKRCQ

« Hide

References

[1]"Amino acid sequence of a presynaptic neurotoxin from the venom of Notechis scutatus scutatus (Australian tiger snake)."
Halpert J., Eaker D.
J. Biol. Chem. 250:6990-6997(1975) [PubMed: 1158892] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"On the purification of notexin. Isolation of a single amino acid variant from the venom of Notechis scutatus scutatus."
Chwetzoff S., Mollier P., Bouet F., Rowan E.G., Harvey A.L., Menez A.
FEBS Lett. 261:226-230(1990) [PubMed: 2155818] [Abstract]
Cited for: PROTEIN SEQUENCE (NOTEXIN-S).
Tissue: Venom.
[3]"The role of phospholipase activity in the action of a presynaptic neurotoxin from the venom of Notechis scutatus scutatus (Australian tiger snake)."
Halpert J., Eaker D., Karlsson E.
FEBS Lett. 61:72-76(1976) [PubMed: 1245225] [Abstract]
Cited for: ACTIVE SITE.
[4]"Tryptophan 110, a residue involved in the toxic activity but not in the enzymatic activity of notexin."
Mollier P., Chwetzoff S., Bouet F., Harvey A.L., Menez A.
Eur. J. Biochem. 185:263-270(1989) [PubMed: 2583182] [Abstract]
Cited for: INVOLVEMENT OF TRP-110 IN TOXICITY.
[5]"The three-dimensional structure of notexin, a presynaptic neurotoxic phospholipase A2 at 2.0-A resolution."
Westerlund B., Nordlund P., Uhlim U., Eaker D., Eklund H.
FEBS Lett. 301:159-164(1992) [PubMed: 1568473] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRPSNOAT. A00749.
PSNOAS. S08258.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AE7X-ray2.00A1-119[»]
ProteinModelPortalP00608.
SMRP00608. Positions 1-119.
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 namePA22_NOTSC
AccessionPrimary (citable) accession number: P00608
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 16, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin 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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