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P14421 (PA2N_GLOHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. 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:
Neutral phospholipase A2 agkistrodotoxin
Short name=AGTX
Short name=ATX
Short name=svPLA2
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismGloydius halys (Chinese water mocassin) (Agkistrodon halys)
Taxonomic identifier8714 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Gloydius

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. 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.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.

Mass spectrometry

Molecular mass is 13938 Da from positions 1 - 122. Determined by ESI. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122Neutral phospholipase A2 agkistrodotoxin
PRO_0000161599

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

Disulfide bond26 ↔ 115 Ref.4
Disulfide bond28 ↔ 44 Ref.4
Disulfide bond43 ↔ 95 Ref.4
Disulfide bond49 ↔ 122 Ref.4
Disulfide bond50 ↔ 88 Ref.4
Disulfide bond57 ↔ 81 Ref.4
Disulfide bond75 ↔ 86 Ref.4

Experimental info

Sequence conflict301G → W AA sequence Ref.2

Secondary structure

1 ....................... 122
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14421 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: BB0B7BE5266221F4

FASTA12213,869
        10         20         30         40         50         60 
NLLQFNKMIK EETGKNAIPF YAFYGCYCGG GGQGKPKDGT DRCCFVHDCC YGRLVNCNTK 

        70         80         90        100        110        120 
SDIYSYSLKE GYITCGKGTN CEEQICECDR VAAECFRRNL DTYNNGYMFY RDSKCTETSE 


EC

« Hide

References

[1]"Amino acid sequence of a presynaptic neurotoxin, agkistrodotoxin, from the venom of Agkistrodon halys pallas."
Kondo K., Zhang J.-K., Xu K., Kagamiyama H.
J. Biochem. 105:196-203(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Characterization of the structure and function of three phospholipases A2 from the venom of Agkistrodon halys pallas."
Chen Y.-C., Maraganore J.M., Reardon I., Heinrikson R.L.
Toxicon 25:401-409(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-52.
Tissue: Venom.
[3]"Molecular evolution and structure-function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pit viper venoms."
Chen Y.-H., Wang Y.-M., Hseu M.-J., Tsai I.-H.
Biochem. J. 381:25-34(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-23, FUNCTION, MASS SPECTROMETRY.
Tissue: Venom.
[4]"Crystal structure of agkistrodotoxin, a phospholipase A2-type presynaptic neurotoxin from Agkistrodon halys pallas."
Tang L., Zhou Y.-C., Lin Z.-J.
J. Mol. Biol. 282:1-11(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRC26279.
JX0063.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2AX-ray2.80A/B/C/D/E/F/G/H1-122[»]
1BJJX-ray2.80A/B/C/D/E/F1-122[»]
ProteinModelPortalP14421.
SMRP14421. Positions 1-122.
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

EvolutionaryTraceP14421.

Entry information

Entry namePA2N_GLOHA
AccessionPrimary (citable) accession number: P14421
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 1, 2013
This is version 90 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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