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Protein

Neutral phospholipase A2 agkistrodotoxin

Gene
N/A
Organism
Gloydius halys (Chinese water mocassin) (Agkistrodon halys)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi29 – 291Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi31 – 311Calcium; via carbonyl oxygenCombined sources1 Publication
Active sitei47 – 4711 Publication
Metal bindingi48 – 481CalciumCombined sources1 Publication
Active sitei89 – 8911 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Neurotoxin, Presynaptic neurotoxin, Toxin

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral phospholipase A2 agkistrodotoxin (EC:3.1.1.4)
Short name:
AGTX
Short name:
ATX
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismiGloydius halys (Chinese water mocassin) (Agkistrodon halys)
Taxonomic identifieri8714 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeGloydius

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Neutral phospholipase A2 agkistrodotoxinPRO_0000161599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 115Combined sources2 Publications
Disulfide bondi28 ↔ 44Combined sources2 Publications
Disulfide bondi43 ↔ 95Combined sources2 Publications
Disulfide bondi49 ↔ 122Combined sources2 Publications
Disulfide bondi50 ↔ 88Combined sources2 Publications
Disulfide bondi57 ↔ 81Combined sources2 Publications
Disulfide bondi75 ↔ 86Combined sources2 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Turni18 – 225Combined sources
Turni25 – 273Combined sources
Beta strandi28 – 303Combined sources
Helixi39 – 5315Combined sources
Turni59 – 613Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 755Combined sources
Helixi80 – 9920Combined sources
Helixi100 – 1023Combined sources
Helixi105 – 1073Combined sources
Helixi112 – 1143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2AX-ray2.80A/B/C/D/E/F/G/H1-122[»]
1BJJX-ray2.80A/B/C/D/E/F1-122[»]
ProteinModelPortaliP14421.
SMRiP14421. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14421.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG008137.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14421-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NLLQFNKMIK EETGKNAIPF YAFYGCYCGG GGQGKPKDGT DRCCFVHDCC
60 70 80 90 100
YGRLVNCNTK SDIYSYSLKE GYITCGKGTN CEEQICECDR VAAECFRRNL
110 120
DTYNNGYMFY RDSKCTETSE EC
Length:122
Mass (Da):13,869
Last modified:January 1, 1990 - v1
Checksum:iBB0B7BE5266221F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301G → W AA sequence (PubMed:3617077).Curated

Mass spectrometryi

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

Sequence databases

PIRiC26279.
JX0063.

Cross-referencesi

Sequence databases

PIRiC26279.
JX0063.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2AX-ray2.80A/B/C/D/E/F/G/H1-122[»]
1BJJX-ray2.80A/B/C/D/E/F1-122[»]
ProteinModelPortaliP14421.
SMRiP14421. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiP14421.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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), DISULFIDE BONDS.
  5. "Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit."
    Tang L., Zhou Y.C., Lin Z.J.
    Acta Crystallogr. D 55:1986-1996(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.

Entry informationi

Entry nameiPA2N_GLOHA
AccessioniPrimary (citable) accession number: P14421
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.