Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi27Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi29Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi31Calcium; via carbonyl oxygenCombined sources1 Publication1
Active sitei471 Publication1
Metal bindingi48CalciumCombined sources1 Publication1
Active sitei891 Publication1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001615991 – 122Neutral phospholipase A2 agkistrodotoxinAdd BLAST122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 13Combined sources12
Turni18 – 22Combined sources5
Turni25 – 27Combined sources3
Beta strandi28 – 30Combined sources3
Helixi39 – 53Combined sources15
Turni59 – 61Combined sources3
Beta strandi66 – 68Combined sources3
Beta strandi71 – 75Combined sources5
Helixi80 – 99Combined sources20
Helixi100 – 102Combined sources3
Helixi105 – 107Combined sources3
Helixi112 – 114Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14421.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG008137.

Family and domain databases

CDDicd00125. PLA2c. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti30G → W AA sequence (PubMed:3617077).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiP14421.

Family and domain databases

CDDicd00125. PLA2c. 1 hit.
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...

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: November 30, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin 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.