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Protein

Acidic phospholipase A2

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

Functioni

Snake venom phospholipase A2 (PLA2) that acts in vivo as an anti-thrombotic agent. Inhibits platelet aggregation induced by ADP, arachidonic acid, and thrombin. 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+2 PublicationsNote: Binds 1 Ca2+ ion.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Calcium; via carbonyl oxygenCombined sources2 Publications
Metal bindingi29 – 291Calcium; via carbonyl oxygenCombined sources2 Publications
Metal bindingi31 – 311Calcium; via carbonyl oxygenCombined sources2 Publications
Active sitei47 – 4711 Publication
Metal bindingi48 – 481CalciumCombined sources2 Publications
Active sitei89 – 8911 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Hydrolase, Platelet aggregation inhibiting toxin, Toxin

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.4. 195.

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic phospholipase A2 (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
APLA2
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

Pathology & Biotechi

Pharmaceutical usei

The venom of this snake has been orally administered to patients in China for about 2000 years, mostly to treat thrombotic diseases.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 124124Acidic phospholipase A2PRO_0000161597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 116Combined sources2 Publications
Disulfide bondi28 ↔ 44Combined sources2 Publications
Disulfide bondi43 ↔ 95Combined sources2 Publications
Disulfide bondi49 ↔ 124Combined 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.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Helixi17 – 204Combined sources
Beta strandi21 – 244Combined sources
Turni25 – 273Combined sources
Beta strandi28 – 314Combined sources
Helixi39 – 5214Combined sources
Turni59 – 613Combined sources
Beta strandi65 – 695Combined sources
Beta strandi72 – 787Combined sources
Helixi80 – 9819Combined sources
Helixi99 – 1024Combined sources
Helixi105 – 1084Combined sources
Helixi113 – 1153Combined sources
Helixi118 – 1203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BK9X-ray2.00A1-124[»]
1PSJX-ray2.00A1-124[»]
ProteinModelPortaliP14418.
SMRiP14418. Positions 1-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14418.

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.

P14418-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SLIQFETLIM KVAKKSGMFW YSNYGCYCGW GGQGRPQDAT DRCCFVHDCC
60 70 80 90 100
YGKVTGCDPK MDVYSFSEEN GDIVCGGDDP CKKEICECDR AAAICFRDNL
110 120
TLYNDKKYWA FGAKNCPQEE SEPC
Length:124
Mass (Da):13,974
Last modified:January 1, 1990 - v1
Checksum:i34BE769D31A45D26
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1022TL → NT AA sequence (PubMed:18456297).Curated

Mass spectrometryi

Molecular mass is 13962 Da from positions 1 - 124. Determined by ESI. 1 Publication

Sequence databases

PIRiA26535.

Cross-referencesi

Sequence databases

PIRiA26535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BK9X-ray2.00A1-124[»]
1PSJX-ray2.00A1-124[»]
ProteinModelPortaliP14418.
SMRiP14418. Positions 1-124.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Enzyme and pathway databases

BRENDAi3.1.1.4. 195.

Miscellaneous databases

EvolutionaryTraceiP14418.

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. "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.
    Tissue: Venom.
  2. "Bioassay-directed purification of an acidic phospholipase A(2) from Agkistrodon halys pallas venom."
    Wang Y., Cui G., Zhao M., Yang J., Wang C., Giese R.W., Peng S.
    Toxicon 51:1131-1139(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-114, FUNCTION, BIOASSAY, MASS SPECTROMETRY.
    Tissue: Venom.
  3. "Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0-A resolution."
    Wang X.-Q., Yang J., Gui L.-L., Lin Z.-J., Chen Y.-C., Zhou Y.-C.
    J. Mol. Biol. 255:669-676(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CALCIUM ION, ACTIVE SITE, COFACTOR, DISULFIDE BONDS.
    Tissue: Venom.
  4. "Structure of a snake venom phospholipase A2 modified by p-bromo-phenacyl-bromide."
    Zhao H., Tang L., Wang X., Zhou Y., Lin Z.
    Toxicon 36:875-886(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiPA2A_GLOHA
AccessioniPrimary (citable) accession number: P14418
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 112 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, Pharmaceutical

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.