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Protein

Basic phospholipase A2 B

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 shows potent hemolytic activity, and exhibits medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC50 is 90 nM). It is one of the few phospholipases A2 capable of hydrolyzing the phospholipids of E.coli membranes in the presence of a bactericidal/permeability-increasing protein (BPI) of neutrophils. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.2 Publications

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 bindingi43 – 431Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi45 – 451Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi47 – 471Calcium; via carbonyl oxygenCombined sources1 Publication
Active sitei63 – 6311 Publication
Metal bindingi64 – 641CalciumCombined sources1 Publication
Active sitei105 – 10511 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Basic phospholipase A2 B (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
BPLA(2)
Phosphatidylcholine 2-acylhydrolase
bAhp
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
Signal peptidei1 – 1616By similarityAdd
BLAST
Chaini17 – 138122Basic phospholipase A2 BPRO_0000022776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 131Combined sources2 Publications
Disulfide bondi44 ↔ 60Combined sources2 Publications
Disulfide bondi59 ↔ 111Combined sources2 Publications
Disulfide bondi65 ↔ 138Combined sources2 Publications
Disulfide bondi66 ↔ 104Combined sources2 Publications
Disulfide bondi73 ↔ 97Combined sources2 Publications
Disulfide bondi91 ↔ 102Combined sources2 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
138
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 2912Combined sources
Helixi33 – 364Combined sources
Turni37 – 393Combined sources
Turni41 – 433Combined sources
Beta strandi44 – 463Combined sources
Helixi55 – 6915Combined sources
Turni75 – 773Combined sources
Beta strandi82 – 854Combined sources
Beta strandi88 – 914Combined sources
Helixi96 – 11419Combined sources
Helixi116 – 1183Combined sources
Helixi121 – 1233Combined sources
Helixi128 – 1303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4WX-ray2.60A/B/C/D17-138[»]
1C1JX-ray2.80A/B/C/D18-138[»]
1JIAX-ray2.13A/B18-138[»]
4HG9X-ray1.60A/B/C/D18-138[»]
ProteinModelPortaliO42187.
SMRiO42187. Positions 18-138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO42187.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O42187-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALWIVAVL LLGVEGSLLQ FRKMIKKMTG KEPVVSYAFY GCYCGSGGRG
60 70 80 90 100
KPKDATDRCC FVHDCCYEKL TGCDPKWDDY TYSWKNGTIV CGGDDPCKKE
110 120 130
VCECDKAAAI CFRDNLKTYK KRYMTYPNIL CSSKSEKC
Length:138
Mass (Da):15,614
Last modified:December 13, 2002 - v2
Checksum:i149D21704F4AA437
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015242 mRNA. Translation: AAB71844.1.
PIRiJC1342.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015242 mRNA. Translation: AAB71844.1.
PIRiJC1342.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4WX-ray2.60A/B/C/D17-138[»]
1C1JX-ray2.80A/B/C/D18-138[»]
1JIAX-ray2.13A/B18-138[»]
4HG9X-ray1.60A/B/C/D18-138[»]
ProteinModelPortaliO42187.
SMRiO42187. Positions 18-138.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiO42187.

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. "Cloning of the BPLA(2) gene from Agkistrodon halys pallas."
    Pan H., Ou-Yang L.-L., Yang G.-Z., Zhou Y.-C., Wu X.-F.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 28:579-582(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Diversity of cDNAs encoding phospholipase A2 from Agkistrodon halys pallas venom, and its expression in E. coli."
    Pan H., Liu X.-L., Ou-Yang L.-L., Yang G.-Z., Zhou Y.-C., Li Z.-P., Wu X.-F.
    Toxicon 36:1155-1163(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  3. "Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics."
    Faure G., Gowda V.T., Maroun R.C.
    BMC Struct. Biol. 7:82-82(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTICOAGULANT.
  4. "Structure of a basic phospholipase A2 from Agkistrodon halys pallas at 2.13 A resolution."
    Zhao K., Song S., Lin Z., Zhou Y.-C.
    Acta Crystallogr. D 54:510-521(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 18-138 IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.
    Tissue: Venom.
  5. "Structure of basic phospholipase A2 from Agkistrodon halys pallas: implications for its association, hemolytic and anticoagulant activities."
    Zhao K., Zhou Y.-C., Lin Z.
    Toxicon 38:901-916(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 18-138, FUNCTION, DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiPA2BB_GLOHA
AccessioniPrimary (citable) accession number: O42187
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: December 13, 2002
Last modified: May 11, 2016
This is version 96 of the entry and version 2 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

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.