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Protein

Basic phospholipase A2 beta-bungarotoxin A1 chain

Gene
N/A
Organism
Bungarus multicinctus (Many-banded krait)
Status
Reviewed-Annotation score: Annotation score: 5 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.

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 bindingi55 – 551Calcium; via carbonyl oxygen1 Publication
Metal bindingi57 – 571Calcium; via carbonyl oxygen1 Publication
Metal bindingi59 – 591Calcium; via carbonyl oxygen1 Publication
Active sitei75 – 751By similarity
Metal bindingi76 – 761Calcium1 Publication
Active sitei121 – 1211By similarity

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:
Basic phospholipase A2 beta-bungarotoxin A1 chain (EC:3.1.1.4)
Short name:
Beta-BuTX A1 chain
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismiBungarus multicinctus (Many-banded krait)
Taxonomic identifieri8616 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 0.019 mg/kg by intraperitoneal injection in beta-1 bungarotoxin and 0.028 mg/kg in beta-2.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421C → S: Loss of PA2 activity. No loss in Ca(2+)-binding ability. Weak loss in folding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 2782 PublicationsPRO_0000022835
Chaini28 – 147120Basic phospholipase A2 beta-bungarotoxin A1 chainPRO_0000022836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 – 42Interchain (with a B chain)1 Publication
Disulfide bondi54 ↔ 146Combined sources1 Publication
Disulfide bondi56 ↔ 72Combined sources1 Publication
Disulfide bondi71 ↔ 127Combined sources1 Publication
Disulfide bondi78 ↔ 120Combined sources1 Publication
Disulfide bondi88 ↔ 113Combined sources1 Publication
Disulfide bondi106 ↔ 118Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer; disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors. The A1 chain is found in beta-1 and beta-2 bungarotoxins.1 Publication

Protein-protein interaction databases

MINTiMINT-1515204.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 379Combined sources
Helixi47 – 504Combined sources
Turni53 – 553Combined sources
Beta strandi56 – 583Combined sources
Helixi67 – 8317Combined sources
Turni84 – 863Combined sources
Turni90 – 923Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi103 – 1064Combined sources
Helixi113 – 13018Combined sources
Helixi135 – 1373Combined sources
Helixi142 – 1454Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BUNX-ray2.45A28-147[»]
ProteinModelPortaliP00617.
SMRiP00617. Positions 28-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00617.

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.

P00617-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPAHLLVLS AVCVSLLGAA NIPPHPLNLI NFMEMIRYTI PCEKTWGEYA
60 70 80 90 100
DYGCYCGAGG SGRPIDALDR CCYVHDNCYG DAEKKHKCNP KTQSYSYKLT
110 120 130 140
KRTIICYGAA GTCGRIVCDC DRTAALCFGN SEYIEGHKNI DTARFCQ
Length:147
Mass (Da):16,220
Last modified:September 19, 2002 - v2
Checksum:i12109A187E20C7F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101S → L in CAB62164 (PubMed:10903499).Curated
Sequence conflicti93 – 942QS → SQ AA sequence (PubMed:624701).Curated
Sequence conflicti93 – 942QS → SQ AA sequence (PubMed:7096304).Curated
Sequence conflicti130 – 1323NSE → QSD AA sequence (PubMed:624701).Curated
Sequence conflicti130 – 1323NSE → QSD AA sequence (PubMed:7096304).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161I → V in 20% of the molecules.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ431711 mRNA. Translation: CAD24466.1.
AJ251360 Genomic DNA. Translation: CAB62164.1.
AJ242011 mRNA. Translation: CAB62383.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ431711 mRNA. Translation: CAD24466.1.
AJ251360 Genomic DNA. Translation: CAB62164.1.
AJ242011 mRNA. Translation: CAB62383.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BUNX-ray2.45A28-147[»]
ProteinModelPortaliP00617.
SMRiP00617. Positions 28-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1515204.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiP00617.

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. "Genomic organization of the genes encoding the A chains of beta-bungarotoxins."
    Chang L.-S., Chu Y.P.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Genetic organization of A chain and B chain of beta-bungarotoxin from Taiwan banded krait (Bungarus multicinctus). A chain genes and B chain genes do not share a common origin."
    Wu P.-F., Chang L.-S.
    Eur. J. Biochem. 267:4668-4675(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-147.
    Tissue: Liver.
  3. "Expression of A chain and B chain of beta-bungarotoxin from taiwan banded krait: the functional implication of the interchain disulfide bond between A chain and B chain."
    Wu P.-F., Chang L.-S.
    J. Protein Chem. 20:413-421(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-147, MUTAGENESIS OF CYS-42.
    Tissue: Venom gland.
  4. "Amino acid sequences of the two polypeptide chains in beta1-bungarotoxin from the venom of Bungarus multicinctus."
    Kondo K., Narita K., Lee C.-Y.
    J. Biochem. 83:101-115(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-147.
    Tissue: Venom.
  5. "Amino acid sequence of beta 2-bungarotoxin from Bungarus multicinctus venom. The amino acid substitutions in the B chains."
    Kondo K., Toda H., Narita K., Lee C.-Y.
    J. Biochem. 91:1519-1530(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-147, SEQUENCE REVISION TO 112-114 AND 136.
  6. "Characterization of phospholipase A activity of beta1-bungarotoxin from Bungarus multicinctus venom. II. Identification of the histidine residue of beta1-bungarotoxin modified by p-bromophenacyl bromide."
    Kondo K., Toda H., Narita K.
    J. Biochem. 84:1301-1308(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF PHOSPHOLIPASE A2 ACTIVITY.
  7. "Isolation and characterization of presynaptically acting neurotoxins from the venom of Bungarus snakes."
    Abe T., Alema S., Miledi R.
    Eur. J. Biochem. 80:1-12(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF PRESYNAPTIC NEUROTOXINS.
  8. "What does beta-bungarotoxin do at the neuromuscular junction?"
    Rowan E.G.
    Toxicon 39:107-118(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action."
    Kwong P.D., McDonald N.Q., Sigler P.B., Hendrickson W.A.
    Structure 3:1109-1119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 28-147 IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiPA2B1_BUNMU
AccessioniPrimary (citable) accession number: P00617
Secondary accession number(s): Q8QFN8, Q9PU95, Q9PU98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 19, 2002
Last modified: May 11, 2016
This is version 118 of the entry and version 2 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.