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Protein

Acidic phospholipase A2 homolog vipoxin A chain

Gene
N/A
Organism
Vipera ammodytes meridionalis (Eastern sand viper)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heterodimer: postsynaptic neurotoxin.1 Publication
Monomer: Acidic phospholipase A2 homolog that is non-toxic.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic phospholipase A2 homolog vipoxin A chain
Short name:
svPLA2 homolog
Alternative name(s):
Acidic phospholipase A2 inhibitor vipoxin A chain
Vipoxin acidic component
Short name:
VAC
Vipoxin non-toxic component
OrganismiVipera ammodytes meridionalis (Eastern sand viper)
Taxonomic identifieri73841 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 of the heterodimer is 0.7-1.2 mg/kg by intraperitoneal injection into mice and 0.9-1.3 mg/kg by intravenous injection into mice.1 Publication
LD50 of the acidic component is >30 mg/kg by intraperitoneal injection into mice.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Acidic phospholipase A2 homolog vipoxin A chainPRO_0000161713Add
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.

Interactioni

Subunit structurei

Heterodimer of A and B (AC P14420) chains; non-covalently linked. The A chain (acidic) is non-toxic, and increases the toxicity of the B chain (basic). The A chain may act as factor stabilizing the complex structure and hence retaining its toxicity by preventing non-specific binding. Upon binding to the target membranes the A chain may dissociate.4 Publications

Protein-protein interaction databases

MINTiMINT-220264.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Helixi17 – 193Combined sources
Helixi21 – 233Combined sources
Turni25 – 284Combined sources
Beta strandi32 – 343Combined sources
Helixi39 – 5214Combined sources
Beta strandi54 – 563Combined sources
Turni59 – 613Combined sources
Beta strandi66 – 694Combined sources
Beta strandi72 – 754Combined sources
Helixi80 – 9819Combined sources
Helixi99 – 1024Combined sources
Helixi105 – 1073Combined sources
Helixi111 – 1133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOKX-ray2.00A1-122[»]
1JLTX-ray1.40A1-122[»]
1Q5TX-ray1.90A/B1-112[»]
1VPIX-ray1.76A1-122[»]
ProteinModelPortaliP04084.
SMRiP04084. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04084.

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.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NLFQFGDMIL QKTGKEAVHS YAIYGCYCGW GGQGRAQDAT DRCCFAQDCC
60 70 80 90 100
YGRVNDCNPK TATYTYSFEN GDIVCGDNDL CLRAVCECDR AAAICLGENV
110 120
NTYDKNYEYY SISHCTEESE QC
Length:122
Mass (Da):13,639
Last modified:July 15, 1998 - v3
Checksum:i3759601D80ABA697
GO

Sequence databases

PIRiB29290. PSVII.

Cross-referencesi

Sequence databases

PIRiB29290. PSVII.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOKX-ray2.00A1-122[»]
1JLTX-ray1.40A1-122[»]
1Q5TX-ray1.90A/B1-112[»]
1VPIX-ray1.76A1-122[»]
ProteinModelPortaliP04084.
SMRiP04084. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-220264.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiP04084.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
[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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of the inhibitor of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes)."
    Mancheva I., Kleinschmidt T., Aleksiev B., Braunitzer G.
    Hoppe-Seyler's Z. Physiol. Chem. 365:885-894(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: Bulgarian.
    Tissue: Venom.
  2. "Acute toxicity of vipoxin and its components: is the acidic component an 'inhibitor' of PLA2 toxicity?"
    Atanasov V.N., Stoykova S., Goranova Y., Mitewa M., Petrova S.
    Interdiscip. Toxicol. 5:169-172(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, LETHAL DOSES.
  3. "Crystallization and preliminary X-ray analysis of vipoxin, a complex between a toxic phospholipase A2 and its natural polypeptide inhibitor."
    Betzel C., Visanji M., Wilson K.S., Genov N., Mancheva I., Aleksiev B., Singh T.P.
    J. Mol. Biol. 231:498-500(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    Tissue: Venom.
  4. "Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution."
    Perbandt M., Wilson J.C., Eschenburg S., Mancheva I., Aleksiev B., Genov N., Willingmann P., Weber W., Singh T.P., Betzel C.
    FEBS Lett. 412:573-577(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH VIPOXIN B CHAIN, DISULFIDE BONDS.
  5. "X-ray structure at 1.76-A resolution of a polypeptide phospholipase A2 inhibitor."
    Devedjiev Y., Popov A., Atanasov B., Bartunik H.-D.
    J. Mol. Biol. 266:160-172(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), SEQUENCE REVISION TO 34.
    Tissue: Venom.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH VIPOXIN B CHAIN, DISULFIDE BONDS.
  7. "The X-ray structure of a snake venom Gln48 phospholipase A2 at 1.9A resolution reveals anion-binding sites."
    Georgieva D.N., Perbandt M., Rypniewski W., Hristov K., Genov N., Betzel C.
    Biochem. Biophys. Res. Commun. 316:33-38(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF HOMODIMER IN COMPLEX WITH SULFATE IONS WHICH MIMIC THE TARGET MEMBRANE, DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiPA2A_VIPAE
AccessioniPrimary (citable) accession number: P04084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: July 15, 1998
Last modified: May 11, 2016
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Caution

In contrast to other phospholipases, it lacks the typical His active site (His->Gln in position 47).Curated
The acidic chain was originally postulated to act as an inhibitor of the basic chain.1 Publication

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.