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Protein

Basic phospholipase A2 RV-4

Gene
N/A
Organism
Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heterodimer RV-4/RV-7: acts as a presynaptic neurotoxin.
Monomer: snake venom phospholipase A2 (PLA2) that acts as a presynaptic neurotoxin. 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+By similarityNote: Binds 1 Ca2+ ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Calcium; via carbonyl oxygenBy similarity
Metal bindingi45 – 451Calcium; via carbonyl oxygenBy similarity
Metal bindingi47 – 471Calcium; via carbonyl oxygenBy similarity
Active sitei63 – 631By similarity
Metal bindingi64 – 641CalciumBy similarity
Active sitei105 – 1051By 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 RV-4 (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
F4
Phosphatidylcholine 2-acylhydrolase
S2
Viperotoxin F
Viperotoxin toxic basic component
OrganismiDaboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Taxonomic identifieri343250 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 0.32 mg/kg by intravenous injection for RV-4 and 0.15 mg/kg for RV-4/RV-7 complex.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16162 PublicationsAdd
BLAST
Chaini17 – 138122Basic phospholipase A2 RV-4PRO_0000022977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 1311 Publication
Disulfide bondi44 ↔ 601 Publication
Disulfide bondi59 ↔ 1111 Publication
Disulfide bondi65 ↔ 1381 Publication
Disulfide bondi66 ↔ 1041 Publication
Disulfide bondi73 ↔ 971 Publication
Disulfide bondi91 ↔ 1021 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of a weakly toxic basic protein having phospholipase A2 activity (RV-4) and a non-toxic acidic protein which inhibits its enzymatic activity but potentiates its lethal potency and neurotoxicity (RV-7).

Structurei

Secondary structure

1
138
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 2912Combined sources
Helixi33 – 375Combined sources
Beta strandi38 – 403Combined sources
Turni41 – 433Combined sources
Beta strandi44 – 463Combined sources
Helixi55 – 6814Combined sources
Turni75 – 773Combined sources
Beta strandi82 – 854Combined sources
Beta strandi88 – 914Combined sources
Helixi97 – 11418Combined sources
Turni115 – 1184Combined sources
Helixi121 – 1233Combined sources
Helixi128 – 1314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OQSX-ray1.90B/D/F/H17-138[»]
ProteinModelPortaliQ02471.
SMRiQ02471. Positions 17-138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02471.

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.

Q02471-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLWIVAVC LIGVEGNLFQ FARMINGKLG AFSVWNYISY GCYCGWGGQG
60 70 80 90 100
TPKDATDRCC FVHDCCYGGV KGCNPKLAIY SYSFQRGNIV CGRNNGCLRT
110 120 130
ICECDRVAAN CFHQNKNTYN KEYKFLSSSK CRQRSEQC
Length:138
Mass (Da):15,555
Last modified:July 1, 1993 - v1
Checksum:iBFD471C8BBFE7F77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68385 mRNA. Translation: CAA48456.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68385 mRNA. Translation: CAA48456.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OQSX-ray1.90B/D/F/H17-138[»]
ProteinModelPortaliQ02471.
SMRiQ02471. Positions 17-138.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiQ02471.

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 and molecular cloning of neurotoxic phospholipases A2 from Taiwan viper (Vipera russelli formosensis)."
    Wang Y.-M., Lu P.-J., Ho C.-L., Tsai I.-H.
    Eur. J. Biochem. 209:635-641(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-66, FUNCTION.
    Tissue: Venom and Venom gland.
  2. "Two types of Russell's viper revealed by variation in phospholipases A2 from venom of the subspecies."
    Tsai I.-H., Lu P.-J., Su J.-C.
    Toxicon 34:99-109(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-66, FUNCTION, LETHAL DOSE.
    Tissue: Venom.
  3. "Structure of the heterodimeric neurotoxic complex viperotoxin F (RV-4/RV-7) from the venom of Vipera russelli formosensis at 1.9 A resolution."
    Perbandt M., Tsai I.-H., Fuchs A., Banumathi S., Rajashankar K.R., Georgieva D., Kalkura N., Singh T.P., Genov N., Betzel C.
    Acta Crystallogr. D 59:1679-1687(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-138, DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiPA2B4_DABSI
AccessioniPrimary (citable) accession number: Q02471
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 100 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.