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Protein

Basic phospholipase A2 VRV-PL-VIIIa

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

Functioni

Snake venom phospholipase A2 (PLA2) that shows weak neurotoxicity and medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC50 is 130 nM) (PubMed:18062812). It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.3 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 bindingi27 – 271Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi29 – 291Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi31 – 311Calcium; via carbonyl oxygenCombined sources1 Publication
Active sitei47 – 471By similarity
Metal bindingi48 – 481CalciumCombined sources1 Publication
Active sitei89 – 891By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Hydrolase, Myotoxin, Neurotoxin, Presynaptic neurotoxin, Toxin

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.4. 5485.

Names & Taxonomyi

Protein namesi
Recommended name:
Basic phospholipase A2 VRV-PL-VIIIa (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
DPLA2
P1
Phosphatidylcholine 2-acylhydrolase
Phospholipase A2 4
Short name:
PLA24
OrganismiDaboia russelii (Russel's viper) (Vipera russelii)
Taxonomic identifieri31159 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is between 5.3 and 5.5 mg/kg by intravenous injection into mice.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121121Basic phospholipase A2 VRV-PL-VIIIaPRO_0000161717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 115Combined sources3 Publications
Disulfide bondi28 ↔ 44Combined sources3 Publications
Disulfide bondi43 ↔ 95Combined sources3 Publications
Disulfide bondi49 ↔ 121Combined sources3 Publications
Disulfide bondi50 ↔ 88Combined sources3 Publications
Disulfide bondi57 ↔ 81Combined sources3 Publications
Disulfide bondi75 ↔ 86Combined sources3 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Helixi17 – 204Combined sources
Beta strandi22 – 243Combined sources
Turni25 – 273Combined sources
Beta strandi28 – 303Combined sources
Beta strandi32 – 343Combined sources
Helixi39 – 5214Combined sources
Beta strandi55 – 573Combined sources
Turni59 – 613Combined sources
Beta strandi66 – 694Combined sources
Beta strandi72 – 754Combined sources
Helixi80 – 9819Combined sources
Helixi99 – 1024Combined sources
Helixi105 – 1073Combined sources
Helixi112 – 1143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CL5X-ray2.45A/B1-38[»]
1FB2X-ray1.95A/B1-49[»]
1FV0X-ray1.70A/B1-49[»]
1JQ8X-ray2.00A/B1-121[»]
1JQ9X-ray1.80A/B1-121[»]
1KPMX-ray1.80A/B1-50[»]
1OXLX-ray1.80A/B1-111[»]
1OYFX-ray2.45A1-121[»]
1SKGX-ray1.21A1-121[»]
1SQZX-ray1.20A1-111[»]
1SV3X-ray1.35A1-50[»]
1SV9X-ray2.71A1-111[»]
1SXKX-ray1.21A1-111[»]
1TDVX-ray1.70A1-121[»]
1TG1X-ray1.25A1-121[»]
1TG4X-ray1.70A1-121[»]
1TGMX-ray1.86A1-121[»]
1TH6X-ray1.23A1-121[»]
1TJ9X-ray1.10A1-121[»]
1TJKX-ray1.25A1-121[»]
1TK4X-ray1.10A1-111[»]
1TP2X-ray2.40A/B1-111[»]
1Y38X-ray2.44A/B1-121[»]
1ZR8X-ray2.03A1-111[»]
1ZWPX-ray1.10A1-111[»]
1ZYXX-ray1.95A1-121[»]
2B17X-ray2.71A1-121[»]
2DO2X-ray2.60A1-121[»]
2DPZX-ray2.10A1-121[»]
2FNXX-ray2.70A1-111[»]
2G58X-ray0.98A1-121[»]
2GNSX-ray2.30A1-121[»]
2O1NX-ray2.80A1-121[»]
2OLIX-ray2.21A1-121[»]
2OTFX-ray1.95A1-121[»]
2OTHX-ray2.90A1-121[»]
2OUBX-ray2.75A1-121[»]
2OYFX-ray1.20A1-121[»]
2PB8X-ray2.00A1-121[»]
2PMJX-ray2.40A1-121[»]
2PVTX-ray2.10A1-117[»]
2PWSX-ray2.21A1-121[»]
2PYCX-ray1.50A1-121[»]
2Q1PX-ray1.50A1-121[»]
2QHWX-ray2.21A1-121[»]
2QU9X-ray2.08A1-121[»]
2QUEX-ray2.25A1-121[»]
2QVDX-ray1.93A1-121[»]
2ZBHX-ray2.60A1-121[»]
3CBIX-ray3.15A/B/C/D1-121[»]
3G8FX-ray1.25A1-121[»]
3H1XX-ray1.40A1-121[»]
ProteinModelPortaliP59071.
SMRiP59071. Positions 1-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59071.

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.

P59071-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SLLEFGKMIL EETGKLAIPS YSSYGCYCGW GGKGTPKDAT DRCCFVHDCC
60 70 80 90 100
YGNLPDCNPK SDRYKYKRVN GAIVCEKGTS CENRICECDK AAAICFRQNL
110 120
NTYSKKYMLY PDFLCKGELK C
Length:121
Mass (Da):13,611
Last modified:November 1, 2002 - v1
Checksum:i5CDF82DDA7DA638E
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CL5X-ray2.45A/B1-38[»]
1FB2X-ray1.95A/B1-49[»]
1FV0X-ray1.70A/B1-49[»]
1JQ8X-ray2.00A/B1-121[»]
1JQ9X-ray1.80A/B1-121[»]
1KPMX-ray1.80A/B1-50[»]
1OXLX-ray1.80A/B1-111[»]
1OYFX-ray2.45A1-121[»]
1SKGX-ray1.21A1-121[»]
1SQZX-ray1.20A1-111[»]
1SV3X-ray1.35A1-50[»]
1SV9X-ray2.71A1-111[»]
1SXKX-ray1.21A1-111[»]
1TDVX-ray1.70A1-121[»]
1TG1X-ray1.25A1-121[»]
1TG4X-ray1.70A1-121[»]
1TGMX-ray1.86A1-121[»]
1TH6X-ray1.23A1-121[»]
1TJ9X-ray1.10A1-121[»]
1TJKX-ray1.25A1-121[»]
1TK4X-ray1.10A1-111[»]
1TP2X-ray2.40A/B1-111[»]
1Y38X-ray2.44A/B1-121[»]
1ZR8X-ray2.03A1-111[»]
1ZWPX-ray1.10A1-111[»]
1ZYXX-ray1.95A1-121[»]
2B17X-ray2.71A1-121[»]
2DO2X-ray2.60A1-121[»]
2DPZX-ray2.10A1-121[»]
2FNXX-ray2.70A1-111[»]
2G58X-ray0.98A1-121[»]
2GNSX-ray2.30A1-121[»]
2O1NX-ray2.80A1-121[»]
2OLIX-ray2.21A1-121[»]
2OTFX-ray1.95A1-121[»]
2OTHX-ray2.90A1-121[»]
2OUBX-ray2.75A1-121[»]
2OYFX-ray1.20A1-121[»]
2PB8X-ray2.00A1-121[»]
2PMJX-ray2.40A1-121[»]
2PVTX-ray2.10A1-117[»]
2PWSX-ray2.21A1-121[»]
2PYCX-ray1.50A1-121[»]
2Q1PX-ray1.50A1-121[»]
2QHWX-ray2.21A1-121[»]
2QU9X-ray2.08A1-121[»]
2QUEX-ray2.25A1-121[»]
2QVDX-ray1.93A1-121[»]
2ZBHX-ray2.60A1-121[»]
3CBIX-ray3.15A/B/C/D1-121[»]
3G8FX-ray1.25A1-121[»]
3H1XX-ray1.40A1-121[»]
ProteinModelPortaliP59071.
SMRiP59071. Positions 1-121.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Enzyme and pathway databases

BRENDAi3.1.1.4. 5485.

Miscellaneous databases

EvolutionaryTraceiP59071.

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. "Primary sequence determination of the most basic myonecrotic phospholipase A2 from the venom of Vipera russelli."
    Gowda T.V., Schmidt J., Middlebrook J.L.
    Toxicon 32:665-673(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, SUBUNIT.
    Tissue: Venom.
  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 1-50, FUNCTION, LETHAL DOSE.
    Tissue: Venom.
  3. "Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka."
    Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G., Athauda S.B., Moriyama A.
    Biomed. Res. 31:71-81(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-21, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Venom.
  4. "Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelli) venom."
    Kasturi S., Gowda T.V.
    Toxicon 27:229-237(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, LETHAL DOSE.
    Tissue: Venom.
  5. "Antibodies to a phospholipase A2 from Vipera russelli selectively neutralize venom neurotoxicity."
    Kasturi S., Rudrammaji L.M., Gowda T.V.
    Immunology 70:175-180(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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.
  7. "Three-dimensional structure of a presynaptic neurotoxic phospholipase A2 from Daboia russelli pulchella at 2.4 A resolution."
    Chandra V., Kaur P., Srinivasan A., Singh T.P.
    J. Mol. Biol. 296:1117-1126(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-38.
  8. "Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A resolution."
    Chandra V., Kaur P., Jasti J., Betzel C., Singh T.P.
    Acta Crystallogr. D 57:1793-1798(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-49.
  9. "Design of specific peptide inhibitors of phospholipase A2: structure of a complex formed between Russell's viper phospholipase A2 and a designed peptide Leu-Ala-Ile-Tyr-Ser (LAIYS)."
    Chandra V., Jasti J., Kaur P., Dey S., Srinivasan A., Betzel C., Singh T.P.
    Acta Crystallogr. D 58:1813-1819(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS.
  10. "Structural basis of phospholipase A2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 A crystal structure."
    Chandra V., Jasti J., Kaur P., Srinivasan A., Betzel C., Singh T.P.
    Biochemistry 41:10914-10919(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-49.
  11. "Crystal structure of a complex formed between a snake venom phospholipase A(2) and a potent peptide inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 A resolution."
    Chandra V., Jasti J., Kaur P., Dey S., Perbandt M., Srinivasan A., Betzel C., Singh T.P.
    J. Biol. Chem. 277:41079-41085(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), DISULFIDE BONDS.
  12. "Crystal structure of a complex formed between group II phospholipase A2 and aspirin at 1.86 A resolution."
    Singh N., Jabeen T., Sharma S., Bhushan A., Singh T.P.
    Submitted (MAY-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.

Entry informationi

Entry nameiPA2B8_DABRR
AccessioniPrimary (citable) accession number: P59071
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: May 11, 2016
This is version 101 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

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.