Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acidic phospholipase A2 BthA-1

Gene
N/A
Organism
Bothrops jararacussu (Jararacussu)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Snake venom phospholipase A2 (PLA2) that induces edema (activity that is inhibited by EDTA and dexamethasone), inhibits phospholipid-dependent collagen/ADP-induced platelet aggregation, possess hypotensive as well as anticoagulant activities. In addition, this enzyme shows bactericidal activity against E.coli and S.aureus. 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 annotation1 Publication

Cofactori

Ca2+2 PublicationsNote: Binds 1 Ca2+ ion per subunit.2 Publications

Enzyme regulationi

Inhibited by EDTA and BPB.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431CalciumCombined sources2 Publications
Metal bindingi47 – 471Calcium; via amide nitrogenCombined sources2 Publications
Metal bindingi48 – 481Calcium; via amide nitrogenCombined sources2 Publications
Active sitei63 – 6311 Publication
Metal bindingi64 – 641CalciumCombined sources2 Publications
Active sitei105 – 10511 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Blood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Hydrolase, Hypotensive agent, Platelet aggregation inhibiting toxin, Toxin

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic phospholipase A2 BthA-1 (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
BOJU-III
BthA-I-PLA2
Hypotensive phospholipase A2
Phosphatidylcholine 2-acylhydrolase
OrganismiBothrops jararacussu (Jararacussu)
Taxonomic identifieri8726 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 show no toxicity when injected into mice: 25 mg/kg by intraperitoneal injection, 7.5 mg/kg by intravenous injection, and 0.5 mg/kg by intracerebroventricular injection.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 138122Acidic phospholipase A2 BthA-1PRO_0000413804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 131Combined sources3 Publications
Disulfide bondi44 ↔ 60Combined sources3 Publications
Disulfide bondi59 ↔ 111Combined sources3 Publications
Disulfide bondi65 ↔ 138Combined sources3 Publications
Disulfide bondi66 ↔ 104Combined sources3 Publications
Disulfide bondi73 ↔ 97Combined sources3 Publications
Disulfide bondi91 ↔ 102Combined sources3 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.2 Publications

Interactioni

Subunit structurei

Homodimer; non-covalently linked.3 Publications

Structurei

Secondary structure

1
138
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 2912Combined sources
Helixi33 – 386Combined sources
Turni41 – 433Combined sources
Beta strandi44 – 474Combined sources
Helixi55 – 6814Combined sources
Turni75 – 773Combined sources
Beta strandi82 – 854Combined sources
Beta strandi88 – 914Combined sources
Helixi96 – 11419Combined sources
Helixi115 – 1184Combined sources
Helixi121 – 1233Combined sources
Helixi128 – 1303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U73X-ray1.90A/B17-138[»]
1UMVX-ray1.79X17-138[»]
1Z76X-ray1.85A/B17-138[»]
1ZL7X-ray1.60A17-138[»]
1ZLBX-ray0.97A17-138[»]
ProteinModelPortaliQ8AXY1.
SMRiQ8AXY1. Positions 17-138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8AXY1.

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.

Q8AXY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLWIMAVL LVGVEGSLWQ FGKMINYVMG ESGVLQYLSY GCYCGLGGQG
60 70 80 90 100
QPTDATDRCC FVHDCCYGKV TGCDPKIDSY TYSKKNGDVV CGGDDPCKKQ
110 120 130
ICECDRVATT CFRDNKDTYD IKYWFYGAKN CQEKSEPC
Length:138
Mass (Da):15,456
Last modified:March 1, 2003 - v1
Checksum:i513647907BFD0F4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY145836 mRNA. Translation: AAN37410.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY145836 mRNA. Translation: AAN37410.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U73X-ray1.90A/B17-138[»]
1UMVX-ray1.79X17-138[»]
1Z76X-ray1.85A/B17-138[»]
1ZL7X-ray1.60A17-138[»]
1ZLBX-ray0.97A17-138[»]
ProteinModelPortaliQ8AXY1.
SMRiQ8AXY1. Positions 17-138.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiQ8AXY1.

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 and identification of a complete cDNA coding for a bactericidal and antitumoral acidic phospholipase A2 from Bothrops jararacussu venom."
    Roberto P.G., Kashima S., Marcussi S., Pereira J.O., Astolfi-Filho S., Nomizo A., Giglio J.R., Fontes M.R., Soares A.M., Franca S.C.
    Protein J. 23:273-285(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Venom and Venom gland.
  2. "Cloning and expression of an acidic platelet aggregation inhibitor phospholipase A2 cDNA from Bothrops jararacussu venom gland."
    Roberto P.G., Kashima S., Soares A.M., Chioato L., Faca V.M., Fuly A.L., Astolfi-Filho S., Pereira J.O., Franca S.C.
    Protein Expr. Purif. 37:102-108(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-138.
    Tissue: Venom gland.
  3. "Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops jararacussu snake venom."
    Andriao-Escarso S.H., Soares A.M., Fontes M.R., Fuly A.L., Correa F.M., Rosa J.C., Greene L.J., Giglio J.R.
    Biochem. Pharmacol. 64:723-732(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-50, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOXIC DOSE, CRYSTALLIZATION.
    Tissue: Venom.
  4. "Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A2 in the monomeric and dimeric states: insights into its oligomeric state."
    Magro A.J., Murakami M.T., Marcussi S., Soares A.M., Arni R.K., Fontes M.R.
    Biochem. Biophys. Res. Commun. 323:24-31(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 17-138 IN COMPLEX WITH CALCIUM ION, COFACTOR, SUBUNIT, DISULFIDE BONDS.
  5. "Structure of BthA-I complexed with p-bromophenacyl bromide: possible correlations with lack of pharmacological activity."
    Magro A.J., Takeda A.A., Soares A.M., Fontes M.R.
    Acta Crystallogr. D 61:1670-1677(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 17-138, DISULFIDE BONDS.
  6. "Insights into metal ion binding in phospholipases A2: ultra high-resolution crystal structures of an acidic phospholipase A2 in the Ca2+ free and bound states."
    Murakami M.T., Gabdoulkhakov A., Genov N., Cintra A.C.O., Betzel C., Arni R.K.
    Biochimie 88:543-549(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 17-138 IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS.

Entry informationi

Entry nameiPA2A_BOTJR
AccessioniPrimary (citable) accession number: Q8AXY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 74 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

Miscellaneous

This enzyme has been found to be not myotoxic, not cytotoxic, not hemorrhagic and not lethal.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.