UniProtKB - Q8AXY1 (PA2A_BOTJR)
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>sp|Q8AXY1|PA2A_BOTJR Acidic phospholipase A2 BthA-1 OS=Bothrops jararacussu OX=8726 PE=1 SV=1 MRTLWIMAVLLVGVEGSLWQFGKMINYVMGESGVLQYLSYGCYCGLGGQGQPTDATDRCC FVHDCCYGKVTGCDPKIDSYTYSKKNGDVVCGGDDPCKKQICECDRVATTCFRDNKDTYD IKYWFYGAKNCQEKSEPCHelp videoAdd a publicationFeedback
Protein
Acidic phospholipase A2 BthA-1
Gene
N/A
Organism
Bothrops jararacussu (Jararacussu)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Snake venom phospholipase A2 (PLA2) that displays edema-inducing activities (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.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.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, FUNCTION. - Ref.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, TOXIC DOSE, CRYSTALLIZATION.
Miscellaneous
This enzyme has been found to be not myotoxic, not cytotoxic, not hemorrhagic and not lethal.1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.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, TOXIC DOSE, CRYSTALLIZATION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- a 1,2-diacyl-sn-glycero-3-phosphocholineEC:3.1.1.4
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- See the description of this molecule in ChEBI.
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<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.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, TOXIC DOSE, CRYSTALLIZATION.
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- See the description of this EC number in ENZYME.
Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.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, TOXIC DOSE, CRYSTALLIZATION.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
a 1,2-diacyl-sn-glycero-3-phosphocholine- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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+H2O- Search proteins in UniProtKB for this molecule.
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=a 1-acyl-sn-glycero-3-phosphocholine- Search proteins in UniProtKB for this molecule.
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+a fatty acid- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Ca2+
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- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.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. - Ref.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.
Manual assertion inferred by curator fromi
- Ref.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. - Ref.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.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Inhibited by EDTA and bromophenacyl bromide (BPB).2 Publications
Manual assertion based on experiment ini
- Ref.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, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.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 IN COMPLEX WITH BROMOPHENACYL BROMIDE, DISULFIDE BONDS, ACTIVITY REGULATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 43 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 47 | Calcium; via amide nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 48 | Calcium; via amide nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 63 | 1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 64 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Active sitei | 105 | 1 Publication Manual assertion inferred by curator fromi
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- calcium ion binding Source: InterPro
- phospholipase A2 activity Source: UniProtKB-EC
- phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) Source: UniProtKB-EC
- phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) Source: UniProtKB-EC
- toxin activity Source: UniProtKB-KW
GO - Biological processi
- arachidonic acid secretion Source: InterPro
- defense response to bacterium Source: UniProtKB-KW
- lipid catabolic process Source: UniProtKB-KW
- phospholipid metabolic process Source: InterPro
- regulation of blood pressure Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Antibiotic, Antimicrobial, Blood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Hydrolase, Hypotensive agent, Platelet aggregation inhibiting toxin, Toxin |
| Biological process | Lipid degradation, Lipid metabolism |
| Ligand | Calcium, Metal-binding |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Acidic phospholipase A2 BthA-1 (EC:3.1.1.4
Manual assertion based on experiment ini
Short name: svPLA2 Alternative name(s): BOJU-III BthA-I-PLA21 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Hypotensive phospholipase A2 Phosphatidylcholine 2-acylhydrolase |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Bothrops jararacussu (Jararacussu) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 8726 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Extracellular region or secreted
- Secreted 2 Publications
Manual assertion based on experiment ini
- Ref.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, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.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, TOXIC DOSE, CRYSTALLIZATION.
- Secreted 2 Publications
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the lethal dose (LD), paralytic dose (PD), effect dose (ED) or lethal concentration (LC) of a protein toxin.<p><a href='/help/toxic_dose' target='_top'>More...</a></p>Toxic dosei
LD50 is 25 mg/kg by intraperitoneal injection into mice.1 Publication
Manual assertion based on experiment ini
- Ref.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, TOXIC DOSE, CRYSTALLIZATION.
LD50 is 7.5 mg/kg by intravenous injection into mice.1 Publication
Manual assertion based on experiment ini
- Ref.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, TOXIC DOSE, CRYSTALLIZATION.
LD50 is 0.5 mg/kg by intracerebroventricular injection.1 Publication
Manual assertion based on experiment ini
- Ref.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, TOXIC DOSE, CRYSTALLIZATION.
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 16 | 1 Publication Manual assertion based on experiment ini
| 16 | |
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000413804 | 17 – 138 | Acidic phospholipase A2 BthA-1Add BLAST | 122 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 42 ↔ 131 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 44 ↔ 60 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 59 ↔ 111 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 65 ↔ 138 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 66 ↔ 104 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 73 ↔ 97 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 91 ↔ 102 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
|
Keywords - PTMi
Disulfide bond<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Expressed by the venom gland.2 Publications
Manual assertion inferred by curator fromi
- Ref.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, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.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, TOXIC DOSE, CRYSTALLIZATION.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer; non-covalently linked.
3 PublicationsManual assertion based on experiment ini
- Ref.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, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.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. - Ref.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.
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 18 – 29 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 33 – 38 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 41 – 43 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 44 – 47 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 55 – 68 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Turni | 75 – 77 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 82 – 85 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 88 – 91 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 96 – 114 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| Helixi | 115 – 118 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 121 – 123 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 128 – 130 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8AXY1 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q8AXY1 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Keywords - Domaini
SignalFamily and domain databases
Conserved Domains Database More...CDDi | cd00125 PLA2c, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.90.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001211 PLipase_A2 IPR033112 PLipase_A2_Asp_AS IPR016090 PLipase_A2_dom IPR036444 PLipase_A2_dom_sf IPR033113 PLipase_A2_His_AS |
The PANTHER Classification System More...PANTHERi | PTHR11716 PTHR11716, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00068 Phospholip_A2_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00389 PHPHLIPASEA2 |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00085 PA2c, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48619 SSF48619, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00119 PA2_ASP, 1 hit PS00118 PA2_HIS, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
Q8AXY1-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »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
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i513647907BFD0F4E
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AY145836 mRNA Translation: AAN37410.1 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8AXY1 | Acidic phospholipase A2 (Fragment) | 60 | UniRef100_Q8AXY1 | |||
| +1 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8AXY1 | Acidic phospholipase A2 (Fragment) | 60 | UniRef90_Q8AXY1 | |||
| Acidic phospholipase A2 BpirPLA2-I | 122 | |||||
| +2 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8AXY1 | Basic phospholipase A2 ammodytoxin A | ) | 138 | UniRef50_P00626 | ||
| Basic phospholipase A2 vurtoxin | 138 | |||||
| Basic phospholipase A2 (Fragment) | 12 | |||||
| Acidic phospholipase A2 VP8 | 137 | |||||
| Acidic phospholipase A2 CC-PLA2-2 | 136 | |||||
| +528 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1U73 | X-ray | 1.90 | A/B | 17-138 | [»] | |
| 1UMV | X-ray | 1.79 | X | 17-138 | [»] | |
| 1Z76 | X-ray | 1.85 | A/B | 17-138 | [»] | |
| 1ZL7 | X-ray | 1.60 | A | 17-138 | [»] | |
| 1ZLB | X-ray | 0.97 | A | 17-138 | [»] | |
| SMRi | Q8AXY1 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | Q8AXY1 |
Family and domain databases
| CDDi | cd00125 PLA2c, 1 hit |
| Gene3Di | 1.20.90.10, 1 hit |
| InterProi | View protein in InterPro IPR001211 PLipase_A2 IPR033112 PLipase_A2_Asp_AS IPR016090 PLipase_A2_dom IPR036444 PLipase_A2_dom_sf IPR033113 PLipase_A2_His_AS |
| PANTHERi | PTHR11716 PTHR11716, 1 hit |
| Pfami | View protein in Pfam PF00068 Phospholip_A2_1, 1 hit |
| PRINTSi | PR00389 PHPHLIPASEA2 |
| SMARTi | View protein in SMART SM00085 PA2c, 1 hit |
| SUPFAMi | SSF48619 SSF48619, 1 hit |
| PROSITEi | View protein in PROSITE PS00119 PA2_ASP, 1 hit PS00118 PA2_HIS, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | PA2A_BOTJR | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q8AXY1Primary (citable) accession number: Q8AXY1 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 16, 2011 |
| Last sequence update: | March 1, 2003 | |
| Last modified: | April 22, 2020 | |
| This is version 86 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Annotation program | Animal Toxin Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
