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UniProtKB - Q8AXY1 (PA2A_BOTJR)

Entry version 81 (05 Dec 2018)
Sequence version 1 (01 Mar 2003)
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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>

<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 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

Miscellaneous

This enzyme has been found to be not myotoxic, not cytotoxic, not hemorrhagic and not lethal.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

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

<p>This subsection of the ‘Function’ 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 BPB.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi43CalciumCombined sources2 Publications1
Metal bindingi47Calcium; via amide nitrogenCombined sources2 Publications1
Metal bindingi48Calcium; via amide nitrogenCombined sources2 Publications1
<p>This subsection of the ‘Function’ 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 sitei631 Publication1
Metal bindingi64CalciumCombined sources2 Publications1
Active sitei1051 Publication1

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionAntibiotic, Antimicrobial, Blood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Hydrolase, Hypotensive agent, Platelet aggregation inhibiting toxin, Toxin
Biological processLipid degradation, Lipid metabolism
LigandCalcium, 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_and_taxonomy_section">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)
Short name:
svPLA2
Alternative name(s):
BOJU-III
BthA-I-PLA2
Hypotensive phospholipase A2
Phosphatidylcholine 2-acylhydrolase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiBothrops jararacussu (Jararacussu)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri8726 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › 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 Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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_and_biotech_section">'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 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

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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 peptidei1 – 161 PublicationAdd BLAST16
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000041380417 – 138Acidic phospholipase A2 BthA-1Add BLAST122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 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

<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

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; non-covalently linked.3 Publications

<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

1138
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q8AXY1

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q8AXY1

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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

Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG008137

Family 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 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
<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
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links 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

<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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137

Miscellaneous databases

EvolutionaryTraceiQ8AXY1

Family and domain databases

CDDicd00125 PLA2c, 1 hit
Gene3Di1.20.90.10, 1 hit
InterProiView 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
PANTHERiPTHR11716 PTHR11716, 1 hit
PfamiView protein in Pfam
PF00068 Phospholip_A2_1, 1 hit
PRINTSiPR00389 PHPHLIPASEA2
SMARTiView protein in SMART
SM00085 PA2c, 1 hit
SUPFAMiSSF48619 SSF48619, 1 hit
PROSITEiView protein in PROSITE
PS00119 PA2_ASP, 1 hit
PS00118 PA2_HIS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiPA2A_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>AccessioniPrimary (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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: March 1, 2003
Last modified: December 5, 2018
This is version 81 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal 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 sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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