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Entry version 118 (18 Sep 2019)
Sequence version 2 (01 Mar 1992)
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Protein

Basic phospholipase A2 ammodytoxin A

Gene
N/A
Organism
Vipera ammodytes ammodytes (Western sand viper)
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 acts as a presynaptic neurotoxin, an inhibitor of blood coagulation, and has been found to bind with high affinity to intracellular proteins. The response of indirectly stimulated neuromuscular preparations to ammodytoxin (Atx) is triphasic. The first phase, the transient inhibition of the acetylcholine (ACh) release, starts soon after the addition of Atx and lasts for several minutes. This phase is probably independent of Atx enzymatic activity. The effect may be due to the specific binding of the toxin to presynaptic receptors. These receptors, called N-type receptors, are still unidentified. It is noteworthy that a neuronal isoform of the M-type PLA2 receptor (R180) has been identified as a high-affinity receptor for Atx in neuronal plasma membranes. It was demonstrated however that this receptor is not essential for expression of neurotoxicity by Atx. The second phase corresponds to an augmentation of neurotransmitter release. A peak is reached 10-20 min after exposure of the preparation to Atx and is followed by a gradual reduction. In this phase, the enzymatic activity of Atx of the mammalian is not significant. It is speculated that the increased release of neurotransmitter in this phase is induced by the interference of Atx with voltage-gated potassium channels. Measurements of ionic currents showed however that voltage-gated potassium channels are not affected by Atx. The third phase of the response of neuromuscular preparations to Atx, which corresponds to a complete and irreversible paralysis, is clearly dependent on the hydrolytic activity of the toxin. In addition to its presynaptic neurotoxicity, Atx shows an anticoagulant activity by binding with high affinity to activated coagulation factor X (F10) thus inhibiting the formation of the prothrombinase complex (FX/FV) and its activity (IC50 is 20 nM). Surprisingly, Atx was discovered to bind intracellular proteins such as calmodulin (CaM) (IC50 is 6 nM), 14-3-3 proteins gamma (YWHAG) and epsilon (YWHAE) (by similarity with AtxC), as well as R25 (by similarity with AtxC), a mitochondrial integral membrane protein found in cerebral cortex. These findings raised a doubt about the dogma of the exclusively extracellular action of PLA2s, defended by the potential instability of these molecules in the reducing environment of the eukaryotic cytosol coupled with their possible inability to act as enzymes in this cellular compartment, due to too low concentration of calcium ions. This hypothesis was challenged efficiently by demonstrating the internalization of AtxA into a culture cells, but still remains to be directly demonstrated in vivo. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.5 Publications

Miscellaneous

Does not affect mKv1.1/KCNA1, rKv1.2/KCNA2, mKv1.3/KCNA3, hKv1.5/KCNA5 and mKv3.1/KCNC1 voltage-gated potassium channels.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+1 PublicationNote: Binds 1 Ca2+ ion.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei18Putative membrane binding site1
Sitei19Putative membrane binding site1
Sitei34Putative membrane binding site1
Sitei35Putative membrane binding site1
Sitei39Putative membrane binding site1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi43Calcium; via carbonyl oxygenBy similarity1
Metal bindingi45Calcium; via carbonyl oxygenBy similarity1
Sitei46Putative membrane binding site1
Metal bindingi47Calcium; via carbonyl oxygenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei63By similarity1
Metal bindingi64CalciumBy similarity1
Sitei76Putative membrane binding site1
Sitei77Putative membrane binding site1
Sitei79Putative membrane binding site1
Sitei82Putative membrane binding site1
Active sitei105By similarity1
Sitei124Putative membrane binding site1
Sitei125Putative membrane binding site1
Sitei129Putative membrane binding site1

<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

GO - Biological processi

<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 functionBlood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Hydrolase, Neurotoxin, Presynaptic neurotoxin, 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:
Basic phospholipase A2 ammodytoxin A (EC:3.1.1.4)
Short name:
AtxA
Short name:
svPLA2
Alternative name(s):
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>OrganismiVipera ammodytes ammodytes (Western sand viper)
<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 identifieri8705 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Host cytoplasm, 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 is 0.021 mg/kg by intravenous injection into mice.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi39F → A: Is 4-fold less toxic than wild-type AtxA, is similarly enzymatically active on anionic POPG vesicles and 3.2-fold less active on zwitterionic POPC vesicles. 2 Publications1
Mutagenesisi39F → N: Is 130-fold less toxic than wild-type AtxA, is similarly enzymatically active on anionic POPG vesicles and 3.5-fold less active on zwitterionic POPC vesicles. 2 Publications1
Mutagenesisi39F → S: Is 18-fold less toxic than wild-type AtxA, is similarly enzymatically active on anionic POPG vesicles and 5.4-fold less active on zwitterionic POPC vesicles. 2 Publications1
Mutagenesisi39F → W: Is 8-fold less toxic than wild-type AtxA, is similarly enzymatically active on anionic POPG vesicles and on zwitterionic POPC vesicles. 2 Publications1
Mutagenesisi39F → Y: Is 16-fold less toxic than wild-type AtxA, is similarly enzymatically active on anionic POPG vesicles and on zwitterionic POPC vesicles. 2 Publications1
Mutagenesisi46V → W: Is 6-fold less toxic than wild-type AtxA, has 2-fold higher enzymatic activity on anionic POPG vesicles and 27-fold more active on zwitterionic POPC vesicles. 1 Publication1
Mutagenesisi79R → E: Is 4-fold less toxic than wild-type AtxA, has 2.5-fold lower enzymatic activity on anionic POPG vesicles and 6-fold on zwitterionic POPC vesicles, and has 8.5-fold lower activity in inhibiting prothrombinase activity. 2 Publications1
Mutagenesisi79R → I: Is 1.5-fold less toxic than wild-type AtxA, and has 1.5-fold higher enzymatic activity on anionic POPG and 3.5-fold on zwitterionic POPC vesicles. 2 Publications1
Mutagenesisi79R → K: Is 2.4-fold less toxic than wild-type AtxA, and has 1.6-fold lower enzymatic activity on anionic POPG vesicles and 1.6-fold on zwitterionic POPC vesicles. 2 Publications1
Mutagenesisi79R → S: Is 2.6-fold less toxic than wild-type AtxA, has 1.4-fold lower enzymatic activity on anionic POPG vesicles and 1.2-fold on zwitterionic POPC vesicles, and has 3.5-fold lower activity in inhibiting prothrombinase activity. 2 Publications1
Mutagenesisi81 – 84KYHR → SYSL: Is 13-fold less toxic than wild-type AtxA, has 1.2-fold lower enzymatic activity on anionic POPG vesicles and 1.7-fold on zwitterionic POPC vesicles, and has 19-fold lower activity in inhibiting prothrombinase activity. 2 Publications4
Mutagenesisi93K → A: Is 1.1-fold less toxic than wild-type AtxA, and has 1.3-fold lower enzymatic activity on anionic POPG vesicles and 1.4-fold on zwitterionic POPC vesicles. 1 Publication1
Mutagenesisi93K → E: Is 1.5-fold less toxic than wild-type AtxA, and has 1.1-fold lower enzymatic activity on anionic POPG vesicles and 1.2-fold on zwitterionic POPC vesicles. 1 Publication1
Mutagenesisi93K → G: Is 1.6-fold less toxic than wild-type AtxA, and has 1.1-fold lower enzymatic activity on anionic POPG vesicles and 1.7-fold on zwitterionic POPC vesicles. 1 Publication1
Mutagenesisi93K → R: Is 1.5-fold less toxic than wild-type AtxA, and is similarly enzymatically active on anionic POPG vesicles and 1.4-fold less active on zwitterionic POPC vesicles. 1 Publication1
Mutagenesisi114K → N: Is 3-fold less toxic (by intraperitoneal injection) than wild-type AtxA (by intravenous injection), has 1.6-fold higher enzymatic activity, has 2.8-fold lower binding affinity for CaM, and has similar binding affinity for bovine brain receptor; when associated with N-117. 4 Publications1
Mutagenesisi114K → N: Is 30-fold less toxic than wild-type AtxA, has 3-fold higher enzymatic activity, has 20-fold lower activity in inhibiting prothrombinase activity, and has 4.5-fold lower binding affinity to CaM; when associated with N-117 and 132-T--E-137. 4 Publications1
Mutagenesisi117K → N: Is 3-fold less toxic (by intraperitoneal injection) than wild-type AtxA (by intravenous injection), has 1.6-fold higher enzymatic activity, has 2.8-fold lower binding affinity for CaM, and has similar binding affinity for bovine brain receptor; when associated with N-114. 4 Publications1
Mutagenesisi117K → N: Is 30-fold less toxic than wild-type AtxA, has 3-fold higher enzymatic activity, has 20-fold lower activity in inhibiting prothrombinase activity, and has 4.5-fold lower binding affinity to CaM; when associated with N-114 and 132-T--E-137. 4 Publications1
Mutagenesisi121 – 125YIYRN → KKYML: Is >200-fold less toxic than wild-type AtxA, is similarly enzymatically active on anionic POPG vesicles, and 5-fold more active on zwitterionic POPC vesicles, has 3.5-fold lower activity in inhibiting prothrombinase activity, and has 8.3-fold lower binding affinity for CaM. 4 Publications5
Mutagenesisi121 – 122YI → KK: Is <200-fold less toxic than wild-type AtxA, has 2-fold lower enzymatic activity (on phosphatidylcholine micelle), and has 3.5-fold lower binding affinity for CaM. 2 Publications2
Mutagenesisi132 – 137KKESEK → TETSEE: Is 30-fold less toxic than wild-type AtxA, has 3-fold higher enzymatic activity, has 20-fold lower activity in inhibiting prothrombinase activity, and has 4.5-fold lower binding affinity for CaM; when associated with N-114 and N-117. 3 Publications6
Mutagenesisi132K → T: Is 2-fold less toxic than wild-type AtxA, has slight lower enzymatic activity, has 7-fold lower activity in inhibiting prothrombinase activity and has 3.3-fold lower binding affinity to CaM. 1 Publication1
Mutagenesisi133K → E: Is 2-fold less toxic (by intraperitoneal injection) than wild-type AtxA (by intravenous injection), has similar enzymatic activity, has a slightly weaker binding affinity for bovine brain receptor, has 13-fold lower activity in inhibiting prothrombinase activity, and has 2.3-fold lower binding affinity for CaM. 2 Publications1

<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_000002297017 – 138Basic phospholipase A2 ammodytoxin AAdd 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 ↔ 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

<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.

<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

Monomer. Binds to calmodulin, coagulation factor X (F10), M-type PLA2 receptor (R-180). May also bind to 14-3-3 proteins gamma (YWHAG) and epsilon (YWHAE), and R25, a mitochondrial membrane protein.

<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

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

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SMRi
P00626

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00626

<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

Signal

Family and domain databases

Conserved Domains Database

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CDDi
cd00125 PLA2c, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.90.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR11716 PTHR11716, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00068 Phospholip_A2_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00389 PHPHLIPASEA2

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00085 PA2c, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48619 SSF48619, 1 hit

PROSITE; a protein domain and family database

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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>. 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_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.

P00626-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRTLWIVAVC LIGVEGSLLE FGMMILGETG KNPLTSYSFY GCYCGVGGKG
60 70 80 90 100
TPKDATDRCC FVHDCCYGNL PDCSPKTDRY KYHRENGAIV CGKGTSCENR
110 120 130
ICECDRAAAI CFRKNLKTYN YIYRNYPDFL CKKESEKC
Length:138
Mass (Da):15,531
Last modified:March 1, 1992 - v2
<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:iD9FAF40A04E31BB2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X53471 mRNA Translation: CAA37567.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39561 PSVIAA

<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
X53471 mRNA Translation: CAA37567.1
PIRiA39561 PSVIAA

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G8GX-ray1.70A17-138[»]
SMRiP00626
ModBaseiSearch...
PDBe-KBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00626

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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiPA2BA_VIPAA
<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: P00626
<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: July 21, 1986
Last sequence update: March 1, 1992
Last modified: September 18, 2019
This is version 118 of the entry and version 2 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 programAnimal Toxin Annotation Program
Annotation programChordata Protein 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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