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Entry version 109 (26 Feb 2020)
Sequence version 1 (01 Mar 1992)
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Protein

Phospholipase A2 crotoxin basic chain CBa2

Gene
N/A
Organism
Crotalus durissus terrificus (South American rattlesnake)
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

Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity (PubMed:20109480). Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported (PubMed:20109480).1 Publication
Monomer CBa2: The basic subunit of crotoxin is a snake venom phospholipase A2 (PLA2) that exhibits weak neurotoxicity (10-fold less than the heterodimer) and strong anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC50 is 41 nM) (PubMed:18062812). In addition, it shows the same effects described for the heterodimer and binds the nucleotide-binding domain (NBD1) of CFTR chloride channels and increases the channel current (PubMed:27241308). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.2 Publications

Miscellaneous

The crotoxin heterodimer is inhibited by the crotoxin inhibitor from Crotalus serum (CICS). CICS neutralizes the lethal potency of crotoxin and inhibits its PLA2 activity. CICS only binds tightly to the CB subunit and induces the dissociation of the heterodimer (By similarity). Tested on the CA2-CBd heterodimer (PubMed:10903514).By similarity1 Publication

<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

<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+By similarityNote: Binds 1 Ca2+ ion.By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.06 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (monomer CBa2)1 Publication
  2. KM=0.05 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA2-CBa2)1 Publication
  3. KM=0.05 µM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA3-CBa2)1 Publication
  1. Vmax=24 µmol/min/mg enzyme (monomer CBa2)1 Publication
  2. Vmax=25 µmol/min/mg enzyme (class 2 heterodimer CA2-CBa2)1 Publication
  3. Vmax=24 µmol/min/mg enzyme (class 2 heterodimer CA3-CBa2)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>Sitei17Responsible for the weak stability and toxicity1 Publication1
Sitei18Putative interfacial binding surface (IBS)1 Publication1
Sitei19Putative interfacial binding surface (IBS)1 Publication1
Sitei23Putative interfacial binding surface (IBS)1 Publication1
Sitei26Putative interfacial binding surface (IBS)1 Publication1
Sitei33Putative interfacial binding surface (IBS)1 Publication1
Sitei34Putative interfacial binding surface (IBS)1 Publication1
Sitei38Putative interfacial binding surface (IBS)1 Publication1
Sitei39Putative interfacial binding surface (IBS)1 Publication1
<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 bindingi43Calcium; via carbonyl oxygenBy similarity1
Metal bindingi45Calcium; via carbonyl oxygenBy similarity1
Metal bindingi47Calcium; via carbonyl oxygenBy similarity1
<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 sitei63By similarity1
Metal bindingi64CalciumBy similarity1
Sitei76Putative interfacial binding surface (IBS)1 Publication1
Active sitei105By similarity1
Sitei119Putative interfacial binding surface (IBS)1 Publication1
Sitei133Responsible for the reduced anticoagulant activity (compared with CBc)1 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

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, Ion channel impairing toxin, Neurotoxin, Presynaptic neurotoxin, Toxin
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.4, 1711

<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:
Phospholipase A2 crotoxin basic chain CBa2 (EC:3.1.1.4)
Short name:
CB2
Short name:
CTX subunit CBa2
Short name:
svPLA2
Alternative name(s):
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>OrganismiCrotalus durissus terrificus (South American rattlesnake)
<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 identifieri8732 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

<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

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

In monomer CBa2, LD50 is 700 µg/kg by intravenous injection into mice.1 Publication
In monomer CBa2, LD50 is >3000 µg/kg by subcutaneous injection into mice.1 Publication
In class 2 heterodimer CA2-CBa2, LD50 is 420 µg/kg by intravenous injection into mice.1 Publication
In class 2 heterodimer CA2-CBa2, LD50 is 650 µg/kg by subcutaneous injection into mice.1 Publication
In class 2 heterodimer CA3-CBa2, LD50 is 450 µg/kg by intravenous injection into mice.1 Publication

<p>This subsection of the 'Pathology and Biotech' section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

May be used to develop new agents to treat the most common mutation of cystic fibrosis (DelF508CFTR). It shows a double function: (i) as a potentiator, by increasing the chloride channel current, and (ii) as a corrector, by permitting DelF508CFTR to escape from the degradation pathway, facilitating its biosynthesis and subsequent delivery to the plasma membrane.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 – 162 PublicationsAdd BLAST16
<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_000002286117 – 138Phospholipase A2 crotoxin basic chain CBa2Add 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 sources1 Publication
Disulfide bondi44 ↔ 60Combined sources1 Publication
Disulfide bondi59 ↔ 111Combined sources1 Publication
Disulfide bondi65 ↔ 138Combined sources1 Publication
Disulfide bondi66 ↔ 104Combined sources1 Publication
Disulfide bondi73 ↔ 97Combined sources1 Publication
Disulfide bondi91 ↔ 102Combined sources1 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%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

Heterodimer of one of the acidic (CA1, CA2, CA3 or CA4) and one of the basic (CBa1, CBa2, CBb, CBc or CBd) subunits; non-covalently linked. The acidic subunit is non-toxic, without enzymatic activity and comprises 3 peptides that are cross-linked by 5 disulfide bridges. The basic subunit is toxic, has phospholipase A2 activity and is composed of a single chain. Multiple variants of each subunit give different crotoxin complexes that can be subdivided into 2 classes: (1) those of high toxicity, low PLA2 activity (CBb, CBc and CBd linked with high affinity to any CA) and high stability (K(d)=4.5 nM) and (2) those of moderate toxicity, high PLA2 activity (CBa2 linked with low affinity to any CA) and low stability (K(d)=25 nM).

Interacts with human NBD1 domain of CFTR (PubMed:27241308).

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

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

More...
SMRi
P24027

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
P24027

<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

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.

P24027-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRALWIVAVL LVGVEGSLLQ FNKMIKFETR KNAVPFYAFY GCYCGWGGQG
60 70 80 90 100
RPKDATDRCC FVHDCCYGKL AKCNTKWDIY RYSLKSGYIT CGKGTWCKEQ
110 120 130
ICECDRVAAE CLRRSLSTYK NEYMFYPDSR CREPSETC
Length:138
Mass (Da):15,969
Last modified:March 1, 1992 - 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:i935D12258D47B058
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti34V → I AA sequence (PubMed:15032748).Curated1

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 14245±1 Da. Determined by ESI. 1 Publication
Molecular mass is 14244 Da. Determined by ESI. 1 Publication

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
X16100 mRNA Translation: CAA34227.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S15068, PSRSB2

<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
X16100 mRNA Translation: CAA34227.1
PIRiS15068, PSRSB2

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
2QOGX-ray2.28A/D17-138[»]
SMRiP24027
ModBaseiSearch...
PDBe-KBiSearch...

Enzyme and pathway databases

BRENDAi3.1.1.4, 1711

Miscellaneous databases

EvolutionaryTraceiP24027

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...

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 nameiPA2BA_CRODU
<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: P24027
Secondary accession number(s): P0DJN2
<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 historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: February 26, 2020
This is version 109 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, Pharmaceutical

Documents

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