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Protein

Pertussis toxin subunit 1

Gene

ptxA

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
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

S1 is an NAD-dependent ADP-ribosyltransferase, which plays a crucial role in the pathogenesis of B.pertussis causing disruption of normal host cellular regulation. It catalyzes the ADP-ribosylation of a cysteine in the alpha subunit of host heterotrimeric G proteins. In the absence of G proteins it also catalyzes the cleavage of NAD+ into ADP-ribose and nicotinamide. It irreversibly uncouples the G-alpha GTP-binding proteins from their membrane receptors.

Miscellaneous

Thiol:disulfide oxidoreductases DsbA and DsbB are required for periplasmic toxin assembly, whereas DbsC is important for extracellular toxin secretion.
Experiments with temporal expression of PTX indicate that holotoxin secretion is at a rate of 3 molecules/min/cell. Also, more of toxin chains S1, S2 and S3 are produced than secreted; one half of each chain is incorporated into holotoxin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei60NAD1
<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 sitei691
Active sitei1631

<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

<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 functionGlycosyltransferase, Toxin, Transferase
Biological processVirulence
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BPER257313:BP3783-MONOMER

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.C.72.1.1 the pertussis toxin (ptx) family

<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:
Pertussis toxin subunit 1
Short name:
PTX S1
Alternative name(s):
Islet-activating protein S1
Short name:
IAP S1
NAD-dependent ADP-ribosyltransferase (EC:2.4.2.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ptxA
Ordered Locus Names:BP3783
<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>OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
<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 identifieri257313 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002676 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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

  • Secreted 1 Publication
  • Note: The individual chains are secreted by a sec-dependent mechanism into the periplasm. Then, S1 associates with the outer membrane before it joins with the B subunit to form the secretion-competent holotoxin. The type IV secretion system ptl mediates secretion of assembled toxin through the outer membrane.

GO - Cellular componenti

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 ‘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

Currently used in vaccines available under the names Daptacel (Sanofi Pasteur), Infanrix (GlaxoSmithKline), Pediarix (GlaxoSmithKline), TriHIBit (Sanofi Pasteur) and Tripedia (Sanofi Pasteur).

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>Mutagenesisi75C → G: 38% of wild-type NAD-glycohydrolase activity. 1 Publication1
Mutagenesisi75C → S: 33% of wild-type NAD-glycohydrolase activity. 1 Publication1
Mutagenesisi75Missing : More than 100-fold reduction of NAD-glycohydrolase activity. 1 Publication1
Mutagenesisi88S → G: No functional toxin produced although some mature size S1 protein accumulates in the periplasm. 1 Publication1
Mutagenesisi89S → G: Very low amount of final toxin secreted; approximately 50% of wild-type toxin level accumulate in the periplasm despite near wild-type levels of mature size S1 in the periplasm. 1 Publication1
Mutagenesisi90S → G: Very low amount of final toxin secreted; approximately 50% of wild-type toxin level accumulate in the periplasm despite near wild-type levels of mature size S1 in the periplasm. 1 Publication1
Mutagenesisi91R → K: Very low amounts of final toxin secreted; about 60% of wild-type toxin levels accumulate in the periplasm. Near wild-type levels of mature size S1 in the periplasm. 1 Publication1
Mutagenesisi163E → D: Reduction of several orders of magnitude of enzymatic activity. 1 Publication1
Mutagenesisi163Missing : Dramatic decrease in enzymatic activity. 1 Publication1
Mutagenesisi269Missing : Affects both protein stability and outer membrane targeting. 1 Publication1

Keywords - Diseasei

Whooping cough

<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 – 34Add BLAST34
<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_000001935935 – 269Pertussis toxin subunit 1Add BLAST235

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 bondi75 ↔ 235

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P04977

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Activated by the two-component regulatory system BvgS/BvgA.

<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

Pertussis toxin contains five different chains, S1-S5. They are organized into 2 functional subunits: A, composed of S1 (which is toxic) and B, containing S2, S3, S5, and two copies of S4 (B binds to the membrane receptors). Dimers of S2-S4 and S3-S4 are held together by S5.1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
257313.BP3783

<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

1269
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
1BCPX-ray2.70A/G35-269[»]
1PRTX-ray2.90A/G36-269[»]
1PTOX-ray3.50A/G26-269[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P04977

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

More...
SMRi
P04977

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
P04977

<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 general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The region which spans amino acids 42-49 is required for enzymatic activity and contributes to the formation of a potentially important antigenic determinant.1 Publication

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4106DF6 Bacteria
ENOG410XY7Z LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000154667

KEGG Orthology (KO)

More...
KOi
K11023

Identification of Orthologs from Complete Genome Data

More...
OMAi
YIYQIRA

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003898 Borpert_toxA

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02917 Pertussis_S1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01395 BORPETOXINA

<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.

P04977-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRCTRAIRQT ARTGWLTWLA ILAVTAPVTS PAWADDPPAT VYRYDSRPPE
60 70 80 90 100
DVFQNGFTAW GNNDNVLDHL TGRSCQVGSS NSAFVSTSSS RRYTEVYLEH
110 120 130 140 150
RMQEAVEAER AGRGTGHFIG YIYEVRADNN FYGAASSYFE YVDTYGDNAG
160 170 180 190 200
RILAGALATY QSEYLAHRRI PPENIRRVTR VYHNGITGET TTTEYSNARY
210 220 230 240 250
VSQQTRANPN PYTSRRSVAS IVGTLVRMAP VIGACMARQA ESSEAMAAWS
260
ERAGEAMVLV YYESIAYSF
Length:269
Mass (Da):29,974
Last modified:August 13, 1987 - 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:iF6C88C16DA6B08AB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti68D → E in strain: 10536, CZ, 18323 and B6. 1
Natural varianti129N → S in strain: CS. 1
Natural varianti196S → P in strain: CZ and 18323. 1
Natural varianti228M → I in strain: 287, Al1561, B572, CHANG and HAV. 1
Natural varianti232I → M in strain: CZ and 18323. 1
Natural varianti232I → V in strain: 10536 and B6. 1

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
M14378 Genomic DNA Translation: AAA83980.1
M13223 Genomic DNA Translation: AAA22981.1
X16347 Genomic DNA Translation: CAA34397.1
AJ245366 Genomic DNA Translation: CAB51472.1
AJ245367 Genomic DNA Translation: CAB51542.1
AJ245368 Genomic DNA Translation: CAB51543.1
AJ506996 Genomic DNA Translation: CAD44970.1
AJ006151 Genomic DNA Translation: CAA06893.1
AJ006153 Genomic DNA Translation: CAA06895.1
AJ006155 Genomic DNA Translation: CAA06897.1
AJ006157 Genomic DNA Translation: CAA06899.1
AJ006159 Genomic DNA Translation: CAA06901.1
AJ007363 Genomic DNA Translation: CAA07478.1
AJ007364 Genomic DNA Translation: CAA07479.1
AJ506994 Genomic DNA Translation: CAD44968.1
AJ506995 Genomic DNA Translation: CAD44969.1
AY879289 Genomic DNA Translation: AAW72734.1
AJ920066 Genomic DNA Translation: CAI72620.1
BX640422 Genomic DNA Translation: CAE44038.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A24144 WEBR1P
A24394 WEBR11

NCBI Reference Sequences

More...
RefSeqi
NP_882282.1, NC_002929.2
WP_010931648.1, NC_002929.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAE44038; CAE44038; BP3783

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2665068

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bpe:BP3783

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|257313.5.peg.4087

<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
M14378 Genomic DNA Translation: AAA83980.1
M13223 Genomic DNA Translation: AAA22981.1
X16347 Genomic DNA Translation: CAA34397.1
AJ245366 Genomic DNA Translation: CAB51472.1
AJ245367 Genomic DNA Translation: CAB51542.1
AJ245368 Genomic DNA Translation: CAB51543.1
AJ506996 Genomic DNA Translation: CAD44970.1
AJ006151 Genomic DNA Translation: CAA06893.1
AJ006153 Genomic DNA Translation: CAA06895.1
AJ006155 Genomic DNA Translation: CAA06897.1
AJ006157 Genomic DNA Translation: CAA06899.1
AJ006159 Genomic DNA Translation: CAA06901.1
AJ007363 Genomic DNA Translation: CAA07478.1
AJ007364 Genomic DNA Translation: CAA07479.1
AJ506994 Genomic DNA Translation: CAD44968.1
AJ506995 Genomic DNA Translation: CAD44969.1
AY879289 Genomic DNA Translation: AAW72734.1
AJ920066 Genomic DNA Translation: CAI72620.1
BX640422 Genomic DNA Translation: CAE44038.1
PIRiA24144 WEBR1P
A24394 WEBR11
RefSeqiNP_882282.1, NC_002929.2
WP_010931648.1, NC_002929.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCPX-ray2.70A/G35-269[»]
1PRTX-ray2.90A/G36-269[»]
1PTOX-ray3.50A/G26-269[»]
ProteinModelPortaliP04977
SMRiP04977
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257313.BP3783

Protein family/group databases

TCDBi1.C.72.1.1 the pertussis toxin (ptx) family

Proteomic databases

PRIDEiP04977

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE44038; CAE44038; BP3783
GeneIDi2665068
KEGGibpe:BP3783
PATRICifig|257313.5.peg.4087

Phylogenomic databases

eggNOGiENOG4106DF6 Bacteria
ENOG410XY7Z LUCA
HOGENOMiHOG000154667
KOiK11023
OMAiYIYQIRA

Enzyme and pathway databases

BioCyciBPER257313:BP3783-MONOMER

Miscellaneous databases

EvolutionaryTraceiP04977

Family and domain databases

InterProiView protein in InterPro
IPR003898 Borpert_toxA
PfamiView protein in Pfam
PF02917 Pertussis_S1, 1 hit
PRINTSiPR01395 BORPETOXINA

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 nameiTOX1_BORPE
<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: P04977
Secondary accession number(s): O69258
, O70057, Q599G4, Q5EIB9, Q93V22
<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: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 7, 2018
This is version 128 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 programProkaryotic 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, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

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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