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Entry version 47 (22 Nov 2017)
Sequence version 1 (05 Jul 2004)
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Protein

Bradykinin-potentiating and C-type natriuretic peptides

Gene
N/A
Organism
Bothrops jararaca (Jararaca) (Bothrops jajaraca)
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

Bradykinin-potentiating peptide 5a: modestly inhibits ACE (with highest affinity for the N-site) and reveals strong bradykinin-potentiating activity. Induces nitric oxide (NO) production depended on muscarinic acetylcholine receptor M1 subtype (CHRM1) and bradykinin B2 receptor (BDKRB2) activation. Both these receptors contribute to the vasodilation induced by this peptide that may have an indirect action on BDKRB2 and a direct agonistic action on CHRM1.
Bradykinin-potentiating peptide 10c: peptide with several activities. It inhibits the activity of the angiotensin-converting enzyme (ACE) by a preferential interaction with its C-domain (PubMed:11994001). It evokes transient hypotension (-14 mmHg) similar to that evoked by 0,5 µg of bradykinin, when injected alone into rats. It has a high bradykinin-potentiating effect (120%), when 60 nmol of BPP-10c are coinjected with 0.5 µg of bradykinin into rats (PubMed:22869554). Does not affect angiotensin-1 pressor effects. Shows potent and long-lasting antihypertensive activity as well as a reduction of the heart rate (PubMed:17475904). It also binds and dose-dependently promotes the activation of cytosolic argininosuccinate synthase (ASS1), an enzyme that catalyzes the conversion of citrulline, L-aspartate and ATP to argininosuccinate, AMP and pyrophosphate. It also enhances ASS1-dependent arginine production in HEK 293 cells, as well as in spontaneous hypertensive rat (SHR) and Wistar rat plasma. In addition, it induces the production of nitric-oxide (NO) by HUVEC cells via the endothelial nitric-oxide synthase (NOS3), which use arginine as a substrate and produce NO. It has been shown to be internalized by ASS1-expressing endothelial (HUVEC) and kidney (HEK 293) cells, and is detected homogenously distributed within the cell cytoplasm for up to 2 hours (PubMed:19491403).4 Publications
Bradykinin-potentiating peptide 10c-F: has much lower activity than the full-length bradykinin-potentiating peptides.1 Publication
Poly-His-poly-Gly peptide 1: may serve as a metalloproteinase inhibitor during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the victim.By similarity
Snake venom natriuretic peptide that exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity).By similarity

Miscellaneous

Does not bind to type-1 angiotensin-2 receptor (AGTR1).1 Publication
Bradykinin-potentiating peptide 10c-F is present only in female snakes.1 Publication

<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 functionG-protein coupled receptor impairing toxin, Hypotensive agent, Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor, Toxin, Vasoactive, Vasodilator

<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:
Bradykinin-potentiating and C-type natriuretic peptides
Alternative name(s):
BPP-CNP
Cleaved into the following 13 chains:
Bradykinin-potentiating peptide 6a1 Publication
Short name:
BPP-6a1 Publication
Bradykinin-potentiating peptide 10a2 Publications
Short name:
BPP-10a2 Publications
Alternative name(s):
Bradykinin-potentiating peptide IV-1-A2 Publications
Short name:
BPPIV-1-A1 Publication
Bradykinin-potentiating peptide V-81 Publication
Bradykinin-potentiating peptide 13a+QQWA1 Publication
Short name:
BPP-13a+QQWA1 Publication
Bradykinin-potentiating peptide 13a+QWA1 Publication
Short name:
BPP-13a+QWA1 Publication
Bradykinin-potentiating peptide 13a3 Publications
Short name:
BPP-13a3 Publications
Alternative name(s):
Bradykinin-potentiating peptide III-1-A2 Publications
Short name:
III-1-A1 Publication
Bradykinin-potentiating peptide V-91 Publication
Bradykinin-potentiating peptide 10c+QQWA1 Publication
Short name:
BPP-10c+QQWA1 Publication
Bradykinin-potentiating peptide 10c2 Publications
Short name:
BPP-10c2 Publications
Short name:
BPP-21 Publication
Alternative name(s):
Bradykinin-potentiating peptide IV-1-Bbeta1 Publication
Short name:
BPP IV-1-Bbeta1 Publication
Bradykinin-potentiating peptide V-71 Publication
Bradykinin-potentiating peptide 10c-F1 Publication
Short name:
BPP-10c-F1 Publication
Bradykinin-potentiating peptide 11b1 Publication
Short name:
BPP-11b1 Publication
Alternative name(s):
Bradykinin-potentiating peptide IIa
Short name:
BPP-IIa
Bradykinin-potentiating peptide IIb1 Publication
Short name:
BPP-IIb1 Publication
Bradykinin-potentiating peptide 5a1 Publication
Short name:
BPP-5a1 Publication
Alternative name(s):
Bradykinin-potentiating peptide Va1 Publication
Short name:
BPPVa1 Publication
Proline-rich peptide 5a1 Publication
Short name:
Bj-PRO-5a1 Publication
Short name:
PRO-5a1 Publication
Poly-His-poly-Gly peptide 11 Publication
Short name:
pHpG-11 Publication
C-type natriuretic peptide1 Publication
Alternative name(s):
Bj-CNP1 Publication
<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 jararaca (Jararaca) (Bothrops jajaraca)
<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 identifieri8724 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

<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

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

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>Mutagenesisi34P → A: Low decrease in ability to enhance AsS activity. 1 Publication1
Mutagenesisi36P → A: Low decrease in ability to enhance AsS activity. 1 Publication1
Mutagenesisi38I → A: Low decrease in ability to enhance AsS activity. 1 Publication1
Mutagenesisi39P → A: Important decrease in ability to enhance AsS activity. 1 Publication1
Mutagenesisi40P → A: Important decrease in ability to enhance AsS activity. 1 Publication1

<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 – 23Sequence analysisAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000025205024 – 30Curated7
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000025205131 – 40Bradykinin-potentiating peptide 10a3 Publications10
PeptideiPRO_000029202931 – 36Bradykinin-potentiating peptide 6a1 Publication6
PropeptideiPRO_000025205241 – 431 Publication3
PeptideiPRO_000042296144 – 60Bradykinin-potentiating peptide 13a+QQWA1 PublicationAdd BLAST17
PeptideiPRO_000042296245 – 60Bradykinin-potentiating peptide 13a+QWA1 PublicationAdd BLAST16
PeptideiPRO_000025205348 – 60Bradykinin-potentiating peptide 13a6 PublicationsAdd BLAST13
PropeptideiPRO_000025205461 – 63Curated3
PeptideiPRO_000042296364 – 77Bradykinin-potentiating peptide 10c+QQWA1 PublicationAdd BLAST14
PeptideiPRO_000025205568 – 77Bradykinin-potentiating peptide 10c4 Publications10
PeptideiPRO_000029203068 – 73Bradykinin-potentiating peptide 10c-F1 Publication6
PropeptideiPRO_000025205678 – 841 Publication7
PeptideiPRO_000025205785 – 95Bradykinin-potentiating peptide 11b1 Publication1 PublicationAdd BLAST11
PropeptideiPRO_000025205896 – 102Curated7
PeptideiPRO_0000252059103 – 113Bradykinin-potentiating peptide IIb1 PublicationAdd BLAST11
PropeptideiPRO_0000252060114 – 116Curated3
PeptideiPRO_0000252061117 – 121Bradykinin-potentiating peptide 5a1 Publication5
PropeptideiPRO_0000252062122Curated1
PeptideiPRO_0000252063123 – 127Bradykinin-potentiating peptide 5a1 Publication5
PropeptideiPRO_0000252064128 – 207CuratedAdd BLAST80
PeptideiPRO_0000421887208 – 225Poly-His-poly-Gly peptide 11 PublicationAdd BLAST18
PropeptideiPRO_0000421888226 – 234Curated9
PeptideiPRO_0000252065235 – 256C-type natriuretic peptide1 PublicationAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei31Pyrrolidone carboxylic acid3 Publications1
Modified residuei44Pyrrolidone carboxylic acid1 Publication1
Modified residuei45Pyrrolidone carboxylic acid1 Publication1
Modified residuei48Pyrrolidone carboxylic acid6 Publications1
Modified residuei64Pyrrolidone carboxylic acid1 Publication1
Modified residuei68Pyrrolidone carboxylic acid5 Publications1
Modified residuei85Pyrrolidone carboxylic acid1 Publication1
Modified residuei103Pyrrolidone carboxylic acid1 Publication1
Modified residuei117Pyrrolidone carboxylic acid1 Publication1
Modified residuei123Pyrrolidone carboxylic acid1 Publication1
<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 bondi240 ↔ 256By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Pyrrolidone carboxylic acid

<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 in venom gland.4 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

BPP-10a, BPP-10c+QQWA, BPP-13a, BPP-13+QWA and BPP-13A+QQWA seem to be found in both adult and newborn B.jararaca venoms.1 Publication

<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

GO - Molecular functioni

<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

3D structure databases

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

More...
SMRi
Q6LEM5

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi34 – 135Pro-richSequence analysisAdd BLAST102
Compositional biasi216 – 255Gly-richSequence analysisAdd BLAST40

<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

In the N-terminal section; belongs to the bradykinin-potentiating peptide family.Curated
In the central section; belongs to the pHpG family.Curated
In the C-terminal section; belongs to the natriuretic peptide family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG073115

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000663 Natr_peptide
IPR030480 Natr_peptide_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00212 ANP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00710 NATPEPTIDES

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00183 NAT_PEP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00263 NATRIURETIC_PEPTIDE, 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.

Q6LEM5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLSRLAASG LLLLALLALS VDGKPVQQWA QSWPGPNIPP LKVQQWAQGG
60 70 80 90 100
WPRPGPEIPP LTVQQWAQNW PHPQIPPLTV QQWAQGRAPG PPIPPLTVQQ
110 120 130 140 150
WAQGRAPHPP IPPAPLQKWA PLQKWAPLLQ PHESPASGTT ALREELSLGP
160 170 180 190 200
EAASGVPSAG AEVGRSGSKA PAAPHRLSKS KGAAATRPMR DLRPDGKQAR
210 220 230 240 250
QNWGRMAHHD HHAAAGGGGG GGGGARRLKG LAKKGAAKGC FGLKLDRIGT

MSGLGC
Length:256
Mass (Da):26,814
Last modified:July 5, 2004 - 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:i85DBDBA0A9520A45
GO

<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 611.7 Da from positions 117 - 121. Determined by ESI. BPP-5a.1 Publication
Molecular mass is 653.7 Da from positions 31 - 36. Determined by ESI. BPP-6a.1 Publication
Molecular mass is 1075.2 Da from positions 31 - 40. Determined by ESI. BPP-10a.1 Publication
Molecular mass is 1196.3 Da from positions 68 - 77. Determined by ESI. BPP-10c.1 Publication
Molecular mass is 1196.65 Da from positions 68 - 77. Determined by MALDI. BPP-10c.1 Publication
Molecular mass is 1195.6 Da from positions 68 - 77. Determined by ESI. 1 Publication
Molecular mass is 760.33 Da from positions 68 - 73. Determined by MALDI. BPP-10c-F.1 Publication
Molecular mass is 1069.2 Da from positions 85 - 95. Determined by ESI. BPP-11b.1 Publication
Molecular mass is 1370.76 Da from positions 48 - 60. Determined by MALDI. BPP-13a.1 Publication
Molecular mass is 1370.5 Da from positions 48 - 60. Determined by ESI. BPP-13a.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
D85843 mRNA Translation: BAA12879.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A01253 XAVI9B

<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
D85843 mRNA Translation: BAA12879.1
PIRiA01253 XAVI9B

3D structure databases

SMRiQ6LEM5
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG073115

Family and domain databases

InterProiView protein in InterPro
IPR000663 Natr_peptide
IPR030480 Natr_peptide_CS
PfamiView protein in Pfam
PF00212 ANP, 1 hit
PRINTSiPR00710 NATPEPTIDES
SMARTiView protein in SMART
SM00183 NAT_PEP, 1 hit
PROSITEiView protein in PROSITE
PS00263 NATRIURETIC_PEPTIDE, 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 nameiBNP1_BOTJA
<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: Q6LEM5
Secondary accession number(s): P01020, P30421, P68516
<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: October 3, 2006
Last sequence update: July 5, 2004
Last modified: November 22, 2017
This is version 47 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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