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UniProtKB - B8XH01 (LV1A_BUTOS)

Entry version 34 (25 May 2022)
Sequence version 1 (03 Mar 2009)
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Protein

Lipolysis-activating peptide 1-alpha chain

Gene
N/A
Organism
Buthus occitanus israelis (Common yellow scorpion) (Buthus israelis)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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

The heterodimer non-edited LVP1 induces lipolysis in rat adipocytes. Induction of lipolysis by LVP1 appears to be mediated through the beta-2 adrenergic receptor pathway (ADRB2) (By similarity).

By similarity

The edited BmKBTx-like, similar to beta-toxins, may modulate voltage-gated sodium channels (Nav) and may block voltage-gated potassium channels (Kv).

Curated

<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

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionG-protein coupled receptor impairing toxin, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin, Voltage-gated sodium channel impairing toxin

<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:
Lipolysis-activating peptide 1-alpha chain
Short name:
BoiLVP1-alpha
Short name:
LVP1-alpha
Alternative name(s):
Putative beta-like toxin Tx458
Short name:
BoiTx458
Putative beta-like toxin Tx651
Short name:
BoiTx651
Putative beta-like toxin Tx764
Short name:
BoiTx764
Putative beta-like toxin Tx814
Short name:
BoiTx814
Cleaved into the following chain:
Neurotoxin BmKBTx-like
Alternative name(s):
Putative excitatory toxin Tx135
Short name:
BoiTx135
<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>OrganismiButhus occitanus israelis (Common yellow scorpion) (Buthus israelis)
<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 identifieri539894 [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 lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Chelicerata › Arachnida › Scorpiones › Buthida › Buthoidea › Buthidae › Buthus ›

<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

Keywords - Cellular componenti

Secreted

<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 – 22By similarityAdd BLAST22
<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_000039486723 – 96Lipolysis-activating peptide 1-alpha chainAdd BLAST74
ChainiPRO_000039486823 – 80Neurotoxin BmKBTx-likeAdd BLAST58

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 bondi40 ↔ 63PROSITE-ProRule annotation
Disulfide bondi49 ↔ 68PROSITE-ProRule annotation
Disulfide bondi53 ↔ 70PROSITE-ProRule annotation
Disulfide bondi88Interchain (with C-90 in BotLVP1 chain beta)By similarity
<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 residuei96Lysine amideBy similarity1

Keywords - PTMi

Amidation, 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

Monomer (edited version) and heterodimer (non-edited version) of this alpha chain and a beta chain (AC B8XGZ8).

By similarity

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		B8XH01

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

More...SMRi		B8XH01

Database of comparative protein structure models

More...ModBasei		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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini26 – 89LCN-type CS-alpha/betaPROSITE-ProRule annotationAdd BLAST64

<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

Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).Curated

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the long (3 C-C) scorpion toxin superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.30.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR044062, LCN-type_CS_alpha_beta_dom
IPR036574, Scorpion_toxin-like_sf
IPR002061, Scorpion_toxinL/defensin

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00537, Toxin_3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57095, SSF57095, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51863, LCN_CSAB, 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.

B8XH01-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMKLVLFGII VILFSMIGSI HGSDPPGNYP LNTYGNKYAC TILGENDFCQ 
        60         70         80         90 
KICKVHGVQY GYCFNSRCWC EYLEEKDVNI WDAVKRHCKN TILYPKGK
Length:98
Mass (Da):11,247
Last modified:March 3, 2009 - 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:iC2E05BCAC06B4271
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 conflicti2M → I in ACJ23106 (Ref. 1) Curated1
Sequence conflicti2M → T in ACJ23112 (Ref. 1) Curated1
Sequence conflicti6L → I in ACJ23112 (Ref. 1) Curated1
Sequence conflicti10I → V in ACJ23106 (Ref. 1) Curated1
Sequence conflicti21H → L in ACJ23108 (Ref. 1) Curated1
Sequence conflicti21H → L in ACJ23109 (Ref. 1) Curated1
Sequence conflicti23 – 25SDP → TEA in ACJ23112 (Ref. 1) Curated3
Sequence conflicti23S → Y in ACJ23109 (Ref. 1) Curated1
Sequence conflicti33T → V in ACJ23109 (Ref. 1) Curated1
Sequence conflicti39A → V in ACJ23106 (Ref. 1) Curated1
Sequence conflicti41T → R in ACJ23106 (Ref. 1) Curated1
Sequence conflicti41T → R in ACJ23108 (Ref. 1) Curated1
Sequence conflicti41T → R in ACJ23109 (Ref. 1) Curated1
Sequence conflicti42I → A in ACJ23108 (Ref. 1) Curated1
Sequence conflicti42I → M in ACJ23109 (Ref. 1) Curated1
Sequence conflicti47D → E in ACJ23106 (Ref. 1) Curated1
Sequence conflicti47D → E in ACJ23108 (Ref. 1) Curated1
Sequence conflicti47D → E in ACJ23112 (Ref. 1) Curated1
Sequence conflicti47D → V in ACJ23109 (Ref. 1) Curated1
Sequence conflicti52I → V in ACJ23109 (Ref. 1) Curated1
Sequence conflicti55V → A in ACJ23106 (Ref. 1) Curated1
Sequence conflicti55V → L in ACJ23109 (Ref. 1) Curated1
Sequence conflicti58 – 59VQ → GH in ACJ23108 (Ref. 1) Curated2
Sequence conflicti58 – 59VQ → GH in ACJ23109 (Ref. 1) Curated2
Sequence conflicti59Q → K in ACJ23106 (Ref. 1) Curated1
Sequence conflicti59Q → K in ACJ23112 (Ref. 1) Curated1
Sequence conflicti74E → K in ACJ23106 (Ref. 1) Curated1
Sequence conflicti75E → D in ACJ23112 (Ref. 1) Curated1
Sequence conflicti75E → K in ACJ23108 (Ref. 1) Curated1
Sequence conflicti75E → K in ACJ23109 (Ref. 1) Curated1
Sequence conflicti78V → I in ACJ23112 (Ref. 1) Curated1
Sequence conflicti79N → S in ACJ23106 (Ref. 1) Curated1
Sequence conflicti79N → S in ACJ23108 (Ref. 1) Curated1
Sequence conflicti79N → S in ACJ23112 (Ref. 1) Curated1
Sequence conflicti82D → N in ACJ23112 (Ref. 1) Curated1
Sequence conflicti83A → T in ACJ23108 (Ref. 1) Curated1
Sequence conflicti86R → H in ACJ23108 (Ref. 1) Curated1
Sequence conflicti86R → H in ACJ23109 (Ref. 1) Curated1
Sequence conflicti86R → N in ACJ23112 (Ref. 1) Curated1
Sequence conflicti87H → Y in ACJ23109 (Ref. 1) Curated1
Sequence conflicti89K → N in ACJ23108 (Ref. 1) Curated1
Sequence conflicti89K → N in ACJ23109 (Ref. 1) Curated1
Sequence conflicti89K → T in ACJ23112 (Ref. 1) Curated1
Sequence conflicti93 – 96LYPK → VYSQ in ACJ23109 (Ref. 1) Curated4

<p>This subsection of the 'Sequence' section provides information relevant to all types of RNA editing events (conversion, insertion, deletion of nucleotides) that lead to one or more amino acid changes compared to the translation of the non-edited RNA version.<p><a href='/help/rna_editing' target='_top'>More...</a></p>RNA editingi

Edited at position 81.1 Publication
The stop codon (UGA) at position 81 is created by RNA editing.By similarity

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
FJ360790 mRNA Translation: ACJ23110.1
FJ360786 mRNA Translation: ACJ23106.1
FJ360788 mRNA Translation: ACJ23108.1
FJ360789 mRNA Translation: ACJ23109.1
FJ360792 mRNA Translation: ACJ23112.1

Keywords - Coding sequence diversityi

RNA editing

<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
FJ360790 mRNA Translation: ACJ23110.1
FJ360786 mRNA Translation: ACJ23106.1
FJ360788 mRNA Translation: ACJ23108.1
FJ360789 mRNA Translation: ACJ23109.1
FJ360792 mRNA Translation: ACJ23112.1

3D structure databases

AlphaFoldDBiB8XH01
SMRiB8XH01
ModBaseiSearch...

Family and domain databases

Gene3Di3.30.30.10, 1 hit
InterProiView protein in InterPro
IPR044062, LCN-type_CS_alpha_beta_dom
IPR036574, Scorpion_toxin-like_sf
IPR002061, Scorpion_toxinL/defensin
PfamiView protein in Pfam
PF00537, Toxin_3, 1 hit
SUPFAMiSSF57095, SSF57095, 1 hit
PROSITEiView protein in PROSITE
PS51863, LCN_CSAB, 1 hit

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 nameiLV1A_BUTOS
<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: B8XH01
Secondary accession number(s): B8XGZ7
, B8XGZ9, B8XH00, B8XH03
<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: June 15, 2010
Last sequence update: March 3, 2009
Last modified: May 25, 2022
This is version 34 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 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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