ID   LV1B_BUTOS              Reviewed;          98 AA.
AC   B8XGZ8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Lipolysis-activating peptide 1-beta chain;
DE            Short=BoiLVP1-beta;
DE            Short=LVP1-beta;
DE   AltName: Full=Putative beta-like toxin Tx457;
DE   Flags: Precursor;
OS   Buthus occitanus israelis (Common yellow scorpion) (Buthus israelis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=539894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zilberberg N., Kozminsky-Atias A.;
RT   "Buthus occitanus israelis scorpion toxin.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The homodimer inhibits HMG-CoA reductase (HMGCR) (32% of
CC       inhibition produced by 0.6 uM), a glycoprotein involved in the control
CC       of cholesterol biosynthesis. The inhibitory effects of bumarsin are
CC       seen at much lower concentrations (0.6 uM) than that for statins such
CC       as atorvastatin (5 mM) and simvastatin (10 uM). In addition to
CC       inhibition of HMG-CoA reductase, this protein lowers cholesterol levels
CC       by inducing steroid hormone synthesis via StAR, and by increasing
CC       reverse cholesterol transport mediated by the induction of ABCA1 and
CC       APOA1 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: The heterodimer non-edited LVP1 induces lipolysis in rat
CC       adipocytes. Induction of lipolysis by LVP1 appears to be mediated
CC       through the beta-2 adrenergic receptor pathway (ADRB2) (By similarity).
CC       {ECO:0000250|UniProtKB:P84809}.
CC   -!- FUNCTION: The monomer edited version, similar to alpha-toxins, may
CC       modulate voltage-gated sodium channels (Nav) and may block voltage-
CC       gated potassium channels (Kv). {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked or monomer (edited version) or
CC       heterodimer of an alpha chain (AC B8XH01) and this beta chain (non-
CC       edited version). {ECO:0000250|UniProtKB:Q95P90}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q95P90}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- RNA EDITING: Modified_positions=34 {ECO:0000250}; Note=Partially
CC       edited. RNA editing at this position consists of an insertion of three
CC       nucleotides, restoring the first Cys residue that forms a disulfide
CC       bond with Cys-90, giving a monomeric toxin with 4 disulfide bonds (By
CC       similarity). {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC       {ECO:0000305}.
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DR   EMBL; FJ360787; ACJ23107.1; -; mRNA.
DR   AlphaFoldDB; B8XGZ8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; G-protein coupled receptor impairing toxin;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   RNA editing; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..98
FT                   /note="Lipolysis-activating peptide 1-beta chain"
FT                   /id="PRO_0000394869"
FT   SITE            44
FT                   /note="Important for blocking potassium channels"
FT                   /evidence="ECO:0000250"
FT   SITE            47
FT                   /note="Important for blocking potassium channels"
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        90
FT                   /note="Interchain (with C-88 in BoiLVP1 chain alpha)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   98 AA;  11203 MW;  8454F90D2CC91FEE CRC64;
     MANVQVIFVA YIAVIAFSMV YGDDYKPFGE HNSYYGCKKQ TDEFCNKICK LHLAKKGGFC
     HQPAPFVELC KCLDIDYDNT YFLKAMEKQC PKLKGNVN