LV1B_BUTOC
ID LV1B_BUTOC Reviewed; 95 AA.
AC P84809;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Lipolysis-activating peptide 1-beta chain;
DE Short=BotLVP1-beta;
DE Short=LVP1-beta;
DE Flags: Precursor;
OS Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX NCBI_TaxID=6871;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-64 AND 76-95, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15680238; DOI=10.1016/j.bbapap.2004.09.020;
RA Soudani N., Gharbi-Chihi J., Srairi-Abid N., Martin-El Yazidi C.,
RA Planells R., Margotat A., Torresani J., El Ayeb M.;
RT "Isolation and molecular characterization of LVP1 lipolysis activating
RT peptide from scorpion Buthus occitanus tunetanus.";
RL Biochim. Biophys. Acta 1747:47-56(2005).
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).
CC Intracerebroventricular injection is not toxic to mice.
CC {ECO:0000269|PubMed:15680238}.
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|PubMed:15680238}.
CC -!- SUBUNIT: Homodimer; disulfide-linked or monomer (edited version) or
CC heterodimer of an alpha chain (AC P84810) and this beta chain (non-
CC edited version). {ECO:0000250|UniProtKB:Q95P90}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15680238}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15680238}.
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 -!- MASS SPECTROMETRY: Mass=8877; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15680238};
CC -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC {ECO:0000305}.
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DR AlphaFoldDB; P84809; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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 GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:UniProtKB.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor impairing toxin; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; RNA editing; Secreted;
KW Signal; Toxin; Voltage-gated potassium channel impairing toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15680238"
FT CHAIN 23..95
FT /note="Lipolysis-activating peptide 1-beta chain"
FT /id="PRO_0000232423"
FT DISULFID 37..60
FT /evidence="ECO:0000250|UniProtKB:P01493"
FT DISULFID 45..70
FT /evidence="ECO:0000250|UniProtKB:P01493"
FT DISULFID 49..72
FT /evidence="ECO:0000250|UniProtKB:P01493"
FT DISULFID 90
FT /note="Interchain (with C-86 in BotLVP1 chain alpha)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 95 AA; 10386 MW; EA0121562139A0B6 CRC64;
MISVQVIFIA FISIIAFSMV CGGNVFPNRE LGILYGCKGY GNAFCDKVCK MHLARGGGRC
GEPNPVMWAC ECIDIDEDNG YFLNALEKQC PLLKG
