ID   LV1B1_LYCMC             Reviewed;          94 AA.
AC   D9U2A2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Lipolysis-activating peptide 1-beta chain;
DE            Short=LVP1-beta;
DE   AltName: Full=Neurotoxin LmNaTx19;
DE   Flags: Precursor;
OS   Lychas mucronatus (Chinese swimming scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Lychas.
OX   NCBI_TaxID=172552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hainan; TISSUE=Venom gland;
RX   PubMed=20663230; DOI=10.1186/1471-2164-11-452;
RA   Zhao R., Ma Y., He Y., Di Z., Wu Y.-L., Cao Z.-J., Li W.-X.;
RT   "Comparative venom gland transcriptome analysis of the scorpion Lychas
RT   mucronatus reveals intraspecific toxic gene diversity and new venomous
RT   components.";
RL   BMC Genomics 11:452-452(2010).
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 D9U299 or AC D9U2A4) and this beta
CC       chain (non-edited version). {ECO:0000250|UniProtKB:Q95P90}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q95P90}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20663230}.
CC   -!- RNA EDITING: Modified_positions=31 {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-86, 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; EU159294; ABX76767.1; -; mRNA.
DR   AlphaFoldDB; D9U2A2; -.
DR   SMR; D9U2A2; -.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..94
FT                   /note="Lipolysis-activating peptide 1-beta chain"
FT                   /id="PRO_0000403882"
FT   DISULFID        34..56
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        86
FT                   /note="Interchain (with C-86 (AC D9U299) or C-87 (AC
FT                   D9U2A4) in LVP1 chain alpha)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   94 AA;  10464 MW;  FD84DE34E6356A6B CRC64;
     MKILAVVLIS VIVLNTANGE NYYPQKYTND YYGCQKQTDA FCDKVCKLHL ADSGFCDQSW
     GLAKACKCVN VSYDNSFFFN ALESQCPLLN KSAA