ID   LVPAH_LYCMC             Reviewed;          91 AA.
AC   D9U299;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Lipolysis-activating peptide 1-alpha chain;
DE            Short=LVP1-alpha;
DE   AltName: Full=Neurotoxin LmNaTx7;
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 heterodimer LVP1 induces lipolysis in rat adipocytes.
CC       Induction of lipolysis by LVP1 appears to be mediated through the beta-
CC       2 adrenergic receptor pathway (ADRB2) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of this alpha chain and a beta chain (AC D9U2A2).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC       {ECO:0000305}.
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DR   EMBL; EU159282; ABX76755.1; -; mRNA.
DR   AlphaFoldDB; D9U299; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
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   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; G-protein coupled receptor impairing toxin;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..91
FT                   /note="Lipolysis-activating peptide 1-alpha chain"
FT                   /id="PRO_0000403879"
FT   DOMAIN          23..87
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        38..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        47..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        51..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        86
FT                   /note="Interchain (with C-86 in LVP1 chain beta)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   91 AA;  10467 MW;  EA6DE6152ED48B9D CRC64;
     MNIKLFCFLS ILISLTGLSL SGDDGNYPID ANGNRYSCGK LGENEFCLKV CKLHGVKRGY
     CYFFKCYCEL LKDKDIQFFD AYKTYCKNSR I