ID   LVPAY_LYCMC             Reviewed;          83 AA.
AC   P0CI44;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Lipolysis-activating peptide 1-alpha chain;
DE            Short=LVP1-alpha;
DE   Contains:
DE     RecName: Full=Neurotoxin BmKBTx-like;
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=Yunnan; 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 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:P84810}.
CC   -!- FUNCTION: The edited BmKBTx-like, similar to beta-toxins, may modulate
CC       voltage-gated sodium channels (Nav) and may block voltage-gated
CC       potassium channels (Kv). {ECO:0000250|UniProtKB:P84810}.
CC   -!- SUBUNIT: Monomer (edited version) and heterodimer (non-edited version)
CC       of this alpha chain and a beta chain (AC P0CI43).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20663230}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20663230}.
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   -!- RNA EDITING: Modified_positions=76 {ECO:0000250}; Note=The stop codon
CC       (UGA) at position 76 is created by RNA editing. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC       {ECO:0000305}.
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DR   EMBL; GT028572; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0CI44; -.
DR   SMR; P0CI44; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
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   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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..83
FT                   /note="Lipolysis-activating peptide 1-alpha chain"
FT                   /id="PRO_0000403883"
FT   CHAIN           22..75
FT                   /note="Neurotoxin BmKBTx-like"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000403884"
FT   DOMAIN          22..83
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        44..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        48..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        83
FT                   /note="Interchain (with C-86 in LVP1 chain beta)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   83 AA;  9711 MW;  EA8452FB0F63B4FA CRC64;
     MNIILFYFMP ILISLPGLLA SGTYPNDVYG LTYDCGKLGE NEHCLKICKI HGVEYGYCYG
     WRCWCDKLSD KNKLFWDVYK EHC