LV1A_BUTOC
ID LV1A_BUTOC Reviewed; 91 AA.
AC P84810;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Lipolysis-activating peptide 1-alpha chain;
DE Short=BotLVP1-alpha;
DE Short=LVP1-alpha;
DE Contains:
DE RecName: Full=Neurotoxin BmKBTx-like;
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 23-66 AND 73-87, 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 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 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:0000305|PubMed:15680238}.
CC -!- SUBUNIT: Monomer (edited version) and heterodimer (non-edited version)
CC of this alpha chain and a beta chain (AC P84809).
CC {ECO:0000269|PubMed:15680238}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15680238}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15680238}.
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=79 {ECO:0000250}; Note=The stop codon
CC (UGA) at position 79 is created by RNA editing. {ECO:0000250};
CC -!- MASS SPECTROMETRY: [Lipolysis-activating peptide 1-alpha chain]:
CC Mass=8807; Method=MALDI; 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; P84810; -.
DR SMR; P84810; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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 GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:UniProtKB.
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 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..91
FT /note="Lipolysis-activating peptide 1-alpha chain"
FT /id="PRO_0000232422"
FT CHAIN 23..78
FT /note="Neurotoxin BmKBTx-like"
FT /evidence="ECO:0000250"
FT /id="PRO_0000394866"
FT DOMAIN 24..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-90 in BotLVP1 chain beta)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 91 AA; 10457 MW; E337BF3BBA292C90 CRC64;
MMKLVLFGII VILFSLIGSI HGISGNYPLN PYGGYYYCTI LGENEYCKKI CRIHGVRYGY
CYDSACWCET LKDEDVSVWN AVKKHCKNPY L
