LV1A_MESMA
ID LV1A_MESMA Reviewed; 98 AA.
AC Q6WJF5; A1YAC8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Lipolysis-activating peptide 1-alpha chain;
DE Short=BmLVP1-alpha;
DE Short=LVP1-alpha;
DE Contains:
DE RecName: Full=Neurotoxin BmKBTx;
DE Short=BmKBT;
DE Flags: Precursor;
GN Name=LVP1a;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AMIDATION AT ASN-96, AND RNA
RP EDITING.
RX PubMed=17141763; DOI=10.1016/j.febslet.2006.11.040;
RA Zhu S., Gao B.;
RT "Molecular characterization of a new scorpion venom lipolysis activating
RT peptide: evidence for disulfide bridge-mediated functional switch of
RT peptides.";
RL FEBS Lett. 580:6825-6836(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16513212; DOI=10.1016/j.peptides.2006.01.012;
RA Zeng X.-C., Luo F., Li W.-X.;
RT "Molecular dissection of venom from Chinese scorpion Mesobuthus martensii:
RT identification and characterization of four novel disulfide-bridged venom
RT peptides.";
RL Peptides 27:1745-1754(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Jiang D.-H., Cao Z., Li W.-X.;
RT "Cloning and characterizing of a new scorpion toxin from Buthus martensii
RT Karsch.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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, similar to beta-toxins, may modulate
CC voltage-gated sodium channels (Nav) and may block voltage-gated
CC potassium channels (Kv) (Probable). Seems to be a rare component in the
CC venom. {ECO:0000250|UniProtKB:P84810}.
CC -!- SUBUNIT: Monomer (edited version) and heterodimer (non-edited version)
CC of this alpha chain and a beta chain (AC Q95P90).
CC {ECO:0000250|UniProtKB:P84810}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16513212,
CC ECO:0000305|PubMed:17141763}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:16513212, ECO:0000305|PubMed:17141763}.
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=81 {ECO:0000269|PubMed:17141763};
CC Note=The stop codon (UGA) at position 81 is created by RNA editing.;
CC -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC {ECO:0000305}.
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DR EMBL; DQ872673; ABJ09777.1; -; Genomic_DNA.
DR EMBL; AF151798; AAP41418.2; -; mRNA.
DR EMBL; AY282464; AAQ22733.1; -; mRNA.
DR AlphaFoldDB; Q6WJF5; -.
DR SMR; Q6WJF5; -.
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 1: Evidence at protein level;
KW Amidation; 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..22
FT /evidence="ECO:0000250"
FT CHAIN 23..96
FT /note="Lipolysis-activating peptide 1-alpha chain"
FT /id="PRO_0000394865"
FT CHAIN 23..80
FT /note="Neurotoxin BmKBTx"
FT /id="PRO_0000234389"
FT DOMAIN 26..89
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT SITE 43
FT /note="Important for inhibiting sodium channels, in non-
FT edited version"
FT /evidence="ECO:0000250"
FT SITE 46
FT /note="Important for inhibiting sodium channels, in non-
FT edited version"
FT /evidence="ECO:0000250"
FT SITE 48
FT /note="Important for blocking potassium channels, in non-
FT edited version"
FT /evidence="ECO:0000250"
FT SITE 51
FT /note="Important for blocking potassium channels, in non-
FT edited version"
FT /evidence="ECO:0000250"
FT SITE 62
FT /note="Important for inhibiting sodium channels, in non-
FT edited version"
FT /evidence="ECO:0000250"
FT SITE 64
FT /note="Important for inhibiting sodium channels, in non-
FT edited version"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="Asparagine amide"
FT /evidence="ECO:0000305|PubMed:17141763"
FT DISULFID 40..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 49..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 53..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 88
FT /note="Interchain (with C-90 in BmLVP1 chain beta, in non-
FT edited version)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="V -> L (in Ref. 2; AAP41418)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="I -> F (in Ref. 2; AAP41418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 98 AA; 11329 MW; 3904E84539EF9367 CRC64;
MMKFVLFGMI VILFSLMGSI RGDDDPGNYP TNAYGNKYYC TILGENEYCR KICKLHGVTY
GYCYNSRCWC EKLEDKDVTI WNAVKNHCTN TILYPNGK
