LV1A_BUTOS
ID LV1A_BUTOS Reviewed; 98 AA.
AC B8XH01; B8XGZ7; B8XGZ9; B8XH00; B8XH03;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Lipolysis-activating peptide 1-alpha chain;
DE Short=BoiLVP1-alpha;
DE Short=LVP1-alpha;
DE AltName: Full=Putative beta-like toxin Tx458;
DE Short=BoiTx458;
DE AltName: Full=Putative beta-like toxin Tx651;
DE Short=BoiTx651;
DE AltName: Full=Putative beta-like toxin Tx764;
DE Short=BoiTx764;
DE AltName: Full=Putative beta-like toxin Tx814;
DE Short=BoiTx814;
DE Contains:
DE RecName: Full=Neurotoxin BmKBTx-like;
DE AltName: Full=Putative excitatory toxin Tx135;
DE Short=BoiTx135;
DE Flags: Precursor;
OS Buthus occitanus israelis (Common yellow scorpion) (Buthus israelis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX NCBI_TaxID=539894;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RA Zilberberg N., Kozminsky-Atias A.;
RT "Buthus occitanus israelis scorpion toxin.";
RL Submitted (OCT-2008) 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-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 B8XGZ8).
CC {ECO:0000250|UniProtKB:P84810}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84810}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000250|UniProtKB:P84810}.
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|Ref.1}; Note=The stop
CC codon (UGA) at position 81 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; FJ360790; ACJ23110.1; -; mRNA.
DR EMBL; FJ360786; ACJ23106.1; -; mRNA.
DR EMBL; FJ360788; ACJ23108.1; -; mRNA.
DR EMBL; FJ360789; ACJ23109.1; -; mRNA.
DR EMBL; FJ360792; ACJ23112.1; -; mRNA.
DR AlphaFoldDB; B8XH01; -.
DR SMR; B8XH01; -.
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 2: Evidence at transcript 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_0000394867"
FT CHAIN 23..80
FT /note="Neurotoxin BmKBTx-like"
FT /id="PRO_0000394868"
FT DOMAIN 26..89
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 96
FT /note="Lysine amide"
FT /evidence="ECO:0000250|UniProtKB:Q6WJF5"
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 BotLVP1 chain beta)"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="M -> I (in Ref. 1; ACJ23106)"
FT /evidence="ECO:0000305"
FT CONFLICT 2
FT /note="M -> T (in Ref. 1; ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="L -> I (in Ref. 1; ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="I -> V (in Ref. 1; ACJ23106)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="H -> L (in Ref. 1; ACJ23108/ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 23..25
FT /note="SDP -> TEA (in Ref. 1; ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="S -> Y (in Ref. 1; ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="T -> V (in Ref. 1; ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="A -> V (in Ref. 1; ACJ23106)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="T -> R (in Ref. 1; ACJ23106/ACJ23108/ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="I -> A (in Ref. 1; ACJ23108)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="I -> M (in Ref. 1; ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> E (in Ref. 1; ACJ23106/ACJ23108/ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> V (in Ref. 1; ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="I -> V (in Ref. 1; ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="V -> A (in Ref. 1; ACJ23106)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="V -> L (in Ref. 1; ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..59
FT /note="VQ -> GH (in Ref. 1; ACJ23108/ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="Q -> K (in Ref. 1; ACJ23106/ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="E -> K (in Ref. 1; ACJ23106)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="E -> D (in Ref. 1; ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="E -> K (in Ref. 1; ACJ23108/ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="V -> I (in Ref. 1; ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="N -> S (in Ref. 1; ACJ23106/ACJ23108/ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="D -> N (in Ref. 1; ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="A -> T (in Ref. 1; ACJ23108)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="R -> H (in Ref. 1; ACJ23108/ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="R -> N (in Ref. 1; ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="H -> Y (in Ref. 1; ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="K -> N (in Ref. 1; ACJ23108/ACJ23109)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="K -> T (in Ref. 1; ACJ23112)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..96
FT /note="LYPK -> VYSQ (in Ref. 1; ACJ23109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 98 AA; 11247 MW; C2E05BCAC06B4271 CRC64;
MMKLVLFGII VILFSMIGSI HGSDPPGNYP LNTYGNKYAC TILGENDFCQ KICKVHGVQY
GYCFNSRCWC EYLEEKDVNI WDAVKRHCKN TILYPKGK
