3L22_DEMVE
ID 3L22_DEMVE Reviewed; 88 AA.
AC A6MFK5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Long neurotoxin LNTX-2;
DE Flags: Precursor;
OS Demansia vestigiata (Lesser black whip snake) (Demansia atra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Demansia.
OX NCBI_TaxID=412038;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-45, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17608513; DOI=10.1021/pr0701613;
RA St Pierre L., Birrell G.W., Earl S.T.H., Wallis T.P., Gorman J.J.,
RA de Jersey J., Masci P.P., Lavin M.F.;
RT "Diversity of toxic components from the venom of the evolutionarily
RT distinct black whip snake, Demansia vestigiata.";
RL J. Proteome Res. 6:3093-3107(2007).
CC -!- FUNCTION: Binds with high affinity to muscular nicotinic acetylcholine
CC receptors (nAChRs), whereas it binds with a low affinity to neuronal
CC alpha-7/CHRNA7 nAChRs. {ECO:0000250|UniProtKB:P0C8R6}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17608513}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MISCELLANEOUS: Has the length of long neurotoxins, but only 4 disulfide
CC bonds, as short neurotoxins.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ917516; ABK63545.1; -; mRNA.
DR AlphaFoldDB; A6MFK5; -.
DR SMR; A6MFK5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00206; snake_toxin; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR Pfam; PF00021; UPAR_LY6; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..88
FT /note="Long neurotoxin LNTX-2"
FT /id="PRO_5000254109"
FT DISULFID 24..42
FT /evidence="ECO:0000250"
FT DISULFID 35..63
FT /evidence="ECO:0000250"
FT DISULFID 67..78
FT /evidence="ECO:0000250"
FT DISULFID 79..84
FT /evidence="ECO:0000250"
SQ SEQUENCE 88 AA; 9758 MW; 3762D7524AACAC69 CRC64;
MKTLLLTLVV VTIVCLDFGY ARTCLKTPEV KSEPCPPGQE VCYTKAWRDR MCSFRGKVIE
LGCAATCPRQ EPGKEITCCS TDDCNTHP