3NO4H_BUNMU
ID 3NO4H_BUNMU Reviewed; 87 AA.
AC P15818; Q9YGI9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Long neurotoxin homolog {ECO:0000305};
DE AltName: Full=BM10-1 {ECO:0000303|PubMed:14559085};
DE Flags: Precursor;
OS Bungarus multicinctus (Many-banded krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=2315016; DOI=10.1093/nar/18.4.1045;
RA Danse J.-M., Garnier J.-M., Kempf J.;
RT "A cDNA sequence encoding a neurotoxin-homolog from Bungarus
RT multicinctus.";
RL Nucleic Acids Res. 18:1045-1045(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=9844743; DOI=10.1080/15216549800204362;
RA Qian Y.-C., Fan C.-Y., Gong Y., Yang S.-L.;
RT "cDNA cloning and sequence analysis of six neurotoxin-like proteins from
RT Chinese continental banded krait.";
RL Biochem. Mol. Biol. Int. 46:821-828(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-87, FUNCTION,
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver, and Venom;
RX PubMed=14559085; DOI=10.1016/s0041-0101(03)00151-x;
RA Chang L.-S., Chung C., Liou J.-C., Chang C.-W., Yang C.-C.;
RT "Novel neurotoxins from Taiwan banded krait (Bungarus multicinctus) venom:
RT purification, characterization and gene organization.";
RL Toxicon 42:323-330(2003).
CC -!- FUNCTION: Inhibits carbachol-induced muscle contraction in a reversible
CC manner. {ECO:0000269|PubMed:14559085}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14559085}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=7357; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:14559085};
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC subfamily. Orphan group IV sub-subfamily. {ECO:0000305}.
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DR EMBL; X51414; CAA35776.1; -; mRNA.
DR EMBL; AJ006136; CAA06886.1; -; mRNA.
DR EMBL; AJ515363; CAD56380.1; -; Genomic_DNA.
DR PIR; S08401; S08401.
DR AlphaFoldDB; P15818; -.
DR BMRB; P15818; -.
DR SMR; P15818; -.
DR PRIDE; P15818; -.
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; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR InterPro; IPR035076; Toxin/TOLIP.
DR Pfam; PF00087; Toxin_TOLIP; 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:0000269|PubMed:14559085"
FT CHAIN 22..87
FT /note="Long neurotoxin homolog"
FT /evidence="ECO:0000269|PubMed:14559085"
FT /id="PRO_0000035416"
FT DISULFID 24..47
FT /evidence="ECO:0000250|UniProtKB:P81782"
FT DISULFID 27..32
FT /evidence="ECO:0000250|UniProtKB:P81782"
FT DISULFID 40..64
FT /evidence="ECO:0000250|UniProtKB:P81782"
FT DISULFID 68..80
FT /evidence="ECO:0000250|UniProtKB:P81782"
FT DISULFID 81..86
FT /evidence="ECO:0000250|UniProtKB:P81782"
FT CONFLICT 77
FT /note="Y -> D (in Ref. 2; CAA06886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 87 AA; 9658 MW; 57D07EC1223B4B55 CRC64;
MKTLLLTLVV VTIVCLDLGY TMKCKICHFD TCRAGELKVC ASGEKYCFKE SWREARGTRI
ERGCAATCPK GSVYGLYVLC CTTDDCN