3NO52_BUNMU
ID 3NO52_BUNMU Reviewed; 89 AA.
AC Q9YGH9;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Long neurotoxin homolog NTL2;
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=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).
CC -!- FUNCTION: Exhibits M2 muscarinic acetylcholine receptor (CHRM2)-
CC blocking activity, but has a weak binding activity toward nicotinic
CC AChR. Moreover, it inhibits collagen-induced platelet aggregation.
CC {ECO:0000250|UniProtKB:Q9YGJ0}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9YGJ0}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC subfamily. Orphan group V sub-subfamily. {ECO:0000305}.
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DR EMBL; AJ223251; CAA11214.1; -; mRNA.
DR AlphaFoldDB; Q9YGH9; -.
DR SMR; Q9YGH9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR035076; Toxin/TOLIP.
DR Pfam; PF00087; Toxin_TOLIP; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 3: Inferred from homology;
KW Cell adhesion impairing toxin; Disulfide bond;
KW G-protein coupled acetylcholine receptor impairing toxin;
KW G-protein coupled receptor impairing toxin; Hemostasis impairing toxin;
KW Neurotoxin; Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT CHAIN 22..89
FT /note="Long neurotoxin homolog NTL2"
FT /id="PRO_0000035427"
FT MOTIF 54..56
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00293"
FT DISULFID 24..45
FT /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT DISULFID 27..32
FT /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT DISULFID 38..66
FT /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT DISULFID 70..81
FT /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
FT DISULFID 82..87
FT /evidence="ECO:0000250|UniProtKB:Q9YGJ0"
SQ SEQUENCE 89 AA; 9873 MW; 545E79D2EA56E2E5 CRC64;
MKTLLLSLVV VIIVCLDLGY TMQCKTCSFY TCPNSETCPD GKNICVKRSW TAVRGDGPKR
EIRRECAATC PPSKLGLTVF CCTTDNCYH