3NO24_OPHHA
ID 3NO24_OPHHA Reviewed; 86 AA.
AC Q2VBN2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Weak neurotoxin WNTX34;
DE Flags: Precursor;
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16689684; DOI=10.1042/bj20060004;
RA Li J., Zhang H., Liu J., Xu K.;
RT "Novel genes encoding six kinds of three-finger toxins in Ophiophagus
RT hannah (king cobra) and function characterization of two recombinant long-
RT chain neurotoxins.";
RL Biochem. J. 398:233-242(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Binds with low affinity to muscular (alpha-1-beta-1-delta-
CC epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal
CC (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR).
CC {ECO:0000250|UniProtKB:O42255}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24297900}.
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 II sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ273583; ABB83637.1; -; mRNA.
DR AlphaFoldDB; Q2VBN2; -.
DR SMR; Q2VBN2; -.
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 SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..86
FT /note="Weak neurotoxin WNTX34"
FT /id="PRO_5000006493"
FT DISULFID 24..45
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 27..32
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 38..63
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 67..78
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 79..84
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
SQ SEQUENCE 86 AA; 9815 MW; 1C190977139D63EA CRC64;
MKTLLLTLVV VTIVCLDLGY SLTCLNCPEQ YCKRIHTCRN GENVCFKRFY EGKLLCKQFR
RGCAATCPEA KSREIVQCCS TDECNH
