3SI35_OPHHA
ID 3SI35_OPHHA Reviewed; 86 AA.
AC Q53B49;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Short neurotoxin OH-35;
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=15302536; DOI=10.1016/j.toxicon.2004.06.003;
RA He Y.-Y., Lee W.-H., Zhang Y.;
RT "Cloning and purification of alpha-neurotoxins from king cobra (Ophiophagus
RT hannah).";
RL Toxicon 44:295-303(2004).
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 to the muscarinic acetylcholine receptor (CHRM).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24297900}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC residue stands at position 54 (Pro-31 in standard classification).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Aminergic toxin sub-subfamily. {ECO:0000305}.
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DR EMBL; AY596937; AAT97259.1; -; mRNA.
DR AlphaFoldDB; Q53B49; -.
DR SMR; Q53B49; -.
DR TopDownProteomics; Q53B49; -.
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; 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 Disulfide bond; G-protein coupled acetylcholine receptor impairing toxin;
KW G-protein coupled receptor impairing toxin; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..86
FT /note="Short neurotoxin OH-35"
FT /id="PRO_5000093329"
FT DISULFID 24..45
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 38..63
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 67..78
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 79..84
FT /evidence="ECO:0000250|UniProtKB:P60301"
SQ SEQUENCE 86 AA; 9564 MW; 5B5F14392F3C959F CRC64;
MKTLLLTLVV VTIVCLDLGH TLICVKQYTI FGVTPEICAD GQNLCYKTWH MVYPGGYDHT
RGCAATCPKM KNHDTVHCCT TDKCNL